sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0H2UP35 and applied mutation signature Y126F to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'Y126F', Cellobiose-6'P column group: column 'Km (uM)' = 1515; column 'kcat (s^-1)' = 138; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 0.9. The other three numeric cells of the same printed row belong to the pNP-beta-Glc6P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 1515 uM; 1515 / 1000 = 1.515 mM. kcat: printed Table 2 cell 138 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 0.9 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 0.9 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 90.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 138.0 / 1.515 = 91.0891089108911 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'Y126F', Cellobiose-6'P column group: Km = 1515 uM; kcat = 138 s^-1; printed kcat/Km = 0.9 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Y126F', the three Cellobiose-6'P cells (Km, kcat, kcat/Km x10^-1)


organism: Streptococcus pneumoniae

source_db: brenda

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

proof_lines: pH 7.5, 37°C, recombinant His-tagged wild-type enzyme

source: brenda


substrate_name: cellobiose 6-phosphate

source_db: oed

verification_status: verified

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0H2UP35 and applied mutation signature M423A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.5; 310.15 K; buffer 50 mM NaH2PO4. The Enzymatic Activity Assays section states this

column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'M423A', Cellobiose-6'P column group: column 'Km (uM)' = 1320; column 'kcat (s^-1)' = 145; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 1.1. The other three numeric cells of the same printed row belong to the pNP-beta-Glc6P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 1320 uM; 1320 / 1000 = 1.32 mM. kcat: printed Table 2 cell 145 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 1.1 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 1.1 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 110.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 145.0 / 1.32 = 109.84848484848484 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'M423A', Cellobiose-6'P column group: Km = 1320 uM; kcat = 145 s^-1; printed kcat/Km = 1.1 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'M423A', the three Cellobiose-6'P cells (Km, kcat, kcat/Km x10^-1)

table_label: Table 2: Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P (J. Biol. Chem. 2013, 288(21):14949-14958)

data_origin: experimental

substrate: cellobiose 6-phosphate

status: verified

source: oed


organism: Escherichia coli

substrate_name: UDP-GlcNAc

sequence_source: UniProtKB REST P17443 FASTA/JSON checked 2026-06-04

proof_lines:
wild type enzyme
wild-type enzyme

substrate: UDP-GlcNAc


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

sequence_source: UniProtKB P17443 canonical sequence used only as mutation context; row-specific variant sequence not resolved

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: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant N198A C-terminal His-tag


proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant Y105A C-terminal His-tag


proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant H124A C-terminal His-tag


substrate_name: UDP-N-acetyl-D-glucosamine

substrate: UDP-N-acetyl-D-glucosamine


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

source_databases_merged: sabio_rk brenda skid


organism: Klebsiella pneumoniae subsp. pneumoniae

substrate_name: Unknown

kcat_display: Not reported

km_display: Not reported

ki_unit: mM

sequence_source: UniProtKB A6T4N3 FASTA/JSON direct lookup, reviewed Swiss-Prot entry MURG_KLEP7.

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

substrate: Unknown


enzyme_display_name: trehalose-phosphatase

organism: Brugia malayi

substrate_name: trehalose 6-phosphate

verification_status: unverified

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution N228A. and applied mutation signature N228A to reconstruct the assayed variant sequence.

enzyme: trehalose-phosphatase

substrate: trehalose 6-phosphate

status: unverified


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution E384A. and applied mutation signature E384A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution W280A. and applied mutation signature W280A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution D336A. and applied mutation signature D336A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution D378A. and applied mutation signature D378A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution R337A. and applied mutation signature R337A to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB A8NS89 canonical sequence by applying selected row substitution E384A.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed E125A substitution and applied mutation signature E125A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed S191A substitution and applied mutation signature S191A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed T15A substitution and applied mutation signature T15A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant T15A C-terminal His-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed Y105A substitution and applied mutation signature Y105A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:P17443 canonical sequence with reconstructed S191A substitution

proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant S191A C-terminal His-tag


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed R260A substitution and applied mutation signature R260A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P17443 canonical sequence with reconstructed N291A substitution and applied mutation signature N291A to reconstruct the assayed variant sequence.


organism: Thermotoga maritima

substrate_name: 4-Nitrophenyl beta-D-glucopyranoside 6-phosphate; H2O

sequence_source: UniProtKB Q9X108 direct lookup on 2026-06-04

proof_lines:
pH 7.5, 50°C
pH 7.5
Raw SKiD Env: Temp=50°C, pH=7.5


organism: uncultured organism

sequence_source: UniProtKB L7Y2Z6 direct lookup on 2026-06-04


enzyme_display_name: beta-ureidopropionase

organism: Arabidopsis thaliana

substrate_name: H2O; N-Carbamoyl-beta-alanine

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

sequence_source: UniProtKB Q8H183 direct lookup on 2026-06-04

enzyme: beta-ureidopropionase

substrate: H2O; N-Carbamoyl-beta-alanine


organism: Caenorhabditis elegans

substrate_name: 3-ureidopropionic acid

sequence_source: UniProtKB Q19437 direct lookup on 2026-06-04

substrate: 3-ureidopropionic acid


organism: Homo sapiens

sequence_source: UniProtKB Q9UBR1 direct lookup on 2026-06-04


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


organism: Lachancea kluyveri

substrate_name: N-Carbamoyl-beta-alanine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q96W94 direct lookup plus E159D one-based substitution computed on 2026-06-04 and applied mutation signature E159D to reconstruct the assayed variant sequence.

substrate: N-Carbamoyl-beta-alanine


sequence_source: UniProtKB Q96W94 direct lookup on 2026-06-04

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


enzyme_display_name: ribokinase

substrate_name: ATP

sequence_source: UniProtKB Q9H477 direct REST lookup, release 2026_01

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

enzyme: ribokinase

substrate: ATP


substrate_name: D-ribose

substrate: D-ribose


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9H477 direct REST lookup plus explicit N199L reconstruction and applied mutation signature N199L to reconstruct the assayed variant sequence.

proof_lines: mutant N199L, presence of Mg2+, pH 7.2, 37°C


proof_lines: wild-type, presence of Mg2+, pH 7.2, 37°C

proof_lines: wild-type, presence of Mn2+, pH 7.2, 37°C


organism: Leishmania donovani

sequence_source: UniProtKB E9BIX7 direct REST lookup redirects to A0A3S7X0F5, release 2026_01

assay_conditions_summary: pH 8.5; 298.15 K; cofactor ATP


organism: Staphylococcus aureus

sequence_source: UniProtKB A0A0H2WZY4 direct REST lookup, release 2026_01

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0H2UP35 canonical sequence; Y126F reconstructed by replacing canonical residue 126 Y with F and applied mutation signature Y126F to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant His-tagged mutant Y126F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0H2UP35 and applied mutation signature M423A to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'M423A', pNP-beta-Glc6P column group: column 'Km (uM)' = 512; column 'kcat (s^-1)' = 168; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 3.3. The other three numeric cells of the same printed row belong to the Cellobiose-6'P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 512 uM; 512 / 1000 = 0.512 mM. kcat: printed Table 2 cell 168 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 3.3 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 3.3 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 330.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 168.0 / 0.512 = 328.125 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'M423A', pNP-beta-Glc6P column group: Km = 512 uM; kcat = 168 s^-1; printed kcat/Km = 3.3 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'M423A', the three pNP-beta-Glc6P cells (Km, kcat, kcat/Km x10^-1)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A0A0H2UP35 and applied mutation signature Y126F to reconstruct the assayed variant sequence.

column_label: Table 2 (Kinetic constants of BglA-2 and mutants toward pNP-beta-Glc6P and cellobiose-6'P), enzyme row 'Y126F', pNP-beta-Glc6P column group: column 'Km (uM)' = 598; column 'kcat (s^-1)' = 146; column 'kcat/Km x10^-1 (s^-1 uM^-1)' = 2.4. The other three numeric cells of the same printed row belong to the Cellobiose-6'P column group.

normalized_value_unit_evidence: Km: printed Table 2 cell 598 uM; 598 / 1000 = 0.598 mM. kcat: printed Table 2 cell 146 s^-1; already in s^-1, so no unit conversion applies. kcat/Km: printed Table 2 cell 2.4 in a column headed kcat/Km x10^-1 with unit s^-1 uM^-1, so the printed cell is 2.4 x 10^-1 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so the printed cell becomes 240.0 s^(-1)*mM^(-1), and the full-precision quotient of the same two printed cells is 146.0 / 0.598 = 244.14715719063545 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, enzyme row 'Y126F', pNP-beta-Glc6P column group: Km = 598 uM; kcat = 146 s^-1; printed kcat/Km = 2.4 x 10^-1 s^-1 uM^-1.

row_label: Table 2, enzyme row 'Y126F', the three pNP-beta-Glc6P cells (Km, kcat, kcat/Km x10^-1)


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A0H2UP35 canonical sequence; M423A reconstructed by replacing canonical residue 423 M with A and applied mutation signature M423A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 37°C, recombinant His-tagged mutant M423A


organism: Streptococcus pyogenes

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


substrate_name: 4-nitrophenyl 6-phospho-beta-glucoside

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

sequence_source: UniProtKB:Q99YP9 canonical sequence; RCSB 4B3K/4B3L/5FOO SIFTS mapping supports the same accession

proof_lines:
at pH 6.0 and 37°C
Raw SKiD Env: Temp=37°C, pH=6

source_databases_merged: brenda skid

substrate: 4-nitrophenyl 6-phospho-beta-glucoside


sequence_source: UniProtKB:Q9X108 reviewed canonical sequence; RCSB 1UP4/1UP6/1UP7 SIFTS mapping supports the same accession


enzyme_display_name: 8-amino-7-oxononanoate synthase

organism: Mycobacterium tuberculosis

sequence_source: UniProtKB reviewed accession P9WQ87; direct REST check on 2026-06-04; P0A4X4 is listed as a secondary accession of P9WQ87.

assay_conditions_summary: pH 7.7; 298.15 K; cofactor CoA

enzyme: 8-amino-7-oxononanoate synthase


substrate_name: 6-Carboxyhexanoyl-CoA; L-Alanine

sequence_source: UniProtKB reviewed accession P9WQ87; direct REST check on 2026-06-04.

assay_conditions_summary: cofactor CoA

substrate: 6-Carboxyhexanoyl-CoA; L-Alanine


substrate_name: L-Alanine

substrate: L-Alanine


substrate_name: D-Alanine

substrate: D-Alanine


organism: Thermus thermophilus

sequence_source: UniProtKB reviewed accession Q5SHZ8; direct REST check on 2026-06-04.


