sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5W059 and applied mutation signature R195A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer 0.1 M HEPES

column_label: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'R195A'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 2890; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 11.5; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 3.98 x 10^3.

normalized_value_unit_evidence: Km: printed cell 2890 uM; 2890 / 1000 = 2.89 mM. kcat: printed cell 11.5 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 3.98 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.98 x 10^3 / 1000 = 3.98 s^-1 mM^-1. The exact quotient of the two printed component cells is 11.5 / 2.89 = 3.979238754325259 s^-1 mM^-1, and the printed efficiency cell reproduces that quotient at its own printed precision of three significant figures.

raw_value_unit_evidence: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'R195A', the '+ 2 mM Pi' block: Km cell 2890 under column head 'Km (uM)'; kcat cell 11.5 under column head 'kcat (s-1)'; catalytic efficiency cell 3.98 x 10^3 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 11.5 ± 0.67 s^-1, Km 2890 ± 210 uM, kcat/Km (3.98 ± 0.37) x 10^3 M^-1 s^-1.

row_label: Table 3, enzyme line 'R195A', the three '+ 2 mM Pi' kinetic columns


organism: Pseudomonas putida

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB:A5W059 canonical sequence plus selected-record T145A mutation signature and applied mutation signature T145A to reconstruct the assayed variant sequence.

mutation_type: substitution

proof_lines: mutant enzyme T145A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme T145A, in the absence of phosphate, at pH 8.0 and 25°C

source: brenda


mutation_signature: Unknown

sequence_source: UniProtKB:A5W059 FASTA/JSON direct lookup 2026-06-04

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines: wild type enzyme, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: wild type enzyme, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


source_db: oed

verification_status: verified

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5W059 and applied mutation signature R40A to reconstruct the assayed variant sequence.

column_label: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'R40A'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 3260; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 36.6; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 1.12 x 10^4.

normalized_value_unit_evidence: Km: printed cell 3260 uM; 3260 / 1000 = 3.26 mM. kcat: printed cell 36.6 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 1.12 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.12 x 10^4 / 1000 = 11.2 s^-1 mM^-1. The exact quotient of the two printed component cells is 36.6 / 3.26 = 11.226993865030677 s^-1 mM^-1, and the printed efficiency cell reproduces that quotient at its own printed precision of three significant figures.

raw_value_unit_evidence: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'R40A', the '+ 2 mM Pi' block: Km cell 3260 under column head 'Km (uM)'; kcat cell 36.6 under column head 'kcat (s-1)'; catalytic efficiency cell 1.12 x 10^4 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 36.6 ± 1.0 s^-1, Km 3260 ± 340 uM, kcat/Km (1.12 ± 0.12) x 10^4 M^-1 s^-1.

row_label: Table 3, enzyme line 'R40A', the three '+ 2 mM Pi' kinetic columns

data_origin: experimental

status: verified

source: oed


verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5W059 and applied mutation signature N71A to reconstruct the assayed variant sequence.

column_label: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'N71A'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 1110; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 0.0184; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 16.5.

normalized_value_unit_evidence: Km: printed cell 1110 uM; 1110 / 1000 = 1.11 mM. kcat: printed cell 0.0184 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 16.5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 16.5 / 1000 = 0.0165 s^-1 mM^-1. That printed cell is the paper's own independently fitted catalytic efficiency, and it is the value this record carries for kcat_over_km.

raw_value_unit_evidence: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'N71A', the '+ 2 mM Pi' block: Km cell 1110 under column head 'Km (uM)'; kcat cell 0.0184 under column head 'kcat (s-1)'; catalytic efficiency cell 16.5 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 0.0184 ± 0.00034 s^-1, Km 1110 ± 82.7 uM, kcat/Km 16.5 ± 1.3 M^-1 s^-1.

row_label: Table 3, enzyme line 'N71A', the three '+ 2 mM Pi' kinetic columns

status: corrected


enzyme_display_name: biuret amidohydrolase

organism: Rhizobium leguminosarum bv. viciae

substrate_name: Biuret

verification_status: unverified

sequence_variant_note: Resolved canonical sequence from UniProtKB Q1M7F4 direct FASTA/JSON lookup; K142A reconstructed from the canonical sequence after confirming residue 142 is K. and applied mutation signature K142A to reconstruct the assayed variant sequence.

smiles: NC(=O)NC(N)=O

enzyme: biuret amidohydrolase

substrate: Biuret

status: unverified


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1M7F4 direct FASTA/JSON lookup; F41W reconstructed from the canonical sequence after confirming residue 41 is F. and applied mutation signature F41W to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q1M7F4 direct FASTA/JSON lookup; K142A reconstructed from the canonical sequence after confirming residue 142 is K.


sequence_source: UniProtKB Q1M7F4 direct FASTA/JSON lookup; F41W reconstructed from the canonical sequence after confirming residue 41 is F.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1M7F4 direct FASTA/JSON lookup; Q215A reconstructed from the canonical sequence after confirming residue 215 is Q. and applied mutation signature Q215A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1M7F4 direct FASTA/JSON lookup; Q215N reconstructed from the canonical sequence after confirming residue 215 is Q. and applied mutation signature Q215N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q1M7F4 direct FASTA/JSON lookup.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q1M7F4 direct FASTA/JSON lookup; Q215E reconstructed from the canonical sequence after confirming residue 215 is Q. and applied mutation signature Q215E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04 and applied mutation signature F41A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04 and applied mutation signature Q215E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04 and applied mutation signature F41Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04 and applied mutation signature Q215N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q1M7F4 direct FASTA/API check on 2026-06-04 and applied mutation signature F41L to reconstruct the assayed variant sequence.


enzyme_display_name: N(1)-aminopropylagmatine synthase

organism: Thermus thermophilus

substrate_name: Agmatine; S-Adenosylmethioninamine

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org); CC BY-NC-ND 4.0

sequence_source: UniProtKB reviewed accession Q5SK28 direct FASTA/REST lookup on 2026-06-04.

proof_lines:
pH 9.0, 37°C
Raw SKiD Env: Temp=37°C, pH=9

source_databases_merged: sabio_rk brenda skid

enzyme: N(1)-aminopropylagmatine synthase

substrate: Agmatine; S-Adenosylmethioninamine


substrate_name: agmatine

smiles: N=C(N)NCCCCN

substrate: agmatine


substrate_name: spermidine

smiles: NCCCCNCCCN

substrate: spermidine


substrate_name: norspermidine

smiles: NCCCNCCCN

substrate: norspermidine


smiles: NCCCN(CCCN)CCCN


substrate_name: S-adenosyl 3-(methylthio)propylamine

substrate: S-adenosyl 3-(methylthio)propylamine


enzyme_display_name: 8-oxo-dGTP diphosphatase

organism: Homo sapiens

kcat_display: Not reported

source_license: CC BY 4.0; CC BY-NC-ND 4.0

sequence_source: UniProtKB reviewed accession P36639 direct FASTA/REST lookup on 2026-06-04.

assay_conditions_summary: pH 8; 310.15 K; buffer Tris-HCl

proof_lines:
in Tris-HCl buffer (pH 8.0), at 37°C
Raw SKiD Env: Temp=37°C, pH=8

source_databases_merged: brenda skid

enzyme: 8-oxo-dGTP diphosphatase


organism: Saccharomyces cerevisiae

substrate_name: Coenzyme A

sequence_source: UniProtKB reviewed accession Q12524 direct FASTA/REST lookup on 2026-06-04.

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

substrate: Coenzyme A


organism: Pyrococcus furiosus

sequence_source: UniProtKB direct REST lookup for Q8U4G1

proof_lines:
pH 7.4, 70°C
Raw SKiD Env: Temp=70°C, pH=7.4


substrate_name: putrescine

smiles: NCCCCN

substrate: putrescine


smiles: NCCCN


column_label: Table 5 (Kinetic parameters of ACAPT from P. furiosus), row 'Agmatine'; column 'Km (uM)' = 7.6; column 'kcat (s^-1)' = 0.10; column 'kcat/Km (M^-1 s^-1) (x10^2)' = 134 (i.e. 134 x 10^2 = 13,400 M^-1 s^-1).

normalized_value_unit_evidence: kcat: printed cell 0.10 s^-1; already in s^-1, no unit change applies; the exported value is 0.1 s^(-1), an exact match. Km: printed cell 7.6 uM = 0.0076 mM at full printed precision; the exported value 0.008 mM is that same printed cell at the export's own coarser reporting precision. kcat/Km: the printed column cell is 134 x 10^2 M^-1 s^-1 = 13,400 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 13,400 / 1000 = 13.4 s^-1 mM^-1 exactly. This is the paper's own independently printed efficiency cell for the row, not a quotient recomputed from Km and kcat, and it is proposed as the corrected value in place of the exported 12.5 s^-1 mM^-1.

raw_value_unit_evidence: Table 5, row Agmatine: Km = 7.6 uM; kcat = 0.10 s^-1; printed kcat/Km column value = 134, with the column head noting a shared x10^2 scale, i.e. 134 x 10^2 = 13,400 M^-1 s^-1.

row_label: Table 5, row Agmatine

table_label: Table 5: Kinetic parameters of ACAPT from P. furiosus (J Bacteriol 2007, 189(16):6057-6067)


organism: Thermococcus kodakarensis

sequence_source: UniProtKB direct REST lookup for Q5JFG9


substrate_name: cadaverine

smiles: NCCCCCN

substrate: cadaverine


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct REST/FASTA lookup and applied mutation signature H75A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct REST/FASTA lookup and applied mutation signature K147A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K147A, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme K147A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct REST/FASTA lookup and applied mutation signature G144V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme G144V, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme G144V, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


sequence_source: UniProtKB A5W059 direct REST/FASTA lookup


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5W059 and applied mutation signature T145A to reconstruct the assayed variant sequence.

column_label: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'T145A'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 1780; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 10.7; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 6.01 x 10^3.

normalized_value_unit_evidence: Km: printed cell 1780 uM; 1780 / 1000 = 1.78 mM. kcat: printed cell 10.7 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 6.01 x 10^3 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 6.01 x 10^3 / 1000 = 6.01 s^-1 mM^-1. The exact quotient of the two printed component cells is 10.7 / 1.78 = 6.011235955056179 s^-1 mM^-1, and the printed efficiency cell reproduces that quotient at its own printed precision of three significant figures.

