sequence_variant_note: Resolved canonical sequence from UniProtKB Q06892 direct REST check with R293H reconstruction on 2026-06-15 and applied mutation signature R293H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R293H, in 100 mM Tris-HCl, pH 8.0, at 37°C


enzyme_display_name: NADH kinase

organism: Saccharomyces cerevisiae

substrate_name: NAD+

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_source: UniProtKB Q06892 direct REST check on 2026-06-15

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

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

proof_lines: wild type enzyme, in 100 mM Tris-HCl, pH 8.0, at 37°C

enzyme: NADH kinase

substrate: NAD+

source: brenda


substrate_name: ATP

kcat_display: Not reported

sequence_source: UniProtKB P32622 direct REST check on 2026-06-15

assay_conditions_summary: cofactor NADH

proof_lines: pH and temperature not specified in the publication

substrate: ATP


enzyme_display_name: 1,4-dihydroxy-2-naphthoyl-CoA synthase

organism: Escherichia coli (strain K12)

substrate_name: o-succinylbenzoyl-CoA

source_db: uniprot

assay_conditions_summary: pH 7; cofactor CoA

proof_lines: kcat is 620 sec(-1) with o-succinylbenzoyl-CoA as substrate (PubMed:21830810). kcat is 1.24 min(-1) with o-succinylbenzoyl-CoA as substrate (PubMed:23658663). All assays are performed at pH 7.0 at 25 degrees Celsius and in the presence of 2

enzyme: 1,4-dihydroxy-2-naphthoyl-CoA synthase

substrate: o-succinylbenzoyl-CoA

source: uniprot


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: O-succinylbenzoyl-CoA (at 25 degrees Celsius and pH 7.0)

proof_lines: kcat is 14.9 min(-1) with O-succinylbenzoyl-CoA at 25 degrees Celsius and pH 7.0 (PubMed:12909628). kcat is 4620 sec(-1) with O-succinylbenzoyl-CoA at 25 degrees Celsius and pH 7.0 (PubMed:21830810).


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from UniProtKB:P9WNP5 direct accession lookup plus D185N reconstruction and applied mutation signature D185N to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7; 298.15 K; buffer pH 7.0; cofactor CoA


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

ki_unit: mM

sequence_source: UniProtKB:P9WNP5 direct accession lookup

assay_conditions_summary: pH 7.4; 298.15 K; cofactor CoA

proof_lines:
pH 7.4, 25°C
Raw SKiD Env: Temp=25°C, pH=7

source_databases_merged: brenda skid


enzyme_display_name: (+)-abscisic acid 8'-hydroxylase

organism: Unknown

substrate_name: (+)-abscisic acid

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

enzyme: (+)-abscisic acid 8'-hydroxylase

substrate: (+)-abscisic acid


organism: Vibrio sp.

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

sequence_source: UniProt REST accession lookup 2026-06-15

data_origin: experimental

status: unverified

source: oed


assay_conditions_summary: pH 7; 298.15 K; cofactor CoA


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt accession P9WNP5 on 2026-06-15 and applied mutation signature D185N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt accession P9WNP5 on 2026-06-15 and applied mutation signature D185E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from reconstructed from UniProt accession P9WNP5 on 2026-06-15 and applied mutation signature S190A to reconstruct the assayed variant sequence.


proof_lines:
wild type protein, pH 7.0, 25°C
wild type protein protein, pH 7.0, 25°C


sequence_source: reconstructed from UniProt accession P9WNP5 on 2026-06-15


enzyme_display_name: arachidonate 8-lipoxygenase

organism: Mus musculus

substrate_name: (8S)-hydroxyeicosatetraenoic acid

assay_conditions_summary: pH 7.4; 298.15 K; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium phosphate buffer, pH 7.4, at 25°C

enzyme: arachidonate 8-lipoxygenase

substrate: (8S)-hydroxyeicosatetraenoic acid


organism: Plexaura homomalla

substrate_name: arachidonate

substrate: arachidonate


organism: Arabidopsis thaliana

substrate_name: NADH

assay_conditions_summary: pH 7.9; 298.15 K; cofactor NAD+

proof_lines: pH 7.9, 25°C, the specificity constant (vmax/Km) for NADH is 100fold greater than for NAD+