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

proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant E125A C-terminal His-tag


proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant N291A C-terminal His-tag


proof_lines: SABIO-RK modifier species: undecaprenyldiphospho-muramoylpentapeptide beta-N-acetylglucosaminyltransferase(Enzyme) mutant R260A C-terminal His-tag


enzyme_display_name: angiotensin-converting enzyme 2

sequence_source: UniProtKB reviewed accession Q9BYF1 direct lookup on 2026-06-04

proof_lines:
pH 6.5, room temperature
pH 7.4, 37°C
Ki above 0.01 mM

enzyme: angiotensin-converting enzyme 2


substrate_name: Angiotensin I

substrate: Angiotensin I


substrate_name: Dynorphin A (1-13)

substrate: Dynorphin A (1-13)


substrate_name: Angiotensin II

substrate: Angiotensin II


substrate_name: Neurotensin (1-8)

substrate: Neurotensin (1-8)


substrate_name: H2O; Angiotensin II

substrate: H2O; Angiotensin II


enzyme_display_name: adenosyl-fluoride synthase

organism: Nocardia brasiliensis

substrate_name: fluoride

sequence_source: UniProtKB W8JNL4 direct REST lookup; reviewed Swiss-Prot entry FLA_NOCB7, last annotation update 2026-01-28.

enzyme: adenosyl-fluoride synthase

substrate: fluoride


organism: Streptantibioticus cattleyicolor

sequence_source: UniProtKB Q70GK9 direct REST lookup; reviewed Swiss-Prot entry FLA_STRCT, last annotation update 2025-02-05.

proof_lines: 37°C, direct displacement reaction in the absence of L-methionine or S-adenosyl-L-methionine, pH not specified in the publication

proof_lines: about, during turnover, pH and temperature not specified in the publication


organism: Streptomyces cattleya

substrate_name: S-Adenosyl-L-methionine; F-

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

proof_lines:
Raw SKiD Env: Temp=26°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=-----
Raw SKiD Env: Temp=-----, pH=-----

substrate: S-Adenosyl-L-methionine; F-


organism: Streptomyces sp. MA37

substrate_name: S-adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB W0W999 direct REST lookup plus direct A279Y reconstruction from the canonical sequence. and applied mutation signature A279Y to reconstruct the assayed variant sequence.

proof_lines: mutant A279Y, pH not specified in the publication, temperature not specified in the publication

substrate: S-adenosyl-L-methionine


sequence_source: UniProtKB W0W999 direct REST lookup; reviewed Swiss-Prot entry FLA_STRSQ, last annotation update 2026-01-28.

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


sequence_variant_note: Resolved canonical sequence from UniProtKB W0W999 direct REST lookup plus direct F213Y/A279L reconstruction from the canonical sequence. and applied mutation signature F213Y/A279L to reconstruct the assayed variant sequence.

proof_lines: mutant F213Y/A279L, pH not specified in the publication, temperature not specified in the publication


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Streptomyces xinghaiensis

sequence_source: UniProtKB A0A068VNW5 direct REST lookup; unreviewed TrEMBL entry A0A068VNW5_9ACTN, last annotation update 2026-01-28.

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

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


substrate_name: angiotensin II

sequence_variant_note: Resolved canonical sequence from UniProt REST direct check for Q9BYF1 on 2026-06-04; R514Q reconstructed from the canonical sequence. and applied mutation signature R514Q to reconstruct the assayed variant sequence.

substrate: angiotensin II


sequence_source: UniProt REST direct check for Q9BYF1 on 2026-06-04.


substrate_name: hDPP4; MERS-CoV pseudovirus

substrate: hDPP4; MERS-CoV pseudovirus


substrate_name: hACE2; SARS-CoV-2 pseudovirus

substrate: hACE2; SARS-CoV-2 pseudovirus


substrate_name: hACE2; SARS-CoV pseudovirus

substrate: hACE2; SARS-CoV pseudovirus


organism: Mus musculus

substrate_name: Angiotensin II; H2O

sequence_source: UniProt REST direct check for Q8R0I0 on 2026-06-04.

substrate: Angiotensin II; H2O


enzyme_display_name: serine--glyoxylate transaminase

organism: Oryza sativa Japonica Group

substrate_name: L-serine

proof_lines:
cosubstrate pyruvate, pH 7.6, 30°C
cosubstrate glyoxylate, pH 7.6, 30°C
cosubstrate L-alanine, pH 7.6, 30°C

enzyme: serine--glyoxylate transaminase

substrate: L-serine


enzyme_display_name: rhodopsin kinase

organism: Bos taurus

substrate_name: rhodopsin

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with S5A reconstructed after residue check and applied mutation signature S5A to reconstruct the assayed variant sequence.

enzyme: rhodopsin kinase

substrate: rhodopsin


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with L166K reconstructed after residue check and applied mutation signature L166K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with D164A reconstructed after residue check and applied mutation signature D164A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with T8E reconstructed after residue check and applied mutation signature T8E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed P28327 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with D164A/L166K reconstructed after residue check and applied mutation signature D164A/L166K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed P28327 canonical sequence with T8A reconstructed after residue check and applied mutation signature T8A to reconstruct the assayed variant sequence.


substrate_name: ACE2; Spike glycoprotein

substrate: ACE2; Spike glycoprotein


substrate_name: N-Carbamoyl-beta-alanine

sequence_variant_note: Resolved canonical sequence from UniProtKB Q96W94 direct accession lookup plus selected-record mutation reconstruction and applied mutation signature E159A to reconstruct the assayed variant sequence.

substrate: N-Carbamoyl-beta-alanine


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96W94 direct accession lookup plus selected-record mutation reconstruction and applied mutation signature H262A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96W94 direct accession lookup plus selected-record mutation reconstruction and applied mutation signature R322A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96W94 direct accession lookup plus selected-record mutation reconstruction and applied mutation signature H397N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q96W94 direct accession lookup

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


organism: Rattus norvegicus

substrate_name: N-Carbamoyl-beta-alanine; H2O

sequence_source: UniProtKB Q03248 direct accession lookup

substrate: N-Carbamoyl-beta-alanine; H2O


organism: Zea mays

substrate_name: H2O; N-Carbamoyl-beta-alanine

sequence_source: UniProtKB B4FSZ8 direct accession lookup

substrate: H2O; N-Carbamoyl-beta-alanine


sequence_source: UniProtKB:A0A068VNW5 direct REST lookup on 2026-06-04


organism: Arabidopsis thaliana

substrate_name: ATP

sequence_source: UniProtKB:A1A6H3 direct REST lookup on 2026-06-04

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: pH 8.0, temperature not specified in the publication

substrate: ATP


organism: Homo sapiens

substrate_name: ATP; D-Ribose

sequence_source: UniProtKB:Q9H477 direct REST lookup on 2026-06-04

assay_conditions_summary: cofactor ATP

substrate: ATP; D-Ribose


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9H477 direct REST lookup on 2026-06-04 plus E202L reconstruction and applied mutation signature E202L to reconstruct the assayed variant sequence.

proof_lines: mutant E202L, presence of Mg2+, pH 7.2, 37°C


sequence_source: UniProtKB:Q9H477 direct REST lookup on 2026-06-04 plus E202L reconstruction


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9H477 direct REST lookup on 2026-06-04 plus N199L reconstruction and applied mutation signature N199L to reconstruct the assayed variant sequence.


substrate_name: D-ribose

sequence_source: UniProtKB:Q9H477 direct REST lookup on 2026-06-04 plus N199L reconstruction

substrate: D-ribose


substrate_name: Rhodopsin; ATP

sequence_source: UniProtKB:P28327 canonical FASTA direct lookup on 2026-06-04

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

substrate: Rhodopsin; ATP


organism: Danio rerio

sequence_source: UniProtKB:Q1XHM0 canonical FASTA direct lookup on 2026-06-04


sequence_source: UniProtKB:Q49HM9 canonical FASTA direct lookup on 2026-06-04


substrate_name: ATP; Rhodopsin

substrate: ATP; Rhodopsin


sequence_source: UniProtKB:Q15835 canonical FASTA direct lookup on 2026-06-04

assay_conditions_summary: pH 7; 303.15 K; cofactor ATP


sequence_source: UniProtKB:Q8WTQ7 canonical FASTA direct lookup on 2026-06-04


sequence_source: UniProt REST direct check for Q9M336 on 2026-06-04.


enzyme_display_name: Uracil phosphoribosyltransferase

organism: [Bacillus] caldolyticus

substrate_name: Uracil

sequence_source: UniProt REST direct check for P70881 on 2026-06-04.