raw_value_unit_evidence: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'T145A', the '+ 2 mM Pi' block: Km cell 1780 under column head 'Km (uM)'; kcat cell 10.7 under column head 'kcat (s-1)'; catalytic efficiency cell 6.01 x 10^3 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 10.7 ± 0.33 s^-1, Km 1780 ± 210 uM, kcat/Km (6.01 ± 0.73) x 10^3 M^-1 s^-1.

row_label: Table 3, enzyme line 'T145A', the three '+ 2 mM Pi' kinetic columns


proof_lines: mutant enzyme H75A, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme H75A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

column_label: Table 1. Pi activation with different substrates. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'CHA + 2 mM Pi'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 104; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 145; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 1.40 x 10^6. The 'Ksi (mM)' column prints ND for this line.

normalized_value_unit_evidence: Km: printed cell 104 uM; 104 / 1000 = 0.104 mM. kcat: printed cell 145 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 1.40 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.40 x 10^6 / 1000 = 1400.0 s^-1 mM^-1. That printed cell is the paper's own independently fitted catalytic efficiency, and it is the value this record carries for kcat_over_km.

raw_value_unit_evidence: Table 1. Pi activation with different substrates. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'CHA + 2 mM Pi', the '+ 2 mM Pi' block: Km cell 104 under column head 'Km (uM)'; kcat cell 145 under column head 'kcat (s-1)'; catalytic efficiency cell 1.40 x 10^6 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 145 ± 1.3 s^-1, Km 104 ± 9.9 uM, kcat/Km (1.40 ± 0.13) x 10^6 M^-1 s^-1.

row_label: Table 1, substrate line 'CHA', the three '+ 2 mM Pi' kinetic columns


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct REST/FASTA lookup and applied mutation signature R40A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R40A, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme R40A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


enzyme_display_name: lactaldehyde dehydrogenase

organism: Escherichia coli

substrate_name: (S)-lactaldehyde

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P25553 direct lookup; N286H reconstructed on 2026-06-04 and applied mutation signature N286H to reconstruct the assayed variant sequence.

enzyme: lactaldehyde dehydrogenase

substrate: (S)-lactaldehyde


sequence_source: UniProtKB reviewed P25553 direct lookup on 2026-06-04


sequence_source: UniProtKB reviewed P25553 direct lookup; N286H reconstructed on 2026-06-04


substrate_name: NAD+; H2O; L-Glyceraldehyde

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org); CC BY-NC-ND 4.0

assay_conditions_summary: pH 7; 310.15 K; cofactor NAD+

substrate: NAD+; H2O; L-Glyceraldehyde


organism: Methanocaldococcus jannaschii

substrate_name: H2O; NAD+; Lactaldehyde

source_license: CC BY 4.0; SABIO-RK terms (free for academic use; see sabiork.h-its.org)

sequence_source: UniProtKB reviewed Q58806 direct lookup on 2026-06-04

assay_conditions_summary: pH 7.5; cofactor NAD+

substrate: H2O; NAD+; Lactaldehyde


substrate_name: Lactaldehyde

smiles: CC(O)C=O

substrate: Lactaldehyde


substrate_name: propanal

smiles: CCC=O

substrate: propanal


enzyme_display_name: L-fuculose-phosphate aldolase

substrate_name: L-Fuculose 1-phosphate

source_license: SABIO-RK terms (free for academic use; see sabiork.h-its.org)

sequence_source: UniProtKB P0AB87 direct lookup, canonical context only

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant Del(207-215)

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant Del(211-215)

enzyme: L-fuculose-phosphate aldolase

substrate: L-Fuculose 1-phosphate


km_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 direct lookup plus explicit mutation reconstruction and applied mutation signature E214D/K207A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 direct lookup plus explicit mutation reconstruction and applied mutation signature E214L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant E214L


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 direct lookup plus explicit mutation reconstruction and applied mutation signature K207A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant K207A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A5W059 and applied mutation signature G144V to reconstruct the assayed variant sequence.

column_label: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556); enzyme line 'G144V'; column head 'Km (uM)' under the '+ 2 mM Pi' block = 6830; column head 'kcat (s-1)' under the '+ 2 mM Pi' block = 0.394; column head 'kcat/Km (M-1s-1)' under the '+ 2 mM Pi' block = 57.7.

normalized_value_unit_evidence: Km: printed cell 6830 uM; 6830 / 1000 = 6.83 mM. kcat: printed cell 0.394 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed cell 57.7 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 57.7 / 1000 = 0.0577 s^-1 mM^-1. The exact quotient of the two printed component cells is 0.394 / 6.83 = 0.057686676427525625 s^-1 mM^-1, and the printed efficiency cell reproduces that quotient at its own printed precision of three significant figures.

raw_value_unit_evidence: Table 3. Steady state kinetic parameters of HMG lyase activity of variants of the HMG/CHA aldolase in the presence or absence of the Pi. (PLoS ONE 2016, 11(10): e0164556) enzyme line 'G144V', the '+ 2 mM Pi' block: Km cell 6830 under column head 'Km (uM)'; kcat cell 0.394 under column head 'kcat (s-1)'; catalytic efficiency cell 57.7 under column head 'kcat/Km (M-1s-1)'. Printed with uncertainties as kcat 0.394 ± 0.0090 s^-1, Km 6830 ± 440 uM, kcat/Km 57.7 ± 3.9 M^-1 s^-1.

row_label: Table 3, enzyme line 'G144V', the three '+ 2 mM Pi' kinetic columns


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct lookup plus explicit mutation reconstruction and applied mutation signature R195A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R195A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme R195A, in the absence of phosphate, at pH 8.0 and 25°C


substrate_name: oxaloacetate

sequence_source: UniProtKB A5W059 direct lookup

smiles: O=C(O)CC(=O)C(=O)O

substrate: oxaloacetate


sequence_variant_note: Resolved canonical sequence from UniProtKB A5W059 direct lookup plus explicit mutation reconstruction and applied mutation signature N71A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N71A, in the absence of phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme N71A, in the presence of 2 mM phosphate, at pH 8.0 and 25°C


organism: Rhizobium leguminosarum

substrate_name: H2O; Biuret

sequence_source: UniProtKB reviewed entry Q1M7F4; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/Q1M7F4.json).

substrate: H2O; Biuret


substrate_name: Biuret

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q1M7F4; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/Q1M7F4.json). and applied mutation signature Q215A to reconstruct the assayed variant sequence.

substrate: Biuret


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry Q1M7F4; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/Q1M7F4.json). and applied mutation signature F41L to reconstruct the assayed variant sequence.


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


substrate_name: Coenzyme A; H2O

sequence_source: UniProtKB reviewed entry Q12524; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/Q12524.json).

assay_conditions_summary: cofactor CoA

substrate: Coenzyme A; H2O


substrate_name: CoA-disulfide

substrate: CoA-disulfide


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry P0AB87; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/P0AB87.json). and applied mutation signature F131A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed entry P0AB87; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/P0AB87.json). and applied mutation signature E214A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant E214A


enzyme_display_name: alpha-L-fucosidase

substrate_name: p-nitrophenyl alpha-L-fucopyranoside

sequence_source: uniprot:P04066 canonical sequence checked 2026-06-04

proof_lines: mutant E70G, 50 mM sodium phosphate buffer, pH 6.8, 37°C

enzyme: alpha-L-fucosidase

substrate: p-nitrophenyl alpha-L-fucopyranoside


proof_lines: mutant E135G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


proof_lines: mutant E289G, 50 mM sodium phosphate buffer, pH 6.8, 37°C, loss of catalytic activity


proof_lines: mutant D225G, 50 mM sodium phosphate buffer, pH 6.8, 37°C, loss of catalytic activity


proof_lines: mutant D258G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


proof_lines: mutant E289Q, 50 mM sodium phosphate buffer, pH 6.8, 37°C, loss of catalytic activity


proof_lines: mutant D158G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


proof_lines: mutant E275G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


organism: Thermotoga maritima

sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature T264A/L322P to reconstruct the assayed variant sequence.

proof_lines:
40°C, mutant enzyme T264A/L322P
70°C, mutant enzyme T264A/L322P


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature G226S/Y237H/T264A to reconstruct the assayed variant sequence.

proof_lines: 70°C, mutant enzyme G226S/Y237H/T264A/L322P4


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature P196L/Y237H/Y267F to reconstruct the assayed variant sequence.

proof_lines:
40°C, mutant enzyme P196L/Y237H/Y267F
70°C, mutant enzyme P196L/Y237H/Y267F


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature Y237H/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines:
70°C, mutant enzyme Y237H/Y267F/L322P
40°C, mutant enzyme Y237H/Y267F/L322P


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature T264A to reconstruct the assayed variant sequence.

proof_lines:
40°C, mutant enzyme T264A
70°C, mutant enzyme T264A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature T264A/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines:
40°C, mutant enzyme T264A/Y267F/L322P
70°C, mutant enzyme T264A/Y267F/L322P


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature G226S/T264A/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines: 70°C, mutant enzyme G226S/T264A/Y267F/L322P

proof_lines: 40°C, mutant enzyme G226S/T264A/Y267F/L322P


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9WYE2 canonical FASTA; row-specific variant reconstructed after validating mutation_signature residues. and applied mutation signature M210V/Y237H/T264A/Y267F to reconstruct the assayed variant sequence.

proof_lines: 40°C, mutant enzyme M210V/Y237H/T264A/Y267F

proof_lines: 70°C, mutant enzyme M210V/Y237H/T264A/Y267F


sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: mutant E79G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


substrate_name: 4-nitrophenyl alpha-L-fucopyranoside

substrate: 4-nitrophenyl alpha-L-fucopyranoside


sequence_source: UniProtKB P04066 canonical reviewed sequence; RCSB 7PLS/7PM4 structural entity maps to P04066