substrate: NADH


organism: Fusarium oxysporum


organism: Micrococcus flavus

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

proof_lines: with ATP as the phosphate donor, mutant enzyme G183R

proof_lines: with tetrapolyphosphate as the phosphate donor, mutant enzyme G183R


proof_lines: with ATP as the phosphate donor, wild type enzyme

proof_lines: with tetrapolyphosphate as the phosphate donor, wild type enzyme


assay_conditions_summary: pH 7.8; 303.15 K; cofactor NADH

proof_lines: pH 7.8, 30°C, in presence of 0.2 M sodium acetate


enzyme_display_name: formimidoylglutamate deiminase

organism: Pseudomonas aeruginosa

substrate_name: N-formimino-L-glutamate

enzyme: formimidoylglutamate deiminase

substrate: N-formimino-L-glutamate


proof_lines: Cu2+-reconstituted wild type enzyme, at pH 8.0 and 30°C

proof_lines: Ni2+-reconstituted wild type enzyme, at pH 8.0 and 30°C

proof_lines: Cd2+-reconstituted wild type enzyme, at pH 8.0 and 30°C


organism: Escherichia coli

substrate_name: o-succinylbenzoate

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProt P0ABU0 MENB_ECOLI after direct check that residue 270 is F; paper/RCSB anchor: PMID 23658663, PDB 4I42 maps fully to P0ABU0. and applied mutation signature F270A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, temperature not specified in the publication, mutant F270A

substrate: o-succinylbenzoate


substrate_name: Unknown

km_display: Not reported

assay_conditions_summary: cofactor CoA

proof_lines: non-competitive inhibitor, pH not specified in the publication, temperature not specified in the publication

proof_lines: non-competitive inhibitor , pH not specified in the publication, temperature not specified in the publication

substrate: Unknown


substrate_name: Abscisate

sequence_source: UniProtKB:Q9FH76 direct REST lookup 2026-06-15

substrate: Abscisate


substrate_name: H+; O2; NADPH; Abscisate

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

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

assay_conditions_summary: pH 7.6; 295.15 K; cofactor NADP+

proof_lines: pH 7.6, 22°C, recombinant isozyme CYP707A12

substrate: H+; O2; NADPH; Abscisate


enzyme_display_name: agmatine deiminase

organism: Helicobacter pylori

substrate_name: agmatine

sequence_source: UniProtKB:Q9ZN18 direct REST lookup 2026-06-15

smiles: N=C(N)NCCCCN

enzyme: agmatine deiminase

substrate: agmatine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9ZN18 direct REST lookup 2026-06-15 and applied mutation signature D198A to reconstruct the assayed variant sequence.


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Listeria monocytogenes serotype 1/2a

sequence_source: UniProtKB:A0A0H3G8U9 direct REST lookup 2026-06-15


proof_lines: in the presence of 10 mM Mg2+, at pH 9.3 and 37°C

proof_lines: in the presence of 5 mM Mg2+, at pH 10.0 and 37°C


substrate_name: CTP

substrate: CTP


substrate_name: (+)-S-abscisate

assay_conditions_summary: pH 7.25; 303.15 K; buffer 50 mM potassium phosphate; cofactor NADPH

proof_lines: 50 mM potassium phosphate buffer, pH 7.25, 50 microM NADPH, 30°C

substrate: (+)-S-abscisate


organism: Zea mays


assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication, mutant R267A


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

substrate_name: agmatin

substrate: agmatin


organism: Aquifex aeolicus

sequence_source: UniProtKB REST direct lookup for O66914, release 2026_02, retrieved 2026-06-15

proof_lines:
pH 9.0, 50°C
Raw SKiD Env: Temp=50°C, pH=9


organism: Burkholderia pseudomallei

sequence_source: UniProtKB REST direct lookup for Q63WL5, release 2026_02, retrieved 2026-06-15


substrate_name: 3-Deoxy-D-manno-octulosonate; CTP

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

sequence_source: UniProtKB REST direct lookup for P04951, release 2026_02, retrieved 2026-06-15

proof_lines: at pH 7.6, temperature not specified in the publication

source_databases_merged: sabio_rk brenda skid

substrate: 3-Deoxy-D-manno-octulosonate; CTP


proof_lines: kcat is 8.77 sec(-1) for 3-deoxy-D-manno-octulosonate.