assay_conditions_summary: pH 8

proof_lines:
Raw SKiD Env: Temp=-----, pH=8
Raw SKiD Env: Temp=-----, pH=-----

enzyme: Uracil phosphoribosyltransferase

substrate: Uracil


enzyme_display_name: Bifunctional protein PyrR

organism: Bacillus subtilis

substrate_name: Diphosphate; UMP

sequence_source: UniProt REST direct check for P39765 on 2026-06-04.

enzyme: Bifunctional protein PyrR

substrate: Diphosphate; UMP


substrate_name: UMP

substrate: UMP


organism: Escherichia coli

substrate_name: 5-Phospho-alpha-D-ribose 1-diphosphate

sequence_source: UniProt REST direct check for P0A8F0 on 2026-06-04.

substrate: 5-Phospho-alpha-D-ribose 1-diphosphate


sequence_variant_note: Resolved canonical sequence from UniProt REST direct check for P0A8F0 on 2026-06-04 plus direct P131D substitution reconstruction. and applied mutation signature P131D to reconstruct the assayed variant sequence.


enzyme_display_name: dimethylargininase

substrate_name: N(omega)-methyl-L-Arginine

sequence_source: UniProtKB:P56965 FASTA fetched during exact accession review

smiles: CN=C(N)NCCCC(N)C(=O)O

enzyme: dimethylargininase

substrate: N(omega)-methyl-L-Arginine


substrate_name: NG-monomethyl-L-arginine

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

substrate: NG-monomethyl-L-arginine


substrate_name: Nomega,Nomega-dimethyl-L-arginine

sequence_variant_note: Resolved canonical sequence from UniProtKB:O94760 FASTA with E78A reconstructed during review and applied mutation signature E78A to reconstruct the assayed variant sequence.

proof_lines: mutant E78A, pH 7.3, temperature not specified in the publication

substrate: Nomega,Nomega-dimethyl-L-arginine


substrate_name: S-methyl-L-thiocitrulline

sequence_source: UniProtKB:O94760 FASTA used only as canonical context

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 E78AA, pH 7.3, temperature not specified in the publication

substrate: S-methyl-L-thiocitrulline


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94760 FASTA with L30A reconstructed during review and applied mutation signature L30A to reconstruct the assayed variant sequence.

proof_lines: mutant L30A, pH 7.3, temperature not specified in the publication


sequence_source: UniProtKB:O94760 FASTA fetched during exact accession review

proof_lines: wild-type, pH 7.3, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:O94760 FASTA with L271G reconstructed during review and applied mutation signature L271G to reconstruct the assayed variant sequence.

proof_lines: mutant L271G, pH 7.3, temperature not specified in the publication


proof_lines: pH and temperature not specified in the publication


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB reviewed accession Q9I4E3 direct REST lookup, accessed 2026-06-04


substrate_name: H2O; NG,NG-Dimethyl-L-arginine

sequence_source: UniProtKB reviewed accession O08557 direct REST lookup, accessed 2026-06-04

substrate: H2O; NG,NG-Dimethyl-L-arginine


enzyme_display_name: thiamine-triphosphatase

substrate_name: thiamine triphosphate

sequence_source: UniProtKB reviewed accession Q8MKF1 direct REST lookup, accessed 2026-06-04

enzyme: thiamine-triphosphatase

substrate: thiamine triphosphate


sequence_source: UniProtKB reviewed accession Q9BU02 direct REST lookup, accessed 2026-06-04


proof_lines:
wild type enzyme
GST-fused wild type enzyme


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9BU02 direct REST lookup, accessed 2026-06-04 and applied mutation signature E63Q to reconstruct the assayed variant sequence.


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q9BU02 direct REST lookup, accessed 2026-06-04 and applied mutation signature E78K to reconstruct the assayed variant sequence.

substrate: Unknown


substrate_name: Thiamine triphosphate; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8JZL3 direct REST lookup, accessed 2026-06-04 and applied mutation signature K11A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant K11A His-tagged

substrate: Thiamine triphosphate; H2O


enzyme_display_name: arsenate reductase (thioredoxin)

substrate_name: arsenate

proof_lines: wild-type Bacillus subtilis, condition: 150 mM NaCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: wild-type Bacillus subtilis, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: wild-type Bacillus subtilis, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

enzyme: arsenate reductase (thioredoxin)

substrate: arsenate


organism: Bacillus thuringiensis


organism: Corynebacterium glutamicum


mutation_signature: N-terminally truncated mutant

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

mutation_type: truncation

proof_lines: N-terminally truncated mutant, pH 8.0, 37°C


organism: Staphylococcus aureus


substrate_name: Reduced thioredoxin; Arsenate

proof_lines: SABIO-RK modifier species: arsenate reductase (thioredoxin)(Enzyme) mutant ArsC C15A

proof_lines: pH 7.5, 37°C, mutant enzyme C15A, at 10 mM arsenate

substrate: Reduced thioredoxin; Arsenate


substrate_name: D-ribose

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9H477 canonical sequence plus selected-row mutation E202L and applied mutation signature E202L to reconstruct the assayed variant sequence.

substrate: D-ribose


substrate_name: ATP

substrate: ATP


organism: Brugia malayi

substrate_name: trehalose 6-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:A8NS89 canonical sequence plus selected-row mutation W280A and applied mutation signature W280A to reconstruct the assayed variant sequence.

substrate: trehalose 6-phosphate


enzyme_display_name: glucan 1,3-beta-glucosidase

organism: Candida albicans

substrate_name: Laminarin

sequence_variant_note: Resolved canonical sequence from UniProtKB:P29717 canonical sequence plus selected-row mutation F229A and applied mutation signature F229A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

enzyme: glucan 1,3-beta-glucosidase

substrate: Laminarin


organism: Cellulomonas fimi


organism: Hordeum vulgare

substrate_name: 4-nitrophenyl beta-D-glucoside

substrate: 4-nitrophenyl beta-D-glucoside


organism: Xanthomonas campestris

substrate_name: UDP-glucuronate

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8GCH2 and applied mutation signature K307A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.2; 293.15 K; buffer 75 mM MgCl2

column_label: Table 2 (Kinetic parameters for wild-type and mutant GumK), enzyme row 'K307A'; column 'Km UDPGlcA (uM)' = 440; column 'Vmax (pmol/ug min)' = 15.2; column 'Kcat (min^-1)' = 0.68. The table has no kcat/Km column.

normalized_value_unit_evidence: Km: printed Table 2 cell 440 uM; 1 uM is 1/1000 mM, so 440 / 1000 = 0.44 mM. kcat: printed Table 2 cell 0.68 min^-1; the printed turnover column is per minute, so 0.68 / 60 = 0.011333333333333334 s^(-1). Vmax: printed Table 2 cell 15.2 pmol/ug min; 1 pmol/(ug min) is 0.000000000001 mol per 0.000001 g per 60 s, so 15.2 / 60 x 0.000001 = 0.00000025333333333333327 mol*s^(-1)*g^(-1). kcat/Km: Table 2 prints no efficiency cell, so the same-measurement quotient of the two printed cells is 0.011333333333333334 / 0.44 = 0.02575757575757576 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, row K307A: column 'Km UDPGlcA (uM)' printed 440; column 'Vmax (pmol/ug min)' printed 15.2; column 'Kcat (min^-1)' printed 0.68. Table 2 carries no catalytic efficiency column.

row_label: Table 2, row K307A, donor UDP-GlcA columns

table_label: Table 2: Kinetic parameters for wild-type and mutant GumK (J. Biol. Chem. 2008, 283(36):25027-25035)

substrate: UDP-glucuronate

status: corrected


enzyme_display_name: uracil phosphoribosyltransferase

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A8F0; direct REST/FASTA lookup 2026-06-04 and applied mutation signature P131D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: uracil phosphoribosyltransferase(Enzyme) mutant P131D

enzyme: uracil phosphoribosyltransferase


substrate_name: 5-Phospho-alpha-D-ribose 1-diphosphate

sequence_source: UniProtKB reviewed accession P0A8F0; direct REST/FASTA lookup 2026-06-04

substrate: 5-Phospho-alpha-D-ribose 1-diphosphate


organism: Toxoplasma gondii

substrate_name: 5-phospho-alpha-D-ribose 1-diphosphate

sequence_source: UniProtKB reviewed accession Q26998; direct REST/FASTA 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:
recombinant wild-type, with GTP
recombinant wild-type, without GTP

substrate: 5-phospho-alpha-D-ribose 1-diphosphate


substrate_name: Glyoxylate; L-Serine

sequence_source: UniProtKB reviewed accession Q56YA5; direct REST/FASTA lookup 2026-06-04

proof_lines:
at 10 mM glyoxylate
cosubstrate glyoxylate, pH 8.0, 30°C
at 30 mM L-alanine

substrate: Glyoxylate; L-Serine


substrate_name: L-Serine

substrate: L-Serine


substrate_name: L-Alanine

substrate: L-Alanine


sequence_source: UniProt REST P0A006 canonical sequence checked 2026-06-04

proof_lines:
high affinity
pH 7.5, 37°C
Raw SKiD Env: Temp=-----, pH=-----


proof_lines: wild-type Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: wild-type Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: wild-type Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A006 canonical sequence with H62Q substitution reconstructed during worker review and applied mutation signature H62Q to reconstruct the assayed variant sequence.