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


sequence_source: UniProtKB P04066 canonical reviewed sequence

assay_conditions_summary: pH 6.8; 310.15 K; buffer P04066 sequence identity preserved. 50 mM sodium phosphate

proof_lines: 50 mM sodium phosphate buffer, pH 6.8, 37°C


sequence_source: UniProtKB Q9BTY2 canonical reviewed sequence


organism: Mus musculus

sequence_source: UniProtKB Q99LJ1 canonical reviewed sequence


organism: Paenibacillus thiaminolyticus

sequence_source: UniProtKB K0JCW6 canonical unreviewed sequence; RCSB 6TVK polymer entity maps to K0JCW6


organism: Rattus norvegicus

substrate_name: p-Nitrophenyl-alpha-L-fucoside; H2O

sequence_source: UniProtKB reviewed entry P17164; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/P17164.json).

substrate: p-Nitrophenyl-alpha-L-fucoside; H2O


organism: Sulfolobus solfataricus

sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

proof_lines: SABIO-RK modifier species: alpha-L-fucosidase(Enzyme) mutant Ssalpha-fuc


substrate_name: H2O; p-Nitrophenyl-alpha-L-fucoside

proof_lines: SABIO-RK modifier species: alpha-L-fucosidase(Enzyme) mutant Asp242Gly

substrate: H2O; p-Nitrophenyl-alpha-L-fucoside


substrate_name: p-Nitrophenyl-alpha-L-fucoside

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

substrate: p-Nitrophenyl-alpha-L-fucoside


organism: Tannerella forsythia

sequence_source: UniProtKB TrEMBL entry G8UMQ6; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/G8UMQ6.json).


substrate_name: alpha-L-fucosyl fluoride

sequence_source: UniProtKB TrEMBL entry Q9WYE2; retrieved via UniProt REST on 2026-06-04 (https://rest.uniprot.org/uniprotkb/Q9WYE2.json).

substrate: alpha-L-fucosyl fluoride


proof_lines:
70°C, wild-type enzyme
40°C, wild-type enzyme


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup of Q9WYE2 on 2026-06-04 plus row-specific reconstruction from the selected mutation_signature. and applied mutation signature M210V/Y237H/T264A to reconstruct the assayed variant sequence.

proof_lines:
70°C, mutant enzyme M210V/Y237H/T264A
40°C, mutant enzyme M210V/Y237H/T264A


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup of Q9WYE2 on 2026-06-04 plus row-specific reconstruction from the selected mutation_signature. and applied mutation signature G226S/Y237H/T264A/L322P to reconstruct the assayed variant sequence.

proof_lines: 40°C, mutant enzyme G226S/Y237H/T264A/L322P


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup of Q9WYE2 on 2026-06-04 plus row-specific reconstruction from the selected mutation_signature. and applied mutation signature R147G/L322P to reconstruct the assayed variant sequence.

proof_lines:
40°C, mutant enzyme R147G/L322P
70°C, mutant enzyme R147G/L322P


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB lookup of Q9WYE2 on 2026-06-04 plus row-specific reconstruction from the selected mutation_signature. and applied mutation signature M210V/Y237H/T264A/Y267F/L322P to reconstruct the assayed variant sequence.

proof_lines: 70°C, mutant enzyme M210V/Y237H/T264A/Y267F/L322P

proof_lines: 40°C, mutant enzyme M210V/Y237H/T264A/Y267F/L322P


organism: uncultured bacterium


organism: Wenyingzhuangia fucanilytica

sequence_source: UniProtKB:A0A1B1NX89 direct lookup on 2026-06-04


enzyme_display_name: malyl-CoA lyase

organism: Cereibacter sphaeroides

substrate_name: beta-methylmalyl-CoA

sequence_source: UniProtKB:Q3J5L6 direct lookup on 2026-06-04

assay_conditions_summary: 303.15 K; cofactor CoA

proof_lines: condensation of acetyl-CoA and glyoxylate, at 30°C

proof_lines: condensation of propionyl-CoA and glyoxylate, at 30°C

enzyme: malyl-CoA lyase

substrate: beta-methylmalyl-CoA


organism: Haloarcula marismortui

substrate_name: Glyoxylate; Propanoyl-CoA

substrate: Glyoxylate; Propanoyl-CoA


sequence_source: UniProtKB:Q5V463 direct lookup on 2026-06-04


organism: Rhodobacter sphaeroides

substrate_name: Acetyl-CoA

assay_conditions_summary: pH 7.5; 303.15 K; cofactor CoA

column_label: Table 1, Mcl1 condensation of acetyl-CoA + glyoxylate: kcat 8.6 s^-1 and target-substrate Km 0.1 mM, yielding current 85.99999999999999 s^-1 mM^-1. The table's printed 2.8 × 10^3 M^-1 s^-1 reaction efficiency uses glyoxylate (Km 3.1 mM); it is preserved separately and is not used as the target-substrate efficiency.

normalized_value_unit_evidence: Same-row Table 1 cells give kcat=8.6 s^-1 and target-substrate Km=0.1 mM. Their stored-precision quotient is 8.6 / 0.1 = 85.99999999999999 s^-1 mM^-1. The separately printed reaction efficiency is not the target-substrate quotient.

raw_value_unit_evidence: kcat raw_value=8.6 raw_unit=s^-1; Km raw_value=0.1 raw_unit=mM; printed reaction efficiency 2.8 × 10^3 M^-1 s^-1, denominator=glyoxylate (Km 3.1 mM)

row_label: Mcl1 / condensation of acetyl-CoA + glyoxylate

table_label: Table 1: Molecular and catalytic properties of recombinant (3S)-malyl-CoA/β-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase from R. sphaeroides

substrate: Acetyl-CoA


enzyme_display_name: glucarate dehydratase

substrate_name: D-Glucarate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature H339Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant H339Q

enzyme: glucarate dehydratase

substrate: D-Glucarate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature D366A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant D366A


substrate_name: L-idarate

sequence_source: UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04

substrate: L-idarate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature K207Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant K207Q


sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature Y150F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant Y150F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature H339N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant H339N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AES2 FASTA and JSON direct REST check on 2026-06-04 and applied mutation signature H339A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant H339A


organism: Aspergillus niger

substrate_name: 4-nitrophenyl alpha-L-fucoside

substrate: 4-nitrophenyl alpha-L-fucoside


organism: Bombyx mori


organism: Clostridium perfringens

proof_lines:
pH 7, 37°C
Raw SKiD Env: Temp=37°C, pH=7


organism: Flavobacterium algicola


organism: Fusarium proliferatum


organism: Homo sapiens

proof_lines: mutant D276G, 50 mM sodium phosphate buffer, pH 6.8, 37°C


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot_reconstructed_variant and applied mutation signature D225N to reconstruct the assayed variant sequence.

proof_lines: mutant D225N, 50 mM sodium phosphate buffer, pH 6.8, 37°C


substrate_name: Glyoxylate

sequence_source: UniProtKB reviewed accession Q3J5L6 direct REST lookup on 2026-06-04

smiles: O=CC(=O)O

column_label: Table 1, Mcl1 condensation of propionyl-CoA plus glyoxylate: kcat 12 s^-1; target-substrate glyoxylate Km 4.1 mM; independently printed reaction efficiency 3.0 × 10^3 M^-1 s^-1 = 3.0 s^-1 mM^-1. The current stored specificity 2.9268292682926833 s^-1 mM^-1 is the deterministic quotient of the exact kcat and target-substrate Km cells; the independently printed value is not substituted for it.

normalized_value_unit_evidence: Same-reaction Table 1 cells give kcat=12 s^-1 and target-substrate Km=4.1 mM; their stored-precision quotient is 12 / 4.1 = 2.9268292682926833 s^-1 mM^-1; the independently printed efficiency normalizes separately to 3.0 s^-1 mM^-1 and is preserved as a distinct primary cell.

raw_value_unit_evidence: kcat raw_value=12 raw_unit=s^-1; glyoxylate Km raw_value=4.1 raw_unit=mM; independently printed reaction efficiency raw_value=3.0 × 10^3 raw_unit=M^-1 s^-1.

row_label: Mcl1 / condensation of propionyl-CoA plus glyoxylate

table_label: Table 1: Molecular and catalytic properties of recombinant (3S)-malyl-CoA/beta-methylmalyl-CoA lyase and (3S)-malyl-CoA thioesterase from R. sphaeroides

substrate: Glyoxylate


column_label: Table 1, Mcl1 cleavage of β-methylmalyl-CoA: kcat 2.8 s^-1; target-substrate Km 0.01 mM; printed kcat/Km 2.8 × 10^5 M^-1 s^-1 = 280 s^-1 mM^-1. Current 280 lies in the printed-efficiency rounding interval [275, 285) s^-1 mM^-1.

normalized_value_unit_evidence: Same-row Table 1 cells give kcat=2.8 s^-1 and target-substrate Km=0.01 mM. Their stored-precision quotient is 2.8 / 0.01 = 280 s^-1 mM^-1. Printed efficiency normalizes separately to 280 s^-1 mM^-1.

raw_value_unit_evidence: kcat raw_value=2.8 raw_unit=s^-1; Km raw_value=0.01 raw_unit=mM; printed kcat/Km raw_value=2.8 × 10^5 raw_unit=M^-1 s^-1

row_label: Mcl1 / cleavage of β-methylmalyl-CoA


substrate_name: Acetyl-CoA; Glyoxylate

substrate: Acetyl-CoA; Glyoxylate


substrate_name: Propanoyl-CoA

column_label: Table 1, Mcl1 condensation of propionyl-CoA + glyoxylate: kcat 12 s^-1 and target-substrate Km 0.2 mM, yielding current 60 s^-1 mM^-1. The table's printed 3.0 × 10^3 M^-1 s^-1 reaction efficiency uses glyoxylate (Km 4.1 mM); it is preserved separately and is not used as the target-substrate efficiency.

normalized_value_unit_evidence: Same-row Table 1 cells give kcat=12 s^-1 and target-substrate Km=0.2 mM. Their stored-precision quotient is 12 / 0.2 = 60 s^-1 mM^-1. The separately printed reaction efficiency is not the target-substrate quotient.