organism: Burkholderia thailandensis

sequence_source: UniProtKB reviewed Q2T0K3 from direct EC+organism lookup; PMID 32588669 paper context names Bt KdsB.


organism: Salmonella enterica subsp. enterica serovar Typhimurium


sequence_variant_note: Resolved canonical sequence from RCSB 4I42 FASTA and UniProtKB reviewed P0ABU0; K89A reconstructed after direct residue check. and applied mutation signature K89A to reconstruct the assayed variant sequence.

proof_lines: pH 7.0, temperature not specified in the publication, mutant K89A


sequence_source: RCSB 4I42/4ELX FASTA and UniProtKB reviewed P0ABU0.

proof_lines: pH 7.0, temperature not specified in the publication, wild-type enzyme


enzyme_display_name: mycothiol S-conjugate amidase

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: MSmB (a bimane derivative of MSH)

proof_lines: at 50 mM HEPES, pH 7.5, 37 degrees Celsius, 50 mM NaCl.

enzyme: mycothiol S-conjugate amidase

substrate: MSmB (a bimane derivative of MSH)


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: MSmB

proof_lines: at 25 mM HEPES, pH 7.5, 30 degrees Celsius.

substrate: MSmB


enzyme_display_name: N-terminal methionine N(alpha)-acetyltransferase NatE

substrate_name: MASS

sequence_source: UniProtKB:Q9LFM3 canonical sequence fetched by exact accession lookup

substrate: MASS


organism: Homo sapiens

substrate_name: MLGTGRRR

sequence_source: UniProtKB:Q9GZZ1 canonical sequence fetched by exact accession lookup

assay_conditions_summary: pH 8.5; 310.15 K; cofactor CoA

proof_lines:
at pH 8.5 and 37°C
recombinant hNatE, pH 8.5, 37°C
recombinant hNaa50, pH 8.5, 37°C

enzyme: N-terminal methionine N(alpha)-acetyltransferase NatE

substrate: MLGTGRRR


organism: Neurospora crassa

substrate_name: MVNALE

mutation_signature: truncated protein residues 93-287

sequence_source: UniProtKB:Q7SF74 residues 93-287 reconstructed from canonical sequence and selected BRENDA paper note

sequence_variant_note: Mutation context was captured, but the signature could not be translated into an exact residue substitution safely.

mutation_type: truncation

proof_lines: trucated protein, residues 93-287, pH not specified in the publication, 30°C

substrate: MVNALE


organism: Thermochaetoides thermophila

mutation_signature: truncated protein

sequence_source: UniProtKB:G0S1V5 canonical sequence only; selected record merges multiple truncation ranges

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

proof_lines: truncated protein, residues 82-289, pH not specified in the publication, 30°C

proof_lines: truncated protein, residues 82-445, pH not specified in the publication, 30°C

proof_lines: truncated protein, residues 1-289, pH not specified in the publication, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:G0S1V5 canonical sequence with Y190F reconstructed after residue-coordinate check and applied mutation signature Y190F to reconstruct the assayed variant sequence.

proof_lines: mutant Y190F, pH not specified in the publication, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:G0S1V5 canonical sequence with H235A reconstructed after residue-coordinate check and applied mutation signature H235A to reconstruct the assayed variant sequence.

proof_lines: mutant H235A, pH not specified in the publication, 30°C


organism: Corynebacterium glutamicum

substrate_name: mycothiol bimane

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8NRQ7 and applied mutation signature H10A to reconstruct the assayed variant sequence.