proof_lines: H62Q mutant Staphylococcus aureus, condition: 150 mM KCl, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: H62Q mutant Staphylococcus aureus, condition: 50 mM Na2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters

proof_lines: H62Q mutant Staphylococcus aureus, condition: 50 mM K2SO4, study about the impact of potassium and the tetrahedral oxyanion sulfate on the steady-state kinetic parameters


sequence_variant_note: Resolved canonical sequence from UniProt REST Q8GCH2 canonical sequence with Q310A substitution reconstructed during worker review and applied mutation signature Q310A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q8GCH2 canonical sequence with E192A substitution reconstructed during worker review and applied mutation signature E192A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant E192A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProt REST Q8GCH2 canonical sequence with D234A substitution reconstructed during worker review and applied mutation signature D234A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant D234A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProt REST Q8GCH2 canonical sequence with E272A substitution reconstructed during worker review and applied mutation signature E272A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant E272A His-tagged


organism: Rhizomucor miehei

substrate_name: cellobiose

substrate: cellobiose


column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row ONPG-6-P; the Michaelis constant 0.6 comes from the printed column K_m (mM), the turnover number 11 from the printed column k_cat (1/s), and the catalytic efficiency 1.9 x 10^4 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.6 mM; already in mM, no unit conversion applies; the exported value is 0.6 mM. kcat: printed cell 11 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 11.0 s^(-1). kcat/Km: printed cell 1.9 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.9 x 10^4 / 1000 = 19.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 18.333333333333336 s^(-1)*mM^(-1), the quotient 11 / 0.6 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 19.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row ONPG-6-P: Km = 0.6 mM; kcat = 11 1/s; printed kcat/Km = 1.9 x 10^4 M^-1 s^-1.


column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row ONPGlc-6-P; the Michaelis constant 0.06 comes from the printed column K_m (mM), the turnover number 70 from the printed column k_cat (1/s), and the catalytic efficiency 1.16 x 10^6 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.06 mM; already in mM, no unit conversion applies; the exported value is 0.06 mM. kcat: printed cell 70 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 70.0 s^(-1). kcat/Km: printed cell 1.16 x 10^6 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.16 x 10^6 / 1000 = 1160.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 1166.6666666666667 s^(-1)*mM^(-1), the quotient 70 / 0.06 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 1160.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row ONPGlc-6-P: Km = 0.06 mM; kcat = 70 1/s; printed kcat/Km = 1.16 x 10^6 M^-1 s^-1.


column_label: Table I: Substrate specificities of 6-phospho-beta-glycosidases (Protein Engineering 1993, 6(8):913-920); printed column heads Enzyme | Substrate | K_m (mM) | k_cat (1/s) | k_cat/K_m [1/(s M)]; Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row PNPGlc-6-P; the Michaelis constant 0.08 comes from the printed column K_m (mM), the turnover number 58 from the printed column k_cat (1/s), and the catalytic efficiency 7.29 x 10^5 from the printed column k_cat/K_m [1/(s M)], whose unit is M^-1 s^-1.

normalized_value_unit_evidence: Km: printed cell 0.08 mM; already in mM, no unit conversion applies; the exported value is 0.08 mM. kcat: printed cell 58 1/s; 1/s is the canonical s^(-1), so no unit conversion applies; the exported value is 58.0 s^(-1). kcat/Km: printed cell 7.29 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.29 x 10^5 / 1000 = 729.0 s^(-1)*mM^(-1). The value carried by this identity for kcat_over_km is 725.0 s^(-1)*mM^(-1), the quotient 58 / 0.08 of the two printed component cells; the paper's own printed efficiency cell is the independently fitted value 729.0 s^(-1)*mM^(-1), and this record proposes that printed cell.

raw_value_unit_evidence: Table I, enzyme block 6-Phospho-beta-glucosidase B E.coli, substrate row PNPGlc-6-P: Km = 0.08 mM; kcat = 58 1/s; printed kcat/Km = 7.29 x 10^5 M^-1 s^-1.


substrate_name: beta-Casomorphin

substrate: beta-Casomorphin


organism: SARS coronavirus

substrate_name: ACE2; Spike glycoprotein RBD-SD1

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

substrate: ACE2; Spike glycoprotein RBD-SD1


organism: Bos taurus

substrate_name: H2O; NG,NG-Dimethyl-L-arginine

proof_lines: in the presence of 5 mM EDTA, at pH 7.3 and 37°C

substrate: H2O; NG,NG-Dimethyl-L-arginine


organism: Hyphomicrobium methylovorum


organism: Methylococcus capsulatus

substrate_name: L-alanine

proof_lines: pH 7.5, temperature not specified in the publication, recombinant enzyme, with glyoxylate

proof_lines: pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-serine

proof_lines: pH 7.5, temperature not specified in the publication, recombinant enzyme, with L-alanine

substrate: L-alanine


organism: Methylotuvimicrobium alcaliphilum

substrate_name: glyoxylate

substrate: glyoxylate


organism: Homo sapiens

substrate_name: Rhodopsin; ATP

substrate: Rhodopsin; ATP


substrate_name: ATP

substrate: ATP


substrate_name: cellotriose

substrate: cellotriose


substrate_name: gentobiose

substrate: gentobiose


substrate_name: cellotetraose

substrate: cellotetraose


substrate_name: NG,NG-Dimethyl-L-arginine

sequence_source: UniProtKB:P56965 reviewed Swiss-Prot direct lookup

substrate: NG,NG-Dimethyl-L-arginine


organism: Mus musculus

substrate_name: thiamine triphosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus W53A reconstruction and applied mutation signature W53A to reconstruct the assayed variant sequence.

substrate: thiamine triphosphate


sequence_source: UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus K65A reconstruction and applied mutation signature K65A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus Y79A reconstruction and applied mutation signature Y79A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus K11A reconstruction and applied mutation signature K11A to reconstruct the assayed variant sequence.


substrate_name: Thiamine triphosphate; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus D37A reconstruction and applied mutation signature D37A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant D37A His-tagged

substrate: Thiamine triphosphate; H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8JZL3 reviewed Swiss-Prot direct lookup plus E81A reconstruction and applied mutation signature E81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04; D207A reconstructed after confirming residue 207 is D. and applied mutation signature D207A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant D207A His-tagged


substrate_name: UDP-glucuronate

sequence_source: UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04.

substrate: UDP-glucuronate


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04; M231A reconstructed after confirming residue 231 is M. and applied mutation signature M231A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04; Y292A reconstructed after confirming residue 292 is Y. and applied mutation signature Y292A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04; K307A reconstructed after confirming residue 307 is K. and applied mutation signature K307A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant K307A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8GCH2 canonical FASTA fetched 2026-06-04; E272A reconstructed after confirming residue 272 is E. and applied mutation signature E272A 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 UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; Y39A sequence reconstructed from the canonical sequence. and applied mutation signature Y39A to reconstruct the assayed variant sequence.


substrate_name: H2O; Thiamine triphosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; K65A sequence reconstructed from the canonical sequence. and applied mutation signature K65A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant K65A His-tagged

substrate: H2O; Thiamine triphosphate


sequence_source: UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; Y39A sequence reconstructed from the canonical sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant Y39A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; D37A sequence reconstructed from the canonical sequence. and applied mutation signature D37A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; Y79A sequence reconstructed from the canonical sequence. and applied mutation signature Y79A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant Y79A His-tagged


sequence_source: UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04.


substrate_name: Triphosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; W53A sequence reconstructed from the canonical sequence. and applied mutation signature W53A to reconstruct the assayed variant sequence.

substrate: Triphosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q8JZL3 direct accession FASTA/JSON check on 2026-06-04; K193A sequence reconstructed from the canonical sequence. and applied mutation signature K193A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession Q8JZL3

proof_lines:
Raw SKiD Env: Temp=37°C, pH=8.5
Raw SKiD Env: Temp=-----, pH=-----


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8JZL3 plus selected mutation_signature K193A reconstruction and applied mutation signature K193A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant K193A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8JZL3 plus selected mutation_signature E81A reconstruction and applied mutation signature E81A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant E81A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8JZL3 plus selected mutation_signature W53A reconstruction and applied mutation signature W53A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant W53A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q8JZL3 plus selected mutation_signature D147A reconstruction and applied mutation signature D147A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: thiamine-triphosphatase(Enzyme) mutant D147A His-tagged


sequence_source: UniProtKB reviewed accession Q8JZL3 plus selected mutation_signature D147A reconstruction


enzyme_display_name: 2-hydroxy-dATP diphosphatase

sequence_source: UniProtKB reviewed accession P36639

enzyme: 2-hydroxy-dATP diphosphatase


sequence_source: UniProtKB reviewed accession P36639 direct REST/FASTA lookup


substrate_name: dGTP

substrate: dGTP


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P36639 direct REST/FASTA lookup plus D119A substitution reconstruction and applied mutation signature D119A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P36639 direct REST/FASTA lookup plus F27A substitution reconstruction and applied mutation signature F27A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P36639 direct REST/FASTA lookup plus F27A substitution reconstruction


sequence_source: UniProtKB:P36639 direct lookup

sequence_variant_note: Resolved canonical sequence from UniProtKB:P36639 direct lookup and applied mutation signature D119A to reconstruct the assayed variant sequence.