raw_value_unit_evidence: kcat raw_value=12 raw_unit=s^-1; Km raw_value=0.2 raw_unit=mM; printed reaction efficiency 3.0 × 10^3 M^-1 s^-1, denominator=glyoxylate (Km 4.1 mM)

row_label: Mcl1 / condensation of propionyl-CoA + glyoxylate

substrate: Propanoyl-CoA


substrate_name: L-Malyl-CoA

column_label: Table 1, Mcl1 cleavage of (3S)-malyl-CoA: kcat 2.5 s^-1; target-substrate Km 0.02 mM; printed kcat/Km 1.3 × 10^5 M^-1 s^-1 = 130 s^-1 mM^-1. Current 125 lies in the printed-efficiency rounding interval [125, 135) s^-1 mM^-1.

normalized_value_unit_evidence: Same-row Table 1 cells give kcat=2.5 s^-1 and target-substrate Km=0.02 mM. Their stored-precision quotient is 2.5 / 0.02 = 125 s^-1 mM^-1. Printed efficiency normalizes separately to 130 s^-1 mM^-1.

raw_value_unit_evidence: kcat raw_value=2.5 raw_unit=s^-1; Km raw_value=0.02 raw_unit=mM; printed kcat/Km raw_value=1.3 × 10^5 raw_unit=M^-1 s^-1

row_label: Mcl1 / cleavage of (3S)-malyl-CoA

substrate: L-Malyl-CoA


organism: Acinetobacter baylyi

sequence_source: UniProtKB reviewed accession Q6FFQ2 direct REST lookup on 2026-06-04

assay_conditions_summary: pH 7.5; 295.15 K; buffer 0.35 ug of D-glucarate dehydratase in 500 ul of Activity

column_label: Table label: TABLE 3 Kinetic parameters for D-glucarate dehydratase and KDG dehydratase. Row: D-Glucarate dehydratase. Columns read: Km (uM) cell 101, kcat (s^-1) cell 6.39, kcat/Km (s^-1 M^-1) cell 6.33 x 10^4. metric: kcat; raw value: 6.39; raw unit: s^-1; normalized value: 6.39 s^(-1); metric: Km; raw value: 101; raw unit: uM; normalized value: 0.101 mM; metric: kcat/Km; raw value: 6.33 x 10^4; raw unit: s^-1 M^-1; normalized value: 63.26732673267326 s^-1 mM^-1; assay condition: D-glucarate dehydratase assayed in Activity Buffer (50 mM Hepes/NaOH, pH 7.5, 100 mM NaCl, and 10% glycerol) containing 5 mM MgCl2; all enzymatic reactions were performed at 25 °C; kinetic parameters obtained from duplicate experiments by nonlinear analysis of initial rates.

normalized_value_unit_evidence: Table 3 row D-Glucarate dehydratase: Km 101 uM = 0.101 mM (1 uM = 0.001 mM); kcat 6.39 s^-1 = 6.39 s^(-1); kcat/Km 6.33 x 10^4 s^-1 M^-1 = 63.3 s^-1 mM^-1 at the printed cell's three-significant-figure precision, carried in the export at full precision as 63.26732673267326 s^-1 mM^-1, which is this row's own quotient 6.39 s^-1 / 0.101 mM and rounds back to the printed cell. In the Europe PMC PDF text render the plus-minus sign is written ⫾, the multiplication sign ⫻, the micro sign ␮ and the superscript minus one ⫺1, and superscript exponents are flattened, so the printed cell `6.33 ⫻ 104` is the paper's 6.33 x 10^4 s^-1 M^-1 and the unit header `␮M s⫺1 s⫺1 M⫺1` is uM, s^-1 and s^-1 M^-1.

raw_value_unit_evidence: TABLE 3 Kinetic parameters for D-glucarate dehydratase and KDG dehydratase; Values correspond to the average of two replicates. | metric header row of Table 3: `Enzyme Km kcat kcat/Km` | unit header row: `␮M s⫺1 s⫺1 M⫺1` | data row: `D-Glucarate dehydratase 101 ⫾ 15 6.39 ⫾ 0.26 6.33 ⫻ 104` | the D-Glucarate dehydratase cells read: Km = 101 ± 15 uM; kcat = 6.39 ± 0.26 s^-1; kcat/Km = 6.33 x 10^4 s^-1 M^-1.

row_label: D-Glucarate dehydratase


assay_conditions_summary: pH 7.5; 298.15 K; buffer 0.35 ug of D-glucarate dehydratase in 500 ul of Activity

table_label: TABLE 3 Kinetic parameters for D-glucarate dehydratase and KDG dehydratase


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0AES2 direct REST lookup plus K207R reconstruction on 2026-06-04 and applied mutation signature K207R to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant K207R


organism: Paenibacillus thiaminolyticus

sequence_source: UniProtKB REST K0JCW6 canonical sequence checked 2026-06-04


sequence_source: UniProtKB REST E3PQQ9 canonical sequence checked 2026-06-04


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST E3PQQ9 canonical sequence checked 2026-06-04 and applied mutation signature W392A to reconstruct the assayed variant sequence.


sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST K0JCW6 canonical sequence checked 2026-06-04 and applied mutation signature H503A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB REST K0JCW6 canonical sequence checked 2026-06-04 and applied mutation signature E235Q to reconstruct the assayed variant sequence.


organism: Pedobacter sp. CAU209

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.


enzyme_display_name: 8-amino-7-oxononanoate synthase

organism: Unknown

substrate_name: L-alanine

enzyme: 8-amino-7-oxononanoate synthase

substrate: L-alanine


sequence_variant_note: Resolved canonical sequence from direct UniProtKB lookup for P0AES2; D366N reconstructed from the reviewed canonical sequence and applied mutation signature D366N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant D366N


sequence_variant_note: Resolved canonical sequence from direct UniProtKB lookup for P0AES2; N341D reconstructed from the reviewed canonical sequence and applied mutation signature N341D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant N341D


sequence_variant_note: Resolved canonical sequence from direct UniProtKB lookup for P0AES2; N341L reconstructed from the reviewed canonical sequence and applied mutation signature N341L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glucarate dehydratase(Enzyme) mutant N341L


sequence_source: direct UniProtKB lookup for reviewed P0AES2 canonical sequence

assay_conditions_summary: pH 8; 295.15 K; buffer pH 8

column_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1). Table 1, row GlucD (glucarate); column kcat (s^-1) = 20; column Km (uM) = 60; column kcat/Km (M^-1 s^-1) = 3.3 x 10^5. captured primary segment: GlucD (glucarate) | kcat 20 ± 1 s^-1 | Km 60 ± 2 uM | kcat/Km 3.3 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 20 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 20.0 s^(-1); the exported value is 20.0 s^(-1). Km: printed Table 1 cell 60 uM; 1 uM is 1/1000 mM, so 60 / 1000 = 0.06 mM; the exported value is 0.06 mM. kcat/Km: printed Table 1 cell 3.3 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.3 x 10^5 / 1000 = 330.0 s^(-1)*mM^(-1). Quotient disclosure for this row: 20.0 / 0.06 = 333.33333333333337 s^-1 mM^-1, the exported value, and the printed efficiency cell is that quotient written to the two significant figures the table uses.

raw_value_unit_evidence: Table 1, row GlucD (glucarate): kcat = 20 s^-1; Km = 60 uM; printed kcat/Km = 3.3 x 10^5 M^-1 s^-1.

row_label: Table 1, row GlucD (glucarate)


substrate_name: L-Idarate

substrate: L-Idarate


organism: Pseudomonas putida


substrate_name: UDP-N-acetylglucosamine

substrate: UDP-N-acetylglucosamine


enzyme_display_name: nitrile hydratase

organism: Comamonas testosteroni

substrate_name: acrylonitrile

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme H80W/H81W

enzyme: nitrile hydratase

substrate: acrylonitrile


proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme R157K


sequence_source: UniProtKB:J9PBS0 direct accession lookup on 2026-06-04


proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme H80A


proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme H80A/H81A


organism: Klebsiella oxytoca

sequence_source: UniProtKB:A0A0H3HE78 direct accession lookup on 2026-06-04


organism: Monosiga brevicollis

substrate_name: Benzonitrile; acrylonitrile

sequence_source: UniProtKB:A9V2C1 direct accession lookup on 2026-06-04

substrate: Benzonitrile; acrylonitrile


smiles: C=CC#N


substrate_name: Benzonitrile

sequence_source: UniProtKB A9V2C1 direct lookup

substrate: Benzonitrile


organism: Nocardia sp.

sequence_source: UniProtKB Q8GJG6 direct lookup


proof_lines: recombinant NHase with modified start codon only


proof_lines: 25°C, pH not specified in the publication, beta-subunit mutant enzyme T173Y


proof_lines: 25°C, pH not specified in the publication, beta-subunit mutant enzyme S189E


proof_lines: 25°C, pH not specified in the publication, beta-subunit mutant enzyme M150C


proof_lines: 25°C, pH not specified in the publication, subunit-fused wild-type nitrile hydratase


organism: Pseudonocardia thermophila


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y114T to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T109S to reconstruct the assayed variant sequence.


substrate_name: Methacrylonitrile

smiles: C=C(C)C#N

substrate: Methacrylonitrile


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y68F to reconstruct the assayed variant sequence.


proof_lines:
isoenzyme B
isoenzyme A


enzyme_display_name: beta-ureidopropionase

substrate_name: N-Carbamoyl-beta-alanine

enzyme: beta-ureidopropionase

substrate: N-Carbamoyl-beta-alanine


sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.


organism: Rhodococcus rhodochrous

smiles: N#CCCCCC(=N)O


substrate_name: cyanoacetamide

smiles: N#CCC(=N)O

substrate: cyanoacetamide


substrate_name: Methacrylonitrile / 4-cyanopyridine / 3-Cyanopyridine / Benzonitrile / acrylonitrile

proof_lines: pH 7.6, 25°C, recombinant wild-type enzyme


substrate_name: Benzonitrile / acrylonitrile / Methacrylonitrile

proof_lines: pH 7.6, 25°C, recombinant mutant betaY68F

proof_lines: pH 7.6, 25°C, recombinant mutant alphaY114T

proof_lines: pH 7.6, 25°C, recombinant mutant alphaT109S


sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature Y114T to reconstruct the assayed variant sequence.