column_label: Table 6 (Steady-state kinetic parameters of C. glutamicum Mca mutants for amidase activity of mycothiol bimane (MSmB)), Mca mutants row '10A', the H10A protein; column 'K m (mM)' = 108.36±5.7; column 'k cat (min−1)' = 4.10±1.8; column 'k cat/K m (M−1 s−1)' = 37.90; column '% WT activity' = 98.41.

normalized_value_unit_evidence: kcat: printed Table 6 cell 4.10 min^-1; the column head of Table 6 is 'k cat (min−1)', so 4.10 / 60 = 0.06833333333333333 s^-1. Km: printed Table 6 cell 108.36 mM; the column is already in mM, so no conversion is applied and the value stays 108.36 mM. kcat/Km: printed Table 6 cell 37.90 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 37.90 / 1000 = 0.037899999999999996 s^-1 mM^-1.

raw_value_unit_evidence: Table 6, Mca mutants row '10A' (the H10A protein): K_m = 108.36±5.7 mM; k_cat = 4.10±1.8 min^-1; printed k_cat/K_m = 37.90 M^-1 s^-1.

table_label: Table 6: Steady-state kinetic parameters of C. glutamicum Mca mutants for amidase activity of mycothiol bimane (MSmB) (PLoS ONE 2014, 9(12):e115075)

substrate: mycothiol bimane

status: corrected


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8NRQ7 and applied mutation signature D14A to reconstruct the assayed variant sequence.

column_label: Table 6 (Steady-state kinetic parameters of C. glutamicum Mca mutants for amidase activity of mycothiol bimane (MSmB)), Mca mutants row '14A', the D14A protein; column 'K m (mM)' = 132.33±1.5; column 'k cat (min−1)' = 2.16±0.7; column 'k cat/K m (M−1 s−1)' = 16.30; column '% WT activity' = 42.32.

normalized_value_unit_evidence: kcat: printed Table 6 cell 2.16 min^-1; the column head of Table 6 is 'k cat (min−1)', so 2.16 / 60 = 0.036000000000000004 s^-1. Km: printed Table 6 cell 132.33 mM; the column is already in mM, so no conversion is applied and the value stays 132.33 mM. kcat/Km: printed Table 6 cell 16.30 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 16.30 / 1000 = 0.016300000000000002 s^-1 mM^-1.

raw_value_unit_evidence: Table 6, Mca mutants row '14A' (the D14A protein): K_m = 132.33±1.5 mM; k_cat = 2.16±0.7 min^-1; printed k_cat/K_m = 16.30 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8NRQ7 and applied mutation signature H139A to reconstruct the assayed variant sequence.

column_label: Table 6 (Steady-state kinetic parameters of C. glutamicum Mca mutants for amidase activity of mycothiol bimane (MSmB)), Mca mutants row '139A', the H139A protein; column 'K m (mM)' = 469.65±1.4; column 'k cat (min−1)' = 0.29±0.4; column 'k cat/K m (M−1 s−1)' = 0.60; column '% WT activity' = 1.66.

normalized_value_unit_evidence: kcat: printed Table 6 cell 0.29 min^-1; the column head of Table 6 is 'k cat (min−1)', so 0.29 / 60 = 0.004833333333333333 s^-1. Km: printed Table 6 cell 469.65 mM; the column is already in mM, so no conversion is applied and the value stays 469.65 mM. kcat/Km: printed Table 6 cell 0.60 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.60 / 1000 = 0.0006 s^-1 mM^-1.

raw_value_unit_evidence: Table 6, Mca mutants row '139A' (the H139A protein): K_m = 469.65±1.4 mM; k_cat = 0.29±0.4 min^-1; printed k_cat/K_m = 0.60 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8NRQ7 and applied mutation signature Y137A to reconstruct the assayed variant sequence.

column_label: Table 6 (Steady-state kinetic parameters of C. glutamicum Mca mutants for amidase activity of mycothiol bimane (MSmB)), Mca mutants row '137A', the Y137A protein; column 'K m (mM)' = 542.37±3.3; column 'k cat (min−1)' = 0.30±0.9; column 'k cat/K m (M−1 s−1)' = 0.560; column '% WT activity' = 1.53.