substrate_name: 8-oxo-dGTP; H2O

proof_lines: at pH 7.4, temperature not specified in the publication

substrate: 8-oxo-dGTP; H2O


sequence_source: UniProtKB:Q8BG93 direct lookup

proof_lines: pH and temperature not specified in the publication


enzyme_display_name: oxaloacetate decarboxylase

organism: Enterococcus faecalis

substrate_name: oxaloacetate

sequence_source: UniProtKB:Q82YW6 direct lookup

proof_lines: calculated value at pH 4.5, temperature not specified in the publication

enzyme: oxaloacetate decarboxylase

substrate: oxaloacetate


substrate_name: Oxaloacetate

sequence_source: UniProtKB:P48163 direct lookup

substrate: Oxaloacetate


sequence_source: UniProtKB:Q6P587 direct lookup


enzyme_display_name: pyridoxal phosphatase

substrate_name: Pyridoxal phosphate; H2O

sequence_source: UniProtKB reviewed entry Q96GD0 direct REST lookup

proof_lines:
pH 7.4, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=7.4

enzyme: pyridoxal phosphatase

substrate: Pyridoxal phosphate; H2O


substrate_name: Pyridoxamine phosphate

substrate: Pyridoxamine phosphate


substrate_name: Pyridoxine phosphate

substrate: Pyridoxine phosphate


substrate_name: Pyridoxal phosphate

substrate: Pyridoxal phosphate


substrate_name: H2O; Pyridoxal phosphate

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

substrate: H2O; Pyridoxal phosphate


substrate_name: pyridoxal 5'-phosphate

sequence_source: UniProtKB reviewed entry P60487 direct REST lookup

substrate: pyridoxal 5'-phosphate


proof_lines:
pH 7.4, 22°C
Raw SKiD Env: Temp=22°C, pH=7.4


organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed entry F4KEV7 direct REST lookup from source accession Q9LVM4

proof_lines:
pH 6.8, 30°C
pH 6.8, 30°C, in presence of Mg2+


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P49789 and applied mutation signature H96G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 5.8; 299.65 K; cofactor NADH

column_label: Table 2: Kinetic Parameters for Catalysis by H96G-Fhit (Biochemistry 2004, 43(23):7637-7642); Table 2, substrate row 'AMP-Im' (footnote a); column 'substrate'; column 'kcat (s-1)'; column 'Km (uM)'; column 'kcat/Km (M-1 s-1)'; the printed cells for this row are kcat 0.91 s-1, Km 26 uM and kcat/Km 3.5 x 10^4 M-1 s-1.

normalized_value_unit_evidence: kcat: printed cell 0.91 s-1; already in s^-1, no unit conversion applies; normalized value 0.91 s^(-1). Km: printed cell 26 uM; 1 uM is 0.001 mM, so 26 / 1000 = 0.026 mM; normalized value 0.026 mM. kcat/Km: printed cell 3.5 x 10^4 M-1 s-1 = 35000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 35000 / 1000 = 35 s^-1 mM^-1; normalized value 35 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2, substrate row 'AMP-Im': kcat = 0.91 s-1; Km = 26 uM; printed kcat/Km = 3.5 x 10^4 M-1 s-1.


sequence_source: UniProtKB:P49789 canonical FASTA

assay_conditions_summary: pH 7; 299.65 K; cofactor NADH

column_label: Table 3: Kinetic Parameters for Catalysis by Wild-Type Fhit (Biochemistry 2004, 43(23):7637-7642); Table 3, substrate row 'AMP-Im' (footnote a); column 'substrate'; column 'kcat (s-1)'; column 'Km (uM)'; column 'kcat/Km (M-1 s-1)'; the printed cells for this row are kcat 4.4 s-1, Km 6.2 uM and kcat/Km 6.4 x 10^5 M-1 s-1.

normalized_value_unit_evidence: kcat: printed cell 4.4 s-1; already in s^-1, no unit conversion applies; normalized value 4.4 s^(-1). Km: printed cell 6.2 uM; 1 uM is 0.001 mM, so 6.2 / 1000 = 0.0062 mM; normalized value 0.0062 mM. kcat/Km: printed cell 6.4 x 10^5 M-1 s-1 = 640000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 640000 / 1000 = 640 s^-1 mM^-1; normalized value 640 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row 'AMP-Im': kcat = 4.4 s-1; Km = 6.2 uM; printed kcat/Km = 6.4 x 10^5 M-1 s-1.


substrate_name: P1,P3-Bis(5'-adenosyl) triphosphate

assay_conditions_summary: pH 7.3; 299.65 K; cofactor ADP

column_label: Table 3: Kinetic Parameters for Catalysis by Wild-Type Fhit (Biochemistry 2004, 43(23):7637-7642); Table 3, substrate row 'Ap3A' (footnote b); column 'substrate'; column 'kcat (s-1)'; column 'Km (uM)'; column 'kcat/Km (M-1 s-1)'; the printed cells for this row are kcat 3.5 s-1, Km 2.9 uM and kcat/Km 11.6 x 10^5 M-1 s-1.

normalized_value_unit_evidence: kcat: printed cell 3.5 s-1; already in s^-1, no unit conversion applies; normalized value 3.5 s^(-1). Km: printed cell 2.9 uM; 1 uM is 0.001 mM, so 2.9 / 1000 = 0.0029 mM; normalized value 0.0029 mM. kcat/Km: printed cell 11.6 x 10^5 M-1 s-1 = 1160000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1160000 / 1000 = 1160 s^-1 mM^-1; normalized value 1160 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row 'Ap3A': kcat = 3.5 s-1; Km = 2.9 uM; printed kcat/Km = 11.6 x 10^5 M-1 s-1.

substrate: P1,P3-Bis(5'-adenosyl) triphosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P49789 canonical FASTA with H96G reconstruction and applied mutation signature H96G to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: bis(5'-adenosyl)-triphosphatase(Enzyme) mutant H96G Fhit


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

assay_conditions_summary: pH 7.3; 299.65 K; cofactor NADH

column_label: Table 3: Kinetic Parameters for Catalysis by Wild-Type Fhit (Biochemistry 2004, 43(23):7637-7642); Table 3, substrate row 'AMP-N-MeIm' (footnote b); column 'substrate'; column 'kcat (s-1)'; column 'Km (uM)'; column 'kcat/Km (M-1 s-1)'; the printed cells for this row are kcat 4.2 s-1, Km 5.3 uM and kcat/Km 7.2 x 10^5 M-1 s-1.

normalized_value_unit_evidence: kcat: printed cell 4.2 s-1; already in s^-1, no unit conversion applies; normalized value 4.2 s^(-1). Km: printed cell 5.3 uM; 1 uM is 0.001 mM, so 5.3 / 1000 = 0.0053 mM; normalized value 0.0053 mM. kcat/Km: printed cell 7.2 x 10^5 M-1 s-1 = 720000 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 720000 / 1000 = 720 s^-1 mM^-1; normalized value 720 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3, substrate row 'AMP-N-MeIm': kcat = 4.2 s-1; Km = 5.3 uM; printed kcat/Km = 7.2 x 10^5 M-1 s-1.


sequence_source: UniProtKB:P49789 canonical FASTA with H96G reconstruction


assay_conditions_summary: pH 6.8; 310.15 K; cofactor ADP

proof_lines: nonphosphorylated recombinant enzyme, pH 6.8, 37°C

proof_lines: monophosphorylated recombinant enzyme, pH 6.8, 37°C

proof_lines: diphosphorylated recombinant enzyme, pH 6.8, 37°C


enzyme_display_name: glutamate 5-kinase

organism: Escherichia coli

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with D170A and applied mutation signature D170A to reconstruct the assayed variant sequence.

enzyme: glutamate 5-kinase

substrate: ATP


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with K217A and applied mutation signature K217A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with N149A and applied mutation signature N149A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with D148A and applied mutation signature D148A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with D170N and applied mutation signature D170N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P0A7B5 canonical sequence reconstructed with T169A and applied mutation signature T169A to reconstruct the assayed variant sequence.


substrate_name: ATP; L-Glutamate

substrate: ATP; L-Glutamate


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: glutamate 5-kinase(Enzyme) mutant ProB (3,4-dehydroproline resistant)


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed E272D variant and applied mutation signature E272D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant E272D His-tagged


sequence_source: UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed E272D variant


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed Q310A variant and applied mutation signature Q310A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant Q310A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed E192A variant and applied mutation signature E192A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed D234A variant and applied mutation signature D234A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed M231A variant and applied mutation signature M231A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant M231A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed Y292A variant and applied mutation signature Y292A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: D-Man-alpha-(1->3)-D-Glc-beta-(1->4)-D-Glc-alpha-1-diphosphoundecaprenol 2-beta-glucuronyltransferase(Enzyme) mutant Y292A His-tagged


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8GCH2 reviewed canonical sequence with reconstructed D207A variant and applied mutation signature D207A to reconstruct the assayed variant sequence.


enzyme_display_name: adenosylmethionine decarboxylase

substrate_name: S-Adenosyl-L-methionine

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q96286 and applied mutation signature C230A to reconstruct the assayed variant sequence.

column_label: Table III: Kinetic parameters of wild type and mutant AdoMetDC (J. Biochem. 1999, 126(6):996-1003), AdoMet substrate; printed column heads Constructs | pH optimum | Km (uM) | Vmax (uM/min-mg) | kcat (min-1) | kcat/Km (uM-1 min-1). Table III, C230A row; column Km (uM) = 25; column kcat (min-1) = 2900; column kcat/Km (uM-1 min-1) = 116.

normalized_value_unit_evidence: Km: printed Table III cell 25 uM; 1 uM is 1/1000 mM, so 25 / 1000 = 0.025 mM. kcat: printed Table III cell 2900 min-1; 1 min-1 is 1/60 s-1, so 2900 / 60 rounds to 48.333 s^(-1). kcat/Km: printed Table III cell 116 uM-1 min-1; 1 uM-1 min-1 is 1000/60 s-1 mM-1, so 116 x 1000 / 60 = 1933.3333333333335 s^(-1)*mM^(-1), against the catalog value 1933.32.