source_db: brenda/skid

ki_unit: mM

proof_lines:
pH 7.5, 25°C
Raw SKiD Env: Temp=25°C, pH=7.6

substrate: Methacrylonitrile / 4-cyanopyridine / 3-Cyanopyridine / Benzonitrile / acrylonitrile

source: brenda/skid


organism: Rhodococcus erythropolis

substrate_name: H2O; Methacrylonitrile

sequence_variant_note: Resolved canonical sequence from UniProt P13448 canonical alpha sequence with alpha-Q90E reconstructed as UniProt Q91E; P13449 beta partner checked by UniProt. and applied mutation signature Q90E with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: nitrile hydratase(Enzyme) mutant alpha-Q90E

substrate: H2O; Methacrylonitrile


substrate_name: (S)-mandelonitrile

sequence_variant_note: Resolved canonical sequence from UniProt P29379 canonical beta sequence with beta-F37H reconstructed; P29378 alpha partner checked by UniProt. and applied mutation signature F37H to reconstruct the assayed variant sequence.

substrate: (S)-mandelonitrile


sequence_source: UniProt P29378 canonical alpha-subunit sequence; source-listed P29379 beta partner checked by UniProt when present.


substrate_name: (R)-mandelonitrile

substrate: (R)-mandelonitrile


sequence_variant_note: Resolved canonical sequence from UniProt P29379 canonical beta sequence with beta-F37H reconstructed; BRENDA-listed P29378 alpha accession checked by UniProt. and applied mutation signature F37H to reconstruct the assayed variant sequence.


sequence_source: UniProt P29378 canonical alpha-subunit sequence.

proof_lines:
pH 7.4, 10°C, wild-type enzyme
pH 7.4, 35°C, wild-type enzyme


substrate_name: synthetic histone H3K18 decanoyllysine peptide

source_db: uniprot

sequence_variant_note: Source notes indicate a mutant or variant enzyme, but no machine-applicable substitution signature was available.

source: uniprot


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: NAD(+)

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

substrate: NAD(+)


assay_conditions_summary: cofactor NAD+


organism: Escherichia coli (strain K12)

substrate_name: pimeloyl-CoA (at pH 7.5 and at 30 degrees Celsius)

assay_conditions_summary: pH 7.5; cofactor CoA


organism: Lysinibacillus sphaericus

substrate_name: pimeloyl-CoA (at pH 7.0 and at 37 degrees Celsius)

assay_conditions_summary: pH 7; cofactor CoA


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: L-glycine (with acetyl-CoA at pH 6 and at 70 degrees Celsius)


organism: Xanthomonas campestris pv. campestris

substrate_name: UDP-glucuronate

substrate: UDP-glucuronate


enzyme_display_name: uracil phosphoribosyltransferase

organism: Bacillus caldolyticus

substrate_name: uracil

enzyme: uracil phosphoribosyltransferase

substrate: uracil


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate (in the presence of 1 mM GTP)


organism: Toxoplasma gondii


enzyme_display_name: acetyl-CoA C-acyltransferase

organism: Arabidopsis thaliana

substrate_name: acetoacetyl-CoA (at 25 degrees Celsius)

enzyme: acetyl-CoA C-acyltransferase

substrate: acetoacetyl-CoA (at 25 degrees Celsius)


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


organism: Rattus norvegicus


organism: Sinorhizobium meliloti

substrate_name: acetamiprid

sequence_source: UniProtKB:V5RFK1 direct lookup; NCBI Protein AHB33637.1

sequence_variant_note: Sequence identity was resolved, but no explicit wild-type or mutant call was captured.

substrate: acetamiprid


substrate_name: thiacloprid

substrate: thiacloprid


substrate_name: Benzonitrile


organism: Streptomyces rimosus

sequence_source: UniProtKB:B6CWJ3 direct lookup; NCBI Protein ACF06641.1

assay_conditions_summary: pH 65

proof_lines: pH 65, temperature not specified in the publication, recombinant trimeric enzyme

proof_lines: pH 65, temperature not specified in the publication, recombinant monomeric alpha enzyme


enzyme_display_name: serine--glyoxylate transaminase

organism: Hyphomicrobium methylovorum

substrate_name: glyoxylate

enzyme: serine--glyoxylate transaminase

substrate: glyoxylate


enzyme_display_name: histidinol-phosphate transaminase

organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)

substrate_name: histidinol phosphate

enzyme: histidinol-phosphate transaminase

substrate: histidinol phosphate


enzyme_display_name: rhodopsin kinase

organism: Danio rerio

substrate_name: rhodopsin

enzyme: rhodopsin kinase

substrate: rhodopsin


organism: Homo sapiens

assay_conditions_summary: cofactor ATP


enzyme_display_name: mitogen-activated protein kinase

substrate_name: ATP

enzyme: mitogen-activated protein kinase

substrate: ATP


organism: Caldalkalibacillus thermarum


organism: Comamonas testosteroni

substrate_name: acrylonitrile

sequence_source: UniProtKB:J9PBS0; RCSB:4FM4 entity 1

proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme H81A

substrate: acrylonitrile


proof_lines: pH 7.0, 25°C, alpha-subunit mutant enzyme R157A


organism: Rhodococcus erythropolis

substrate_name: Methacrylonitrile; H2O

substrate: Methacrylonitrile; H2O


substrate_name: H2O; Methacrylonitrile

proof_lines: SABIO-RK modifier species: nitrile hydratase(Enzyme) mutant alpha-Q90N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P13449 with direct R56K substitution check and applied mutation signature R56K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: nitrile hydratase(Enzyme) mutant beta-R56K


enzyme_display_name: membrane alanyl aminopeptidase

substrate_name: Cys-Gly

sequence_variant_note: No sequence was resolved for this record, so variant-aware sequence handling could not be applied.

enzyme: membrane alanyl aminopeptidase

substrate: Cys-Gly


organism: Brucella melitensis

sequence_source: UniProtKB:Q8YG38 direct REST lookup, fetched 2026-06-04


organism: Escherichia coli

substrate_name: H2O; Leu-p-nitroanilide

sequence_source: UniProtKB:P04825 direct REST lookup, fetched 2026-06-04

substrate: H2O; Leu-p-nitroanilide


sequence_source: UniProtKB:P15144 direct REST lookup, fetched 2026-06-04


substrate_name: H2O; Arg-4-methylcoumaryl-7-amide

proof_lines: pH not specified in the publication, temperature not specified in the publication

substrate: H2O; Arg-4-methylcoumaryl-7-amide


organism: Lactococcus lactis subsp. cremoris

substrate_name: H2O; Arg-Phe

sequence_source: UniProtKB:P0C2T8 direct REST lookup, fetched 2026-06-04

substrate: H2O; Arg-Phe


organism: Neisseria meningitidis serogroup B

substrate_name: Unknown

sequence_source: UniProtKB:Q9JYV4 direct REST lookup, fetched 2026-06-04

substrate: Unknown


enzyme_display_name: pyridoxal phosphatase

substrate_name: pyridoxal 5'-phosphate

enzyme: pyridoxal phosphatase

substrate: pyridoxal 5'-phosphate


substrate_name: lacto-N-fucopentaose II

substrate: lacto-N-fucopentaose II


enzyme_display_name: glucan 1,3-beta-glucosidase

organism: Candida albicans (strain SC5314 / ATCC MYA-2876)

substrate_name: laminaribiose

enzyme: glucan 1,3-beta-glucosidase

substrate: laminaribiose


organism: Escherichia coli (strain K12)


organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)


organism: Mus musculus

substrate_name: ATP (when both Thr-180 and Tyr-182 are phosphorylated)


enzyme_display_name: ribokinase

enzyme: ribokinase


substrate_name: ribose (in the presence of 10 mM inorganic phosphate)


organism: Staphylococcus aureus (strain COL)

substrate_name: ATP (in absence of K(+))

substrate: ATP (in absence of K(+))


enzyme_display_name: glutamate 5-kinase

organism: Leishmania donovani

substrate_name: L-glutamate

enzyme: glutamate 5-kinase

substrate: L-glutamate


substrate_name: dTTP

substrate: dTTP


organism: Arabidopsis thaliana


organism: Rattus norvegicus

substrate_name: N-carbamoyl-beta-alanine

smiles: C(CNC(=O)N)C(=O)O

substrate: N-carbamoyl-beta-alanine


enzyme_display_name: dimethylargininase

substrate_name: asymmetric dimethylarginine (ADMA)

enzyme: dimethylargininase

substrate: asymmetric dimethylarginine (ADMA)


organism: Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C / PRS 101 / PAO1)

substrate_name: N-methyl-L-arginine

substrate: N-methyl-L-arginine


enzyme_display_name: thiamine-triphosphatase

organism: Homo sapiens

substrate_name: thiamine triphosphate

enzyme: thiamine-triphosphatase

substrate: thiamine triphosphate


substrate_name: adenosine 5'-phosphoramidate (at pH 6.8)


organism: Plasmodium falciparum


substrate_name: H2O; L-Alanylglycine

substrate: H2O; L-Alanylglycine


organism: Sus scrofa

substrate_name: H2O; Leu-p-nitroanilide


organism: Trypanosoma congolense


substrate_name: P(1)-P(3)-bis(5'-adenosyl) triphosphate

substrate: P(1)-P(3)-bis(5'-adenosyl) triphosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)


enzyme_display_name: 8-oxo-dGTP diphosphatase

substrate_name: NADH (in the presence of 5 mM of manganese)

assay_conditions_summary: cofactor NADH

enzyme: 8-oxo-dGTP diphosphatase


organism: Bacillus subtilis (strain 168)

substrate_name: dGTP

substrate: dGTP


enzyme_display_name: oxaloacetate decarboxylase

organism: Pseudomonas putida (strain ATCC 700007 / DSM 6899 / JCM 31910 / BCRC 17059 / LMG 24140 / F1)

substrate_name: oxaloacetate (in presence of 1 mM of magnesium)

enzyme: oxaloacetate decarboxylase


organism: Pseudomonas straminea


enzyme_display_name: histone acetyltransferase

substrate_name: histone H4 peptide

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accessions endpoint checked 2026-06-04; accession O14929 and applied mutation signature E64A to reconstruct the assayed variant sequence.