normalized_value_unit_evidence: kcat: printed Table 6 cell 0.30 min^-1; the column head of Table 6 is 'k cat (min−1)', so 0.30 / 60 = 0.005 s^-1. Km: printed Table 6 cell 542.37 mM; the column is already in mM, so no conversion is applied and the value stays 542.37 mM. kcat/Km: printed Table 6 cell 0.560 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 0.560 / 1000 = 0.0005600000000000001 s^-1 mM^-1.

raw_value_unit_evidence: Table 6, Mca mutants row '137A' (the Y137A protein): K_m = 542.37±3.3 mM; k_cat = 0.30±0.9 min^-1; printed k_cat/K_m = 0.560 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8NRQ7 and applied mutation signature E16A to reconstruct the assayed variant sequence.

column_label: Table 6 (Steady-state kinetic parameters of C. glutamicum Mca mutants for amidase activity of mycothiol bimane (MSmB)), Mca mutants row '16A', the E16A protein; column 'K m (mM)' = 107.51±4.1; column 'k cat (min−1)' = 4.19±2.1; column 'k cat/K m (M−1 s−1)' = 38.90; column '% WT activity' = 101.05.

normalized_value_unit_evidence: kcat: printed Table 6 cell 4.19 min^-1; the column head of Table 6 is 'k cat (min−1)', so 4.19 / 60 = 0.06983333333333334 s^-1. Km: printed Table 6 cell 107.51 mM; the column is already in mM, so no conversion is applied and the value stays 107.51 mM. kcat/Km: printed Table 6 cell 38.90 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 38.90 / 1000 = 0.0389 s^-1 mM^-1.

raw_value_unit_evidence: Table 6, Mca mutants row '16A' (the E16A protein): K_m = 107.51±4.1 mM; k_cat = 4.19±2.1 min^-1; printed k_cat/K_m = 38.90 M^-1 s^-1.


sequence_source: UniProtKB:Q8NRQ7 canonical sequence fetched by exact accession lookup

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

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8NRQ7 and applied mutation signature H142A to reconstruct the assayed variant sequence.

column_label: Table 6 (Steady-state kinetic parameters of C. glutamicum Mca mutants for amidase activity of mycothiol bimane (MSmB)), Mca mutants row '142A', the H142A protein; column 'K m (mM)' = 115.33±5.7; column 'k cat (min−1)' = 3.93±3.8; column 'k cat/K m (M−1 s−1)' = 34.11±1.7; column '% WT activity' = 88.66.

normalized_value_unit_evidence: kcat: printed Table 6 cell 3.93 min^-1; the column head of Table 6 is 'k cat (min−1)', so 3.93 / 60 = 0.0655 s^-1. Km: printed Table 6 cell 115.33 mM; the column is already in mM, so no conversion is applied and the value stays 115.33 mM. kcat/Km: printed Table 6 cell 34.11 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 34.11 / 1000 = 0.03411 s^-1 mM^-1.

raw_value_unit_evidence: Table 6, Mca mutants row '142A' (the H142A protein): K_m = 115.33±5.7 mM; k_cat = 3.93±3.8 min^-1; printed k_cat/K_m = 34.11±1.7 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8NRQ7 and applied mutation signature E43A to reconstruct the assayed variant sequence.

column_label: Table 6 (Steady-state kinetic parameters of C. glutamicum Mca mutants for amidase activity of mycothiol bimane (MSmB)), Mca mutants row '43A', the E43A protein; column 'K m (mM)' = 93.37±1.5; column 'k cat (min−1)' = 3.46±3.9; column 'k cat/K m (M−1 s−1)' = 37.10; column '% WT activity' = 96.47.

normalized_value_unit_evidence: kcat: printed Table 6 cell 3.46 min^-1; the column head of Table 6 is 'k cat (min−1)', so 3.46 / 60 = 0.057666666666666665 s^-1. Km: printed Table 6 cell 93.37 mM; the column is already in mM, so no conversion is applied and the value stays 93.37 mM. kcat/Km: printed Table 6 cell 37.10 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 37.10 / 1000 = 0.0371 s^-1 mM^-1.