raw_value_unit_evidence: Table III, C230A row: Km = 25 uM; kcat = 2900 min-1; printed kcat/Km = 116 uM-1 min-1.

row_label: Table III, C230A row

enzyme: adenosylmethionine decarboxylase

substrate: S-Adenosyl-L-methionine


sequence_source: UniProtKB Q96286 reviewed REST lookup on 2026-06-04.

column_label: Table III: Kinetic parameters of wild type and mutant AdoMetDC (J. Biochem. 1999, 126(6):996-1003), AdoMet substrate; printed column heads Constructs | pH optimum | Km (uM) | Vmax (uM/min-mg) | kcat (min-1) | kcat/Km (uM-1 min-1). Table III, Wild Type row; column Km (uM) = 23.1; column kcat (min-1) = 2750; column kcat/Km (uM-1 min-1) = 119.

raw_value_unit_evidence: Table III, Wild Type row: Km = 23.1 uM; kcat = 2750 min-1; printed kcat/Km = 119 uM-1 min-1.

row_label: Table III, Wild Type row


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q96286 and applied mutation signature C83A to reconstruct the assayed variant sequence.

column_label: Table III: Kinetic parameters of wild type and mutant AdoMetDC (J. Biochem. 1999, 126(6):996-1003), AdoMet substrate; printed column heads Constructs | pH optimum | Km (uM) | Vmax (uM/min-mg) | kcat (min-1) | kcat/Km (uM-1 min-1). Table III, C83A row; column Km (uM) = 42.7; column Vmax (uM/min-mg) = 3.98; column kcat (min-1) = 110.

raw_value_unit_evidence: Table III, C83A row: Km = 42.7 uM; Vmax = 3.98 uM/min-mg; kcat = 110 min-1; printed kcat/Km = 2.7 uM-1 min-1 (informational; this export row does not carry a kcat_over_km metric).

row_label: Table III, C83A row


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q96286 and applied mutation signature K81A to reconstruct the assayed variant sequence.

column_label: Table III: Kinetic parameters of wild type and mutant AdoMetDC (J. Biochem. 1999, 126(6):996-1003), AdoMet substrate; printed column heads Constructs | pH optimum | Km (uM) | Vmax (uM/min-mg) | kcat (min-1) | kcat/Km (uM-1 min-1). Table III, K81A row; column Km (uM) = 252.3; column kcat (min-1) = 1640; column kcat/Km (uM-1 min-1) = 6.5.

raw_value_unit_evidence: Table III, K81A row: Km = 252.3 uM; kcat = 1640 min-1; printed kcat/Km = 6.5 uM-1 min-1.

row_label: Table III, K81A row


substrate_name: L-Lysine

sequence_source: UniProtKB Q96286 reviewed REST lookup on 2026-06-04; canonical sequence preserved as accession context because no mutation_signature is present.

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

substrate: L-Lysine


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q96286 and applied mutation signature C50A to reconstruct the assayed variant sequence.

column_label: Table III: Kinetic parameters of wild type and mutant AdoMetDC (J. Biochem. 1999, 126(6):996-1003), AdoMet substrate; printed column heads Constructs | pH optimum | Km (uM) | Vmax (uM/min-mg) | kcat (min-1) | kcat/Km (uM-1 min-1). Table III, C50A row; column Km (uM) = 22.8; column kcat (min-1) = 2690; column kcat/Km (uM-1 min-1) = 118.

raw_value_unit_evidence: Table III, C50A row: Km = 22.8 uM; kcat = 2690 min-1; printed kcat/Km = 118 uM-1 min-1.

row_label: Table III, C50A row


sequence_variant_note: Resolved canonical sequence from UniProtKB Q96286 reviewed REST lookup on 2026-06-04; K81A variant reconstructed from canonical sequence after residue check. and applied mutation signature K81A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: adenosylmethionine decarboxylase(Enzyme) mutant K81A


column_label: Table III: Kinetic parameters of wild type and mutant AdoMetDC (J. Biochem. 1999, 126(6):996-1003), AdoMet substrate; printed column heads Constructs | pH optimum | Km (uM) | Vmax (uM/min-mg) | kcat (min-1) | kcat/Km (uM-1 min-1). Table III, C83A row; column Km (uM) = 42.7; column kcat (min-1) = 110; column kcat/Km (uM-1 min-1) = 2.7.

raw_value_unit_evidence: Table III, C83A row: Km = 42.7 uM; kcat = 110 min-1; printed kcat/Km = 2.7 uM-1 min-1.


organism: Leishmania donovani

sequence_source: UniProtKB A0A0R6Y3I5 direct REST check on 2026-06-04

assay_conditions_summary: pH 7.4; 355.15 K; cofactor ATP


substrate_name: L-Glutamate; ATP

assay_conditions_summary: pH 7.4; cofactor ATP

substrate: L-Glutamate; ATP


substrate_name: L-glutamate

substrate: L-glutamate


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB P9WHU9 direct REST check on 2026-06-04


organism: Vigna aconitifolia

sequence_variant_note: Resolved canonical sequence from UniProtKB P32296 direct REST check on 2026-06-04 plus one-based F129A reconstruction from SABIO-RK mutation note and applied mutation signature F129A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutamate 5-kinase(Enzyme) mutant F129A


sequence_variant_note: Resolved canonical sequence from UniProtKB P32296 direct REST check on 2026-06-04 plus one-based D126A reconstruction from SABIO-RK mutation note and applied mutation signature D126A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: glutamate 5-kinase(Enzyme) mutant D126A


sequence_source: UniProtKB P32296 direct REST check on 2026-06-04


sequence_source: UniProtKB Q9Y6X5 direct REST check on 2026-06-04

proof_lines: capillary electrophoresis assay, pH not specified in the publication, 37°C


organism: Rattus norvegicus

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


organism: Saccharomyces cerevisiae

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


proof_lines: SABIO-RK modifier species: oxaloacetate decarboxylase(Enzyme) mutant R336Q


proof_lines: SABIO-RK modifier species: oxaloacetate decarboxylase(Enzyme) mutant R336K


column_label: Table III: Kinetic parameters of wild type and mutant AdoMetDC (J. Biochem. 1999, 126(6):996-1003), AdoMet substrate; printed column heads Constructs | pH optimum | Km (uM) | Vmax (uM/min-mg) | kcat (min-1) | kcat/Km (uM-1 min-1). Table III, C50A row; column Km (uM) = 22.8; column Vmax (uM/min-mg) = 98; column kcat (min-1) = 2690.

raw_value_unit_evidence: Table III, C50A row: Km = 22.8 uM; Vmax = 98 uM/min-mg; kcat = 2690 min-1; printed kcat/Km = 118 uM-1 min-1 (informational; this export row does not carry a kcat_over_km metric).


column_label: Table III: Kinetic parameters of wild type and mutant AdoMetDC (J. Biochem. 1999, 126(6):996-1003), AdoMet substrate; printed column heads Constructs | pH optimum | Km (uM) | Vmax (uM/min-mg) | kcat (min-1) | kcat/Km (uM-1 min-1). Table III, C230A row; column Km (uM) = 25; column Vmax (uM/min-mg) = 105.6; column kcat (min-1) = 2900.

normalized_value_unit_evidence: Km: printed Table III cell 25 uM; 1 uM is 1/1000 mM, so 25 / 1000 = 0.025 mM. kcat: printed Table III cell 2900 min-1; 1 min-1 is 1/60 s-1, so 2900 / 60 = 48.33333 s^(-1). Vmax: printed Table III cell 105.6 uM/min-mg (umol per min per mg protein); 1 umol is 0.000001 mol, 1/min is 1/60 s^-1, and 1/mg is 1000/g, so 105.6 x 0.000001 / 60 x 1000 = 0.00176 M*s^(-1)*g^(-1).

raw_value_unit_evidence: Table III, C230A row: Km = 25 uM; Vmax = 105.6 uM/min-mg; kcat = 2900 min-1; printed kcat/Km = 116 uM-1 min-1 (informational; this export row does not carry a kcat_over_km metric).


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature D148N to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature D150N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature G51A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature K10A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature M214A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature K217R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P0A7B5 checked by UniProt REST on 2026-06-04 and applied mutation signature T169S to reconstruct the assayed variant sequence.


enzyme_display_name: Histidinol-phosphate aminotransferase

organism: Corynebacterium glutamicum

substrate_name: L-phenylalanine

sequence_variant_note: Resolved canonical sequence from uniprot:Q9KJU4 and applied mutation signature Y123F to reconstruct the assayed variant sequence.

enzyme: Histidinol-phosphate aminotransferase

substrate: L-phenylalanine


sequence_variant_note: Resolved canonical sequence from uniprot:Q9KJU4 and applied mutation signature Y21F to reconstruct the assayed variant sequence.


substrate_name: L-leucine

sequence_variant_note: Resolved canonical sequence from uniprot:Q9KJU4 and applied mutation signature Y257F to reconstruct the assayed variant sequence.

substrate: L-leucine


substrate_name: L-histidinol phosphate

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

substrate: L-histidinol phosphate


sequence_variant_note: Resolved canonical sequence from uniprot:Q9KJU4 and applied mutation signature N99D to reconstruct the assayed variant sequence.