proof_lines: mutant E64A, pH not specified in the publication, temperature not specified in the publication

enzyme: histone acetyltransferase

substrate: histone H4 peptide


substrate_name: acetyl-CoA

sequence_source: UniProtKB REST accessions endpoint checked 2026-06-04; accession Q9H7Z6

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

proof_lines: at 0.030 mM histone H4 peptide, pH and temperature not specified in the publication

proof_lines: at 0.090 mM histone H4 peptide, pH and temperature not specified in the publication

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accessions endpoint checked 2026-06-04; accession Q92830 and applied mutation signature T612G to reconstruct the assayed variant sequence.

proof_lines: mutant GCN5 T612G, pH and temperature not specified in the publication


sequence_source: UniProtKB REST accessions endpoint checked 2026-06-04; accession Q92830

proof_lines: wild-type GCN5, pH and temperature not specified in the publication


sequence_source: UniProtKB REST accessions endpoint checked 2026-06-04; accession Q09472

assay_conditions_summary: pH 7.5; 310.15 K; cofactor CoA

proof_lines: pH and temperature not specified in the publication


substrate_name: Unknown

sequence_source: UniProtKB REST accessions endpoint checked 2026-06-04; accession Q92831


sequence_source: UniProtKB REST accessions endpoint checked 2026-06-04; accession O14929

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accessions endpoint checked 2026-06-04; accession O14929 and applied mutation signature Y282A to reconstruct the assayed variant sequence.

proof_lines: 30°C, pH not specified in the publication, mutant enzyme Y282A


substrate_name: histone H3

assay_conditions_summary: pH 8

proof_lines: mutant having m-fluorophenylalanine incorporated, pH 8.0, temperature not specified in the publication

proof_lines: mutant having p-fluorophenylalanine incorporated, pH 8.0, temperature not specified in the publication

substrate: histone H3


proof_lines: wild-type, pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt O14929 canonical sequence with BRENDA/PMID 22615379 mutation W199A reconstructed after residue check and applied mutation signature W199A to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor CoA

proof_lines: mutant W199A, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt O14929 canonical sequence with BRENDA/PMID 22615379 mutation E187Q reconstructed after residue check and applied mutation signature E187Q to reconstruct the assayed variant sequence.

proof_lines: mutant E187Q, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt O14929 canonical sequence with BRENDA/PMID 22615379 mutation D277N reconstructed after residue check and applied mutation signature D277N to reconstruct the assayed variant sequence.

proof_lines: mutant D277N, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt O14929 canonical sequence with BRENDA/PMID 22615379 mutation D62A reconstructed after residue check and applied mutation signature D62A to reconstruct the assayed variant sequence.

proof_lines: mutant D62A, pH not specified in the publication, temperature not specified in the publication


sequence_source: UniProt O14929 canonical reviewed sequence checked directly against PubMed/RCSB HAT1 context

proof_lines: wild-type, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt O14929 canonical sequence with BRENDA/PMID 22615379 mutation E276Q reconstructed after residue check and applied mutation signature E276Q to reconstruct the assayed variant sequence.

proof_lines: mutant E276Q, pH not specified in the publication, temperature not specified in the publication


organism: Salmonella typhimurium (strain LT2 / SGSC1412 / ATCC 700720)


enzyme_display_name: trehalose-phosphatase

organism: Escherichia coli (strain K12)

substrate_name: Tre6P (with magnesium ions as cofactor and at pH 9)

assay_conditions_summary: pH 9

enzyme: trehalose-phosphatase


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: trehalose-6-phosphate (at 37 degrees Celsius and pH 7.5)


organism: Oryza sativa subsp. japonica

substrate_name: trehalose 6-phosphate

substrate: trehalose 6-phosphate


substrate_name: trehalose 6-phosphate (at pH 6.0)

assay_conditions_summary: pH 6

substrate: trehalose 6-phosphate (at pH 6.0)


substrate_name: succinyl-CoA

sequence_source: UniProtKB REST direct accession lookup, 2026-06-04; accession Q92830

proof_lines:
pH 8.0, 37°C
Raw SKiD Env: Temp=-----, pH=-----

substrate: succinyl-CoA


sequence_source: UniProtKB REST direct accession lookup, 2026-06-04; accession Q92793

proof_lines: against P300, pH and temperature not specified in the publication

substrate: Unknown


organism: Saccharomyces cerevisiae

substrate_name: Acetyl-CoA; Histone

sequence_source: UniProtKB REST direct accession lookup, 2026-06-04; accession Q03330

substrate: Acetyl-CoA; Histone


substrate_name: Acetyl-CoA

assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

substrate: Acetyl-CoA


sequence_source: UniProtKB REST direct accession lookup, 2026-06-04; accession Q08649


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, 2026-06-04; accession Q08649 and applied mutation signature C304A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, 2026-06-04; accession Q08649 and applied mutation signature C304S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup, 2026-06-04; accession Q08649 and applied mutation signature E338Q to reconstruct the assayed variant sequence.


substrate_name: serotonin

substrate: serotonin


organism: Zea mays

substrate_name: core histones

substrate: core histones


organism: Sphingobium sp. (strain NBRC 103272 / SYK-6)


enzyme_display_name: adenosylmethionine decarboxylase

organism: Arabidopsis thaliana

substrate_name: S-adenosyl-L-methionine

enzyme: adenosylmethionine decarboxylase

substrate: S-adenosyl-L-methionine


substrate_name: S-adenosyl-L-methionine (at 25 degrees Celsius in the presence of 0.01 M MgCl(2))


organism: Saccharolobus solfataricus (strain ATCC 35092 / DSM 1617 / JCM 11322 / P2)


organism: Trypanosoma brucei brucei

substrate_name: S-adenosyl-L-methionine (at 37 degrees Celsius)


organism: Trypanosoma cruzi

substrate_name: S-adenosyl-L-methionine (at pH 7.5)

substrate: S-adenosyl-L-methionine (at pH 7.5)


enzyme_display_name: malyl-CoA lyase

organism: Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM B-1809)

substrate_name: (S)-malyl-CoA (cleavage reaction)

enzyme: malyl-CoA lyase

substrate: (S)-malyl-CoA (cleavage reaction)


organism: Rhodobacter capsulatus

substrate_name: L-malyl-CoA

substrate: L-malyl-CoA


enzyme_display_name: glucarate dehydratase

substrate_name: idarate

enzyme: glucarate dehydratase

substrate: idarate


enzyme_display_name: nitrile hydratase

organism: Rhodococcus rhodochrous

substrate_name: 3-cyanopyridine (at pH 7.0 and 20 degrees Celsius)

enzyme: nitrile hydratase


enzyme_display_name: L-fuculose-phosphate aldolase

organism: Methanocaldococcus jannaschii (strain ATCC 43067 / DSM 2661 / JAL-1 / JCM 10045 / NBRC 100440)

substrate_name: dihydroxyacetone phosphate (DHAP)

enzyme: L-fuculose-phosphate aldolase

substrate: dihydroxyacetone phosphate (DHAP)


organism: Pseudomonas putida (strain ATCC 700007 / DSM 6899 / JCM 31910 / BCRC 17059 / LMG 24140 / F1)

substrate_name: oxaloacetate (in presence of 1 mM of magnesium)


organism: Pseudomonas straminea


organism: Cereibacter sphaeroides (strain ATCC 17023 / DSM 158 / JCM 6121 / CCUG 31486 / LMG 2827 / NBRC 12203 / NCIMB 8253 / ATH 2.4.1.)

substrate_name: glyoxylate (for L-malyl-CoA formation)

substrate: glyoxylate (for L-malyl-CoA formation)


organism: Chloroflexus aurantiacus

substrate_name: (S)-malyl-CoA (for L-malyl-CoA lyase activity)


enzyme_display_name: tyrosine 3-monooxygenase

organism: Homo sapiens

substrate_name: tetrahydrobiopterin

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: E332D phosphorylated mutant protein, pH 7.2, 30°C

proof_lines: E332D mutant protein, dopamine bound to the high-affinity site, pH 7.2, 30°C

enzyme: tyrosine 3-monooxygenase

substrate: tetrahydrobiopterin


proof_lines: A297L phosphorylated mutant protein, pH 7.2, 30°C

proof_lines: mutant enzyme A297L, pH and temperature not specified in the publication


sequence_source: UniProt P07101 canonical FASTA, retrieved 2026-06-04 via UniProt REST


proof_lines: Y371F phosphorylated mutant protein, pH 7.2, 30°C

proof_lines: Y371F mutant protein, dopamine bound to the high-affinity site, pH 7.2, 30°C


organism: Bos taurus

substrate_name: O2; L-Tyrosine; Tetrahydrobiopterin

sequence_source: UniProtKB:P17289 reviewed FASTA via rest.uniprot.org on 2026-06-04

substrate: O2; L-Tyrosine; Tetrahydrobiopterin


substrate_name: Tetrahydrobiopterin; L-Tyrosine; O2

sequence_source: UniProtKB:P07101 reviewed FASTA via rest.uniprot.org on 2026-06-04

substrate: Tetrahydrobiopterin; L-Tyrosine; O2


proof_lines: L294A phosphorylated mutant protein, pH 7.2, 30°C


proof_lines: F300Y phosphorylated mutant protein, pH 7.2, 30°C


proof_lines: F300A phosphorylated mutant protein, pH 7.2, 30°C


proof_lines: wild type protein, in the presence of 0.01 mM dopamine, pH 7.2, 30°C

proof_lines: wild type, phosphorylated protein, pH 7.2, 30°C


sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

proof_lines: L294Y phosphorylated mutant protein, pH 7.2, 30°C


substrate_name: L-tyrosine

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E362G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E362G, pH and temperature not specified in the publication

substrate: L-tyrosine


proof_lines: mutant enzyme K366L, pH and temperature not specified in the publication


proof_lines: mutant enzyme E365G, pH and temperature not specified in the publication


proof_lines: mutant enzyme E362R/E365R, pH and temperature not specified in the publication


proof_lines: mutant enzyme R37E/R38E, pH and temperature not specified in the publication


proof_lines: mutant enzyme D361N, pH and temperature not specified in the publication


proof_lines: mutant enzyme S368A, pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P07101-3; reconstructed variant from selected source mutation note. and applied mutation signature K169E/L479A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme K169E/L479A, dimer