substrate_name: L-tyrosine

substrate: L-tyrosine


sequence_source: UniProtKB REST direct lookup, accession P0A7F6


sequence_source: UniProtKB REST direct lookup, accession P17707


organism: Methanocaldococcus jannaschii

sequence_source: UniProtKB REST direct lookup, accession Q57763


organism: Saccharolobus solfataricus

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB REST direct lookup, accession Q9UWY8

substrate: S-adenosyl-L-methionine


organism: Streptomyces griseochromogenes

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup, accession Q841K9; M37Y reconstructed from canonical residue 37 and applied mutation signature M37Y to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; buffer condition '50 mM HEPES

proof_lines: mutant enzyme M37Y, in 50 mM HEPES buffer (pH 8.0), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup, accession Q841K9; M37F reconstructed from canonical residue 37 and applied mutation signature M37F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M37F, in 50 mM HEPES buffer (pH 8.0), at 25°C


sequence_source: UniProtKB REST direct lookup, accession Q841K9; M37Y reconstructed from canonical residue 37


sequence_source: UniProt REST Q841K9, unreviewed TrEMBL blsE entry

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM HEPES

proof_lines: wild type enzyme, in 50 mM HEPES buffer (pH 8.0), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt REST Q841K9 plus direct M37W reconstruction and applied mutation signature M37W to reconstruct the assayed variant sequence.


sequence_source: UniProt REST Q841K9 plus direct M37W reconstruction

proof_lines: mutant enzyme M37W, in 50 mM HEPES buffer (pH 8.0), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProt REST Q841K9 plus direct M37F reconstruction and applied mutation signature M37F to reconstruct the assayed variant sequence.


organism: Sulfolobus solfataricus

sequence_source: UniProt REST Q9UWY8, reviewed Swiss-Prot SPEH_SACS2


organism: Thermotoga maritima

sequence_source: UniProt REST Q9WZC3, reviewed Swiss-Prot SPEH_THEMA


proof_lines:
at pH 6.8 and 65°C
Raw SKiD Env: Temp=65°C, pH=6.8


substrate_name: NAD+; H2O; N6-Acetyl-L-lysyl peptide

assay_conditions_summary: cofactor NAD+

substrate: NAD+; H2O; N6-Acetyl-L-lysyl peptide


substrate_name: [histone H3]-N6-myristoyl-L-lysine9

proof_lines: pH 7.5, temperature not specified in the publication

substrate: [histone H3]-N6-myristoyl-L-lysine9


substrate_name: NAD+

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

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NAD+

substrate: NAD+


substrate_name: acetylated Acetyl-CoA synthetase; H2O; NAD+


organism: Plasmodium falciparum

substrate_name: acetylated Histone H3-peptide; NAD+; H2O


substrate_name: acetylated p300-peptide; NAD+; H2O

substrate: acetylated p300-peptide; NAD+; H2O


substrate_name: H2O; NAD+

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines: Km above 10 1/sec*mM, at pH 8.0 and 37°C

substrate: H2O; NAD+


substrate_name: acetylated Histone H3-peptide; NAD+; Methanol


substrate_name: L-Phenylalanine

sequence_source: UniProtKB reviewed entry P9WML7, sequence version 1, retrieved 2026-06-04

substrate: L-Phenylalanine


substrate_name: L-Phenylalanine; 2-Oxoglutarate

sequence_source: UniProtKB reviewed entry Q9X0D0, sequence version 1, retrieved 2026-06-04

proof_lines:
pH 8.0, 25°C
pH 8.0, 20°C
Raw SKiD Env: Temp=25°C, pH=8

substrate: L-Phenylalanine; 2-Oxoglutarate


substrate_name: L-Histidinol phosphate

substrate: L-Histidinol phosphate


substrate_name: L-Tryptophan

substrate: L-Tryptophan


substrate_name: L-Tyrosine

substrate: L-Tyrosine


organism: Zymomonas mobilis

substrate_name: 2-Oxoglutarate; L-Histidinol phosphate

sequence_source: UniProtKB reviewed entry P34037, sequence version 3, retrieved 2026-06-04

substrate: 2-Oxoglutarate; L-Histidinol phosphate


sequence_source: UniProtKB reviewed entry P49775, sequence version 2, retrieved 2026-06-04


substrate_name: acetylated Histone H4-peptide; H2O; NAD+


substrate_name: acetylated Histone H4-peptide; NAD+; H2O


sequence_variant_note: Resolved canonical sequence from direct_uniprot:P53686|reconstructed_variant and applied mutation signature D118N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines: mutant enzyme D118N, at pH 8.0, temperature not specified in the publication


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


sequence_variant_note: Resolved canonical sequence from direct_uniprot:P53686|reconstructed_variant and applied mutation signature I117F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I117F, at pH 8.0, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from direct_uniprot:P53686|reconstructed_variant and applied mutation signature I117V to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I117V, at pH 8.0, temperature not specified in the publication


organism: Trypanosoma brucei

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB:P50244 canonical sequence; A5HNV7 redirects to P50244 in the live UniProt REST entry.

proof_lines: enzyme in complex with prozyme, absence of putrescine, 37°C, pH 8.0

proof_lines: enzyme in complex with prozyme, presence of putrescine, 37°C, pH 8.0

proof_lines: free enzyme, absence of putrescine, 37°C, pH 8.0


organism: Trypanosoma brucei brucei

substrate_name: S-Adenosyl-L-methionine

sequence_source: UniProtKB:P50244 canonical sequence from live UniProt REST check.

substrate: S-Adenosyl-L-methionine


organism: Trypanosoma cruzi

sequence_source: UniProtKB:O76240 canonical sequence from live UniProt REST check.


enzyme_display_name: L-fuculose-phosphate aldolase

organism: Escherichia coli

substrate_name: L-Fuculose 1-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific Y209F substitution reconstructed after residue check. and applied mutation signature Y209F to reconstruct the assayed variant sequence.

enzyme: L-fuculose-phosphate aldolase

substrate: L-Fuculose 1-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific T26A substitution reconstructed after residue check. and applied mutation signature T26A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific F131A substitution reconstructed after residue check. and applied mutation signature F131A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant F131A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific R212A substitution reconstructed after residue check. and applied mutation signature R212A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific F206W substitution reconstructed after residue check. and applied mutation signature F206W to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant F206W


organism: Lactococcus lactis subsp. lactis bv. Diacetylactis

substrate_name: oxaloacetate

sequence_source: UniProtKB Q7X4Z5 FASTA/JSON direct lookup; PubMed 15251467 supports CitM as the Lactococcus oxaloacetate decarboxylase.

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

substrate: oxaloacetate


substrate_name: Oxaloacetate

substrate: Oxaloacetate


organism: Pseudomonas aeruginosa

sequence_source: UniProtKB reviewed Q9HUU1/OADC_PSEAE direct lookup; PubMed 18081320 and PDB 3B8I map PA4872 to the full UniProt sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines: wild type enzyme, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9HUU1/OADC_PSEAE direct lookup plus UniProt mutagenesis feature H235A from PubMed 18081320. and applied mutation signature H235A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H235A, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C


proof_lines: in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9HUU1/OADC_PSEAE direct lookup plus UniProt mutagenesis feature Y212F from PubMed 18081320. and applied mutation signature Y212F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y212F, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed Q9HUU1/OADC_PSEAE direct lookup plus UniProt mutagenesis feature H235Q from PubMed 18081320. and applied mutation signature H235Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H235Q, in 0.2 mM NADH, 5 mM MgCl2 and 50 mM K+HEPES (pH 7.5), at 25°C


organism: Catharanthus roseus

sequence_source: UniProtKB reviewed Q42679/DCAM_CATRO direct lookup; PubMed 7883014 supports the Catharanthus roseus SAMDC cDNA/proenzyme sequence.

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


enzyme_display_name: 8-oxo-dGTP diphosphatase

organism: Arabidopsis thaliana

substrate_name: dTTP

sequence_source: UniProtKB reviewed accession Q9CA40 direct lookup on 2026-06-04

normalized_value_unit_evidence: kcat: printed cell 0.25 s^-1 -> 0.25 s^(-1) (the printed column is already in export units); the exported value is 0.25 s^(-1). Km: printed cell 15.6 uM -> 0.0156 mM (divide by 1000); the exported value is 0.016 mM, the same measurement flattened to three decimals (issue category source_km_precision_flattened_to_three_decimals). kcat/Km: the paper PRINTS the kcat/Km cell 1.5 x 10^4 s^-1 M^-1 for this row -> 15.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 15.625 s^(-1)*mM^(-1), which is the bare quotient of the exported kcat and the flattened Km, not a printed cell.

row_label: Table III, row evidence block `Table III row: dTTP / AtNUDT1`, substrate row `dTTP`, protein `AtNUDT1`

table_label: Table III (JBC 280:25277-25283) 'Comparison of the kinetic parameters of AtNUDT1/MutT1 in A. thaliana with those of MutT-like proteins in E. coli, human, and yeast'

enzyme: 8-oxo-dGTP diphosphatase

substrate: dTTP


normalized_value_unit_evidence: kcat: printed cell 0.25 s^-1 -> 0.25 s^(-1) (the printed column is already in export units); the exported value is 0.25 s^(-1). Km: printed cell 6.8 uM -> 0.0068 mM (divide by 1000); the exported value is 0.007 mM, the same measurement flattened to three decimals (issue category source_km_precision_flattened_to_three_decimals). kcat/Km: the paper PRINTS the kcat/Km cell 3.7 x 10^4 s^-1 M^-1 for this row -> 37.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 35.714285714285715 s^(-1)*mM^(-1), which is the bare quotient of the exported kcat and the flattened Km, not a printed cell.