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P07101-3; reconstructed variant from selected source mutation note. and applied mutation signature E114K to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme E114K, tetramer


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P07101-3; reconstructed variant from selected source mutation note. and applied mutation signature D467G to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme D467G, tetramer > dimer

proof_lines: pH 7.0, 30°C, mutant enzyme D467G dimer > tetramer


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P07101-3; reconstructed variant from selected source mutation note. and applied mutation signature R410P to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, 30°C, mutant enzyme R410P, tetramer > dimer


organism: Rattus norvegicus

sequence_variant_note: Resolved canonical sequence from UniProtKB REST P04177; reconstructed variant from selected source mutation note. and applied mutation signature F309A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant F309A


sequence_variant_note: Resolved canonical sequence from UniProtKB REST P04177; reconstructed variant from selected source mutation note. and applied mutation signature F300A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant F300A


proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant V379D


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425S, in 50 mM HEPES (pH 7.0), at 30°C


substrate_name: L-phenylalanine

sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425E, in 50 mM HEPES (pH 7.0), at 30°C

substrate: L-phenylalanine


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425N to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425N, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature Q424A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q424A, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425T to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425T, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425Y, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature D425H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425H, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 canonical FASTA fetched directly on 2026-06-04; variant reconstructed from the selected mutation signature. and applied mutation signature Q426A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q426A, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S40E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S40E


sequence_source: UniProtKB P04177 FASTA fetched during review.

sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S19A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S19A


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S19E/S40E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S19E/S40E


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S40A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S40A


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S8A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S8A


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S19E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S19E


sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 FASTA fetched during review; variant reconstructed from selected mutation_signature. and applied mutation signature S31A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S31A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04177 and applied mutation signature D425V to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'D425V TyrH'; column 'Vmax for tyrosine hydroxylation (min-1)' = 1.24; column 'Ktyr (µM)' = 45; column 'V/Ktyr (µM-1 min-1)' = 0.028. The remaining three cells of the same printed row belong to the phenylalanine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'D425V TyrH': Ktyr = 45 uM; Vmax for tyrosine hydroxylation = 1.24 min^-1; V/Ktyr = 0.028 uM^-1 min^-1.

row_label: Table 3, enzyme row 'D425V TyrH', the three tyrosine hydroxylation cells (Vmax for tyrosine hydroxylation, Ktyr, V/Ktyr)


substrate_name: L-Tyrosine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature H264Q/V379D to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H264Q/V379D PheH'; column 'Vmax for tyrosine hydroxylation (min-1)' = 1.2; column 'Ktyr (µM)' = 146; column 'V/Ktyr (µM-1 min-1)' = 8.2 x 10^-3. The remaining three cells of the same printed row belong to the phenylalanine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H264Q/V379D PheH': Ktyr = 146 uM; Vmax for tyrosine hydroxylation = 1.2 min^-1; V/Ktyr = 8.2 x 10^-3 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H264Q/V379D PheH', the three tyrosine hydroxylation cells (Vmax for tyrosine hydroxylation, Ktyr, V/Ktyr)

substrate: L-Tyrosine


sequence_variant_note: Resolved canonical sequence from UniProt REST reviewed entry P04176; variant reconstructed by worker residue check and applied mutation signature H264Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 4

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant H264Q


table_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661)


sequence_variant_note: Resolved canonical sequence from UniProt REST reviewed entry P04177; variant reconstructed by worker residue check and applied mutation signature H331E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant H331E


sequence_variant_note: Resolved canonical sequence from UniProt REST reviewed entry P04177; variant reconstructed by worker residue check and applied mutation signature H336E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant H336E


sequence_variant_note: Resolved canonical sequence from UniProt REST reviewed entry P04177; variant reconstructed by worker residue check and applied mutation signature H336Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant H336Q


substrate_name: L-Phenylalanine

sequence_variant_note: Resolved canonical sequence from UniProtKB P04177 direct FASTA lookup on 2026-06-04 plus Y371F reconstruction from PMID 9819237 and applied mutation signature Y371F to reconstruct the assayed variant sequence.

substrate: L-Phenylalanine


sequence_source: UniProtKB P04177 direct FASTA lookup on 2026-06-04


sequence_source: UniProtKB P04177 direct FASTA lookup on 2026-06-04 plus Y371F reconstruction from PMID 9819237

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant Y371F


organism: Saccharomyces cerevisiae

substrate_name: acetyl-CoA

sequence_source: UniProtKB Q07794 direct FASTA lookup on 2026-06-04

substrate: acetyl-CoA


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425R substitution from canonical sequence and applied mutation signature D425R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425R, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed T427A substitution from canonical sequence and applied mutation signature T427A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T427A, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425M substitution from canonical sequence and applied mutation signature D425M to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425M, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425C substitution from canonical sequence and applied mutation signature D425C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425C, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425L substitution from canonical sequence and applied mutation signature D425L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425L, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425K substitution from canonical sequence and applied mutation signature D425K to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425K, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed D425A substitution from canonical sequence and applied mutation signature D425A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425A, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 FASTA sequence version 3; reconstructed Y423A substitution from canonical sequence and applied mutation signature Y423A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y423A, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04177 and applied mutation signature Q310H to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'Q310H TyrH'; column 'Vmax for tyrosine hydroxylation (min-1)' = 128; column 'Ktyr (µM)' = 54; column 'V/Ktyr (µM-1 min-1)' = 2.37. The remaining three cells of the same printed row belong to the phenylalanine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'Q310H TyrH': Ktyr = 54 uM; Vmax for tyrosine hydroxylation = 128 min^-1; V/Ktyr = 2.37 uM^-1 min^-1.

row_label: Table 3, enzyme row 'Q310H TyrH', the three tyrosine hydroxylation cells (Vmax for tyrosine hydroxylation, Ktyr, V/Ktyr)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04176 and applied mutation signature H264Q/Y277H/V379D to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H264Q/Y277H/V379D PheH'; column 'Vmax for tyrosine hydroxylation (min-1)' = 1.83; column 'Ktyr (µM)' = 1310; column 'V/Ktyr (µM-1 min-1)' = 1.4 x 10^-3. The remaining three cells of the same printed row belong to the phenylalanine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H264Q/Y277H/V379D PheH': Ktyr = 1310 uM; Vmax for tyrosine hydroxylation = 1.83 min^-1; V/Ktyr = 1.4 x 10^-3 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H264Q/Y277H/V379D PheH', the three tyrosine hydroxylation cells (Vmax for tyrosine hydroxylation, Ktyr, V/Ktyr)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P04177 and applied mutation signature H323Y to reconstruct the assayed variant sequence.

column_label: Table 3: Steady-State Kinetic Parameters for Amino Acid Hydroxylation by Mutant Tyrosine and Phenylalanine Hydroxylases (Biochemistry 2000, 39, 9652-9661); enzyme row 'H323Y TyrH'; column 'Vmax for tyrosine hydroxylation (min-1)' = 159; column 'Ktyr (µM)' = 92; column 'V/Ktyr (µM-1 min-1)' = 1.73. The remaining three cells of the same printed row belong to the phenylalanine hydroxylation reaction.

raw_value_unit_evidence: Table 3, enzyme row 'H323Y TyrH': Ktyr = 92 uM; Vmax for tyrosine hydroxylation = 159 min^-1; V/Ktyr = 1.73 uM^-1 min^-1.

row_label: Table 3, enzyme row 'H323Y TyrH', the three tyrosine hydroxylation cells (Vmax for tyrosine hydroxylation, Ktyr, V/Ktyr)


sequence_variant_note: Resolved canonical sequence from UniProt REST P04176 canonical sequence reconstructed with mutation Y277H and applied mutation signature Y277H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant Y277H


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected SABIO-RK mutant note S31E and applied mutation signature S31E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S31E


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected SABIO-RK mutant note S8E and applied mutation signature S8E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant S8E


sequence_variant_note: Mutation context is present, but no sequence was resolved for this record.

proof_lines: SABIO-RK modifier species: tyrosine 3-monooxygenase(Enzyme) mutant TyrHpS31


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected BRENDA mutant note D425I and applied mutation signature D425I to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425I, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Sequence is treated as wild-type because the source explicitly marked the record as wild-type.

proof_lines: wild type enzyme, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected BRENDA mutant note D425G and applied mutation signature D425G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425G, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected BRENDA mutant note D425Q and applied mutation signature D425Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425Q, in 50 mM HEPES (pH 7.0), at 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:P04177 plus selected BRENDA mutant note D425F and applied mutation signature D425F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D425F, in 50 mM HEPES (pH 7.0), at 30°C


enzyme_display_name: Histone acetyltransferase RTT109

sequence_variant_note: Resolved canonical sequence from direct UniProt REST lookup for Q07794 on 2026-06-04 and applied mutation signature D287N to reconstruct the assayed variant sequence.

enzyme: Histone acetyltransferase RTT109


substrate_name: histone H3 tail peptide

sequence_variant_note: Resolved canonical sequence from direct UniProt REST lookup for Q07794 on 2026-06-04 and applied mutation signature D287A/D288A to reconstruct the assayed variant sequence.

substrate: histone H3 tail peptide


sequence_variant_note: Resolved canonical sequence from direct UniProt REST lookup for Q07794 on 2026-06-04 and applied mutation signature D288N to reconstruct the assayed variant sequence.


sequence_source: direct UniProt REST lookup for Q07794 on 2026-06-04


enzyme_display_name: acetyl-CoA C-acyltransferase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: acetoacetyl-CoA

proof_lines: kcat is 4.8 sec(-1) with acetoacetyl-CoA as substrate.

enzyme: acetyl-CoA C-acyltransferase

substrate: acetoacetyl-CoA


organism: Escherichia coli (strain K12)

substrate_name: a synthetic histone H3K9 acetyllysine peptide

proof_lines: kcat is 0.135 sec(-1) for acetyllysine peptide. kcat is 0.242 sec(-1) for succinyllysine peptide.


substrate_name: NAD

proof_lines: kcat is 0.08 sec(-1) for histone H4 H4K16la.

substrate: NAD


proof_lines: kcat is 0.0049 sec(-1) for N6-tetradecanoyl-L-lysyl-peptide (myristoylated peptide) (PubMed:23552949). kcat is 0.0027 sec(-1) for N6-hexadecanoyl-L-lysyl-peptide (palmitoylated peptide) (PubMed:23552949). kcat is 0.0020 sec(-1) for N6-tetra


substrate_name: a peptide of H3 biotinylated at 'Lys-9'

proof_lines: kcat is 0.0019 sec(-1) for the delipoylation of H3 'Lys-9'. kcat is 0.0005 sec(-1) for the debiotinylation of H3 'Lys-9'. kcat is 0.0018 sec(-1) for the delipoylation of DLAT 'Lys-259'.

substrate: a peptide of H3 biotinylated at 'Lys-9'


substrate_name: an peptide acetylated on lysine

proof_lines: kcat is 0.275 sec(-1) with a peptide acetylated on lysine as substrate (PubMed:25704306). kcat is 0.018 sec(-1) with a peptide myristoylated on lysine as substrate (PubMed:25704306).

substrate: an peptide acetylated on lysine


substrate_name: phenylalanine

substrate: phenylalanine


proof_lines: kcat is 1.27 min(-1) with N(6)-acetyl-L-lysyl-[HupB] as substrate.


organism: Proteus mirabilis (strain HI4320)

proof_lines: kcat is 0.225 sec(-1) for a N6-(2-hydroxyisobutyryl)lysine peptide.


enzyme_display_name: 8-amino-7-oxononanoate synthase

organism: Arabidopsis thaliana

substrate_name: pimeloyl-CoA (at pH 7.5 and 30 degrees Celsius)

proof_lines: kcat is 0.1 sec(-1) with pimeloyl-CoA as substrate. kcat is 0.11 sec(-1) with L-alanine as substrate.

enzyme: 8-amino-7-oxononanoate synthase


substrate_name: pimeloyl-CoA (at pH 7.7 and 25 degrees Celsius)

assay_conditions_summary: pH 7.7; cofactor CoA

proof_lines: kcat is 0.007 sec(-1) and 0.0036 sec(-1) with L-alanine and D-alanine as substrate, respectively, and pimeloyl-CoA as co-substrate.


proof_lines: kcat is 172 min(-1) with acetyl-CoA as substrate (PubMed:27382063). kcat is 173 min(-1) with a histone H4 peptide as substrate (PubMed:27382063). kcat is 15 min(-1) with a histone H4K16 peptide as substrate (PubMed:33467728).


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: acetyl-CoA (at pH 7.5, 25 degrees Celsius in the presence of VPS75 chaperone)

proof_lines: kcat is 0.11 sec(-1) with acetyl-CoA as substrate (at pH 7.5, 25 degrees Celsius in the presence of VPS75 chaperone) (PubMed:20560668). kcat is 0.19 sec(-1) with acetyl-CoA as substrate (at pH 7.0, 25 degrees Celsius in the presence of VPS7


substrate_name: lipid I

substrate: lipid I


substrate_name: tRNA(Tyr)

proof_lines: kcat is 0.00121 sec(-1) with tRNA(Tyr) and guanine as substrates.

substrate: tRNA(Tyr)


organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)

proof_lines: kcat is 0.0022 sec(-1) with tRNA(Tyr) and guanine as substrates.


enzyme_display_name: N(1)-aminopropylagmatine synthase

organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: agmatine

proof_lines: kcat is 2.09 sec(-1) for aminopropyl transferase activity with cadaverine as amine acceptor. kcat is 0.18 sec(-1) for aminopropyl transferase activity with putrescine as amine acceptor. kcat is 0.1 sec(-1) for aminopropyl transferase activi

enzyme: N(1)-aminopropylagmatine synthase

substrate: agmatine


organism: Thermococcus kodakarensis (strain ATCC BAA-918 / JCM 12380 / KOD1)

substrate_name: agmatine (at pH 9 and 70 degrees Celsius)

proof_lines: kcat is 0.3 sec(-1) for aminopropyl transferase activity with putrescine as substrate (at pH 9 and 70 degrees Celsius). kcat is 0.28 sec(-1) for aminopropyl transferase activity with agmatine as substrate (at pH 9 and 70 degrees Celsius). k


organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: norspermidine (at pH 9 and 37 degrees Celsius)

sequence_source: source_record; direct UniProt REST exact match to Q5SK28

proof_lines: kcat is 0.73 sec(-1) for aminopropyl transferase activity with S-adenosylmethioninamine as substrate (at pH 9 and 37 degrees Celsius). kcat is 0.65 sec(-1) for aminopropyl transferase activity with spermidine as substrate (at pH 9 and 37 de


enzyme_display_name: adenosyl-fluoride synthase

organism: Actinoplanes sp. (strain N902-109)

substrate_name: S-adenosyl-L-methionine

sequence_source: source_record; direct UniProt REST exact match to R4LHX8

enzyme: adenosyl-fluoride synthase

substrate: S-adenosyl-L-methionine


organism: Nocardia brasiliensis (strain ATCC 700358 / HUJEG-1)

sequence_source: source_record; direct UniProt REST exact match to W8JNL4


organism: Streptantibioticus cattleyicolor

substrate_name: SAM (at pH 7.8 and degrees Celsius)

sequence_source: source_record; direct UniProt REST exact match to Q70GK9

proof_lines: kcat is 0.07 sec(-1) for 5'-FDA synthase activity with SAM as substrate(at pH 7.9 and 37 degrees Celsius). kcat is 0.06 sec(-1) for 5'-FDA synthase activity with fluoride as substrate (at pH 7.9 and 37 degrees Celsius).

substrate: SAM (at pH 7.8 and degrees Celsius)


organism: Streptomyces sp

substrate_name: S-adenosyl-L-methionine (for fluorinase activity)

sequence_source: source_record; direct UniProt REST exact match to W0W999

proof_lines: kcat is 0.262 min(-1) for fluorinase activity (PubMed:24449539). kcat is 0.22 min(-1) for fluorinase activity (PubMed:27739177). kcat is 0.017 min(-1) for SAM hydrolase activity (PubMed:36996195). kcat is 0.008 min(-1) for chlorinase activi


enzyme_display_name: serine--glyoxylate transaminase

substrate_name: alanine (with recombinant enzyme, in the presence of 20 mM glyoxylate)

sequence_source: source_record; direct UniProt REST exact match to Q56YA5

proof_lines: kcat is 6.4 sec(-1) for L-serine. kcat is 2.86 sec(-1) for L-alanine.

enzyme: serine--glyoxylate transaminase


enzyme_display_name: histidinol-phosphate transaminase

substrate_name: histidinol phosphate

proof_lines: kcat is 426 sec(-1) with histidinol phosphate as substrate. kcat is 220 sec(-1) with phenylalanine as substrate. kcat is 3100 sec(-1) with tyrosine as substrate.

enzyme: histidinol-phosphate transaminase

substrate: histidinol phosphate


enzyme_display_name: ribokinase

substrate_name: D-ribose

enzyme: ribokinase

substrate: D-ribose


organism: Leishmania major

substrate_name: ATP

proof_lines: kcat is 10.2 sec(-1) with ATP as substrate and 10.8 sec(-1) with ribose as substrate.

substrate: ATP


proof_lines: kcat is 7.3 sec(-1) with glucose-1-phosphate as substrate. kcat is 7.9 sec(-1) with dTTP as substrate.


organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

proof_lines: kcat is 69.7 sec(-1) for GalN-1-P acetyltransferase activity. kcat is 123.2 sec(-1) for GlcN-1-P acetyltransferase activity.


enzyme_display_name: arylesterase

organism: Gluconobacter oxydans

substrate_name: phenyl acetate

sequence_source: UniProtKB Q5FSJ2 direct REST lookup on 2026-06-04

enzyme: arylesterase

substrate: phenyl acetate


substrate_name: 4-nitrophenyl butanoate

substrate: 4-nitrophenyl butanoate


substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


substrate_name: S-methyl thiobutanoate

smiles: CCCC(=O)SC

substrate: S-methyl thiobutanoate


substrate_name: 2-naphthyl butanoate

assay_conditions_summary: pH 7

substrate: 2-naphthyl butanoate


organism: Homo sapiens

proof_lines:
enzyme variant Q192
enzyme variant R192


substrate_name: 2-naphthyl acetate

proof_lines: pH 8.0, recombinant genetic variant G1B11

proof_lines: pH 8.0, recombinant genetic variant G1A7

proof_lines: pH 8.0, recombinant genetic variant G2C2

substrate: 2-naphthyl acetate


sequence_variant_note: Resolved canonical sequence from Variant reconstructed from UniProtKB P27169 direct REST lookup on 2026-06-04 and applied mutation signature G11S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P27169 canonical sequence with direct residue-substitution reconstruction and applied mutation signature E314A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P27169 canonical sequence with direct residue-substitution reconstruction and applied mutation signature N133S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P27169 canonical sequence with direct residue-substitution reconstruction and applied mutation signature E313A to reconstruct the assayed variant sequence.


sequence_source: UniProt REST P27169 canonical sequence; no single variant sequence reconstructed

sequence_variant_note: Canonical sequence is preserved, but mutation context is present; variant sequence was not attached without safely applying the mutation.

proof_lines: mutant G11A or mutant G11C, pH 8.0, 25°C


sequence_variant_note: Resolved canonical sequence from UniProt REST P27169 canonical sequence with direct residue-substitution reconstruction and applied mutation signature F222Y to reconstruct the assayed variant sequence.

proof_lines:
pH 8.0, 25°C, mutant enzyme F222Y
mutant F222Y, pH 8.0, 25°C


sequence_source: UniProt REST Q15166 canonical sequence