row_label: Table III, row evidence block `Table III row: 8-oxo-dGTP / AtNUDT1`, substrate row `8-oxo-dGTP`, protein `AtNUDT1`


substrate_name: H2O; 8-oxo-dGTP

substrate: H2O; 8-oxo-dGTP


substrate_name: dATP

normalized_value_unit_evidence: kcat: printed cell 0.17 s^-1 -> 0.17 s^(-1) (the printed column is already in export units); the exported value is 0.17 s^(-1). Km: printed cell 16.1 uM -> 0.0161 mM (divide by 1000); the exported value is 0.016 mM, the same measurement flattened to three decimals (issue category source_km_precision_flattened_to_three_decimals). kcat/Km: the paper PRINTS the kcat/Km cell 1.1 x 10^4 s^-1 M^-1 for this row -> 11.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 10.625 s^(-1)*mM^(-1), which is the bare quotient of the exported kcat and the flattened Km, not a printed cell.

row_label: Table III, row evidence block `Table III row: dATP / AtNUDT1`, substrate row `dATP`, protein `AtNUDT1`

substrate: dATP


substrate_name: dGTP

normalized_value_unit_evidence: kcat: printed cell 0.83 s^-1 -> 0.83 s^(-1) (the printed column is already in export units); the exported value is 0.83 s^(-1). Km: printed cell 58.3 uM -> 0.0583 mM (divide by 1000); the exported value is 0.058 mM, the same measurement flattened to three decimals (issue category source_km_precision_flattened_to_three_decimals). kcat/Km: the paper PRINTS the kcat/Km cell 1.4 x 10^4 s^-1 M^-1 for this row -> 14.0 s^(-1)*mM^(-1) (divide by 1000 for M^-1 to mM^-1); the exported value is 14.310344827586205 s^(-1)*mM^(-1), which is the bare quotient of the exported kcat and the flattened Km, not a printed cell.

row_label: Table III, row evidence block `Table III row: dGTP / AtNUDT1`, substrate row `dGTP`, protein `AtNUDT1`

substrate: dGTP


substrate_name: H2O; Coenzyme A

assay_conditions_summary: cofactor NADH

substrate: H2O; Coenzyme A


sequence_source: UniProtKB reviewed accession P08337 direct lookup on 2026-06-04


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific Y113F reconstruction and applied mutation signature Y113F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AB87 and applied mutation signature E214Q to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 310.15 K; buffer A [60 mM Tris; cofactor NADH

column_label: Table 3 (Kinetics for the Cleavage of Fuc1P by FucA Mutants), row label 'E214Q'; column 'relative specific activitya (%)' = 71; column 'kcatb (s-1)' = 20.5 (1.0); column 'KM (mM)' = 6 (0.3). Table 3 has no further data column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 20.5 s-1; s-1 is the canonical export unit s^(-1), so no unit conversion applies and the normalized value is 20.5 s^(-1). Km: printed Table 3 cell 6 mM; mM is the canonical export unit, so no unit conversion applies and the normalized value is 6.0 mM. kcat/Km: this paper prints no catalytic-efficiency cell; the full-precision quotient of the two printed cells of this one Table 3 row is 20.5 / 6.0 = 3.4166666666666665 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row 'E214Q': kcat = 20.5 s-1 (printed with its parenthesised uncertainty 1.0); KM = 6 mM (printed with its parenthesised uncertainty 0.3). Table 3 prints no catalytic-efficiency cell.

row_label: Table 3, mutant row 'E214Q'

table_label: Table 3: Kinetics for the Cleavage of Fuc1P by FucA Mutants (Biochemistry 2000, 39, 6033-6041)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AB87 and applied mutation signature E214A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetics for the Cleavage of Fuc1P by FucA Mutants), row label 'E214A'; column 'relative specific activitya (%)' = 48; column 'kcatb (s-1)' = 18.5 (3); column 'KM (mM)' = 8 (1.3). Table 3 has no further data column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 18.5 s-1; s-1 is the canonical export unit s^(-1), so no unit conversion applies and the normalized value is 18.5 s^(-1). Km: printed Table 3 cell 8 mM; mM is the canonical export unit, so no unit conversion applies and the normalized value is 8.0 mM. kcat/Km: this paper prints no catalytic-efficiency cell; the full-precision quotient of the two printed cells of this one Table 3 row is 18.5 / 8.0 = 2.3125 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row 'E214A': kcat = 18.5 s-1 (printed with its parenthesised uncertainty 3); KM = 8 mM (printed with its parenthesised uncertainty 1.3). Table 3 prints no catalytic-efficiency cell.

row_label: Table 3, mutant row 'E214A'


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific Y209F reconstruction and applied mutation signature Y209F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant Y209F


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific E214D reconstruction and applied mutation signature E214D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0AB87 canonical sequence with row-specific E214Q reconstruction and applied mutation signature E214Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant E214Q


column_label: Table 3 (Kinetics for the Cleavage of Fuc1P by FucA Mutants), row label 'wild type'; column 'relative specific activitya (%)' = 100; column 'kcatb (s-1)' = 19.3 (2); column 'KM (mM)' = 2.2 (0.2). Table 3 has no further data column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 19.3 s-1; s-1 is the canonical export unit s^(-1), so no unit conversion applies and the normalized value is 19.3 s^(-1). Km: printed Table 3 cell 2.2 mM; mM is the canonical export unit, so no unit conversion applies and the normalized value is 2.2 mM. kcat/Km: this paper prints no catalytic-efficiency cell; the full-precision quotient of the two printed cells of this one Table 3 row is 19.3 / 2.2 = 8.772727272727272 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row 'wild type': kcat = 19.3 s-1 (printed with its parenthesised uncertainty 2); KM = 2.2 mM (printed with its parenthesised uncertainty 0.2). Table 3 prints no catalytic-efficiency cell.

row_label: Table 3, wild-type row 'wild type'


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature K207A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature E214D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant E214D


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AB87 and applied mutation signature E214L to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetics for the Cleavage of Fuc1P by FucA Mutants), row label 'E214L'; column 'relative specific activitya (%)' = 6; column 'kcatb (s-1)' = 12.8 (5); column 'KM (mM)' = 74 (30). Table 3 has no further data column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 12.8 s-1; s-1 is the canonical export unit s^(-1), so no unit conversion applies and the normalized value is 12.8 s^(-1). Km: printed Table 3 cell 74 mM; mM is the canonical export unit, so no unit conversion applies and the normalized value is 74.0 mM. kcat/Km: this paper prints no catalytic-efficiency cell; the full-precision quotient of the two printed cells of this one Table 3 row is 12.8 / 74.0 = 0.17297297297297298 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row 'E214L': kcat = 12.8 s-1 (printed with its parenthesised uncertainty 5); KM = 74 mM (printed with its parenthesised uncertainty 30). Table 3 prints no catalytic-efficiency cell.

row_label: Table 3, mutant row 'E214L'


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature E214Q/T26A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature T26A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant T26A


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature R212A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant R212A


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature F206W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P0AB87 canonical sequence with selected source mutation signature applied and applied mutation signature Y113F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant Y113F


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P0AB87 and applied mutation signature E215A to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetics for the Cleavage of Fuc1P by FucA Mutants), row label 'E215A'; column 'relative specific activitya (%)' = 90; column 'kcatb (s-1)' = 21.5 (3); column 'KM (mM)' = 3.1 (0.4). Table 3 has no further data column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 21.5 s-1; s-1 is the canonical export unit s^(-1), so no unit conversion applies and the normalized value is 21.5 s^(-1). Km: printed Table 3 cell 3.1 mM; mM is the canonical export unit, so no unit conversion applies and the normalized value is 3.1 mM. kcat/Km: this paper prints no catalytic-efficiency cell; the full-precision quotient of the two printed cells of this one Table 3 row is 21.5 / 3.1 = 6.935483870967742 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, row 'E215A': kcat = 21.5 s-1 (printed with its parenthesised uncertainty 3); KM = 3.1 mM (printed with its parenthesised uncertainty 0.4). Table 3 prints no catalytic-efficiency cell.

row_label: Table 3, mutant row 'E215A'


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB FASTA lookup for reviewed accession P0AB87 plus computed E215A substitution. and applied mutation signature E215A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: L-fuculose-phosphate aldolase(Enzyme) mutant E215A


sequence_variant_note: Resolved canonical sequence from Direct UniProtKB FASTA lookup for reviewed accession P0AB87 plus computed N29Q substitution. and applied mutation signature N29Q to reconstruct the assayed variant sequence.


sequence_source: Direct UniProtKB FASTA lookup for reviewed accession P0AB87.

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

proof_lines: pH 7.5, 37°C, wild-type enzyme and E214A mutant


substrate_name: dihydroxyacetone phosphate

sequence_source: Direct UniProtKB FASTA lookup for reviewed accession Q58813.

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

proof_lines: assay with DL-glyceraldehyde, pH and temperature not specified in the publication

substrate: dihydroxyacetone phosphate


organism: Pseudomonas putida

sequence_variant_note: Resolved canonical sequence from Direct UniProtKB FASTA lookup for reviewed accession A5W059 plus computed R123K substitution. and applied mutation signature R123K to reconstruct the assayed variant sequence.


sequence_source: Direct UniProtKB FASTA lookup for reviewed accession A5W059.

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


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


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:A5W059 canonical sequence plus selected-record R123K mutation signature and applied mutation signature R123K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 4-hydroxy-4-methyl-2-oxoglutarate aldolase(Enzyme) mutant R123K

proof_lines: mutant enzyme R123K, in the presence of 2 mM phosphate, at pH 8.0 and 25°C

proof_lines: mutant enzyme R123K, in the absence of phosphate, at pH 8.0 and 25°C