raw_value_unit_evidence: Table 6, Mca mutants row '43A' (the E43A protein): K_m = 93.37±1.5 mM; k_cat = 3.46±3.9 min^-1; printed k_cat/K_m = 37.10 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8NRQ7 and applied mutation signature D132A to reconstruct the assayed variant sequence.

column_label: Table 6 (Steady-state kinetic parameters of C. glutamicum Mca mutants for amidase activity of mycothiol bimane (MSmB)), Mca mutants row '132A', the D132A protein; column 'K m (mM)' = 99.92±1.9; column 'k cat (min−1)' = 3.88±2.6; column 'k cat/K m (M−1 s−1)' = 38.80; column '% WT activity' = 100.81.

normalized_value_unit_evidence: kcat: printed Table 6 cell 3.88 min^-1; the column head of Table 6 is 'k cat (min−1)', so 3.88 / 60 = 0.06466666666666666 s^-1. Km: printed Table 6 cell 99.92 mM; the column is already in mM, so no conversion is applied and the value stays 99.92 mM. kcat/Km: printed Table 6 cell 38.80 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 38.80 / 1000 = 0.038799999999999994 s^-1 mM^-1.

raw_value_unit_evidence: Table 6, Mca mutants row '132A' (the D132A protein): K_m = 99.92±1.9 mM; k_cat = 3.88±2.6 min^-1; printed k_cat/K_m = 38.80 M^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q8NRQ7 and applied mutation signature D15A to reconstruct the assayed variant sequence.

column_label: Table 6 (Steady-state kinetic parameters of C. glutamicum Mca mutants for amidase activity of mycothiol bimane (MSmB)), Mca mutants row '15A', the D15A protein; column 'K m (mM)' = 128.76±1.5; column 'k cat (min−1)' = 4.68±1.4; column 'k cat/K m (M−1 s−1)' = 36.30; column '% WT activity' = 94.35.

normalized_value_unit_evidence: kcat: printed Table 6 cell 4.68 min^-1; the column head of Table 6 is 'k cat (min−1)', so 4.68 / 60 = 0.078 s^-1. Km: printed Table 6 cell 128.76 mM; the column is already in mM, so no conversion is applied and the value stays 128.76 mM. kcat/Km: printed Table 6 cell 36.30 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 36.30 / 1000 = 0.0363 s^-1 mM^-1.

raw_value_unit_evidence: Table 6, Mca mutants row '15A' (the D15A protein): K_m = 128.76±1.5 mM; k_cat = 4.68±1.4 min^-1; printed k_cat/K_m = 36.30 M^-1 s^-1.


substrate_name: acetyl-CoA

sequence_source: UniProtKB reviewed Q9GZZ1 (NAA50_HUMAN), fetched by EC 2.3.1.258 plus Homo sapiens lookup; UniProt links hNaa50p and EC 2.3.1.258 to PMID 22311970.

assay_conditions_summary: pH 7.4; cofactor CoA

proof_lines: with acetyl-CoA, pH 7.4, temperature not specified in the publication

proof_lines: with peptide, pH 7.4, temperature not specified in the publication

substrate: acetyl-CoA


organism: Mycobacterium tuberculosis

substrate_name: mycothiol-N-ethylmaleimide

sequence_source: UniProtKB reviewed P9WJN1 (MCA_MYCTU), fetched by EC 3.5.1.115 plus Mycobacterium tuberculosis lookup; UniProt links the catalytic activity to PMIDs 10978158 and 14556638.

proof_lines: kcat above 3.0 s-1, in 50 mM HEPES (pH 7.5) containing 50 mM NaCl and 0.1 mM dithiothreitol, at 37°C

proof_lines: Km above 3.0 mM, in 50 mM HEPES (pH 7.5) containing 50 mM NaCl and 0.1 mM dithiothreitol, at 37°C

substrate: mycothiol-N-ethylmaleimide


organism: Mycolicibacterium smegmatis

substrate_name: mycothiol bimane derivative

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

substrate: mycothiol bimane derivative


organism: Vibrio sp


organism: synthetic construct


organism: Vibrio sp.

substrate_name: xylotetraose

substrate: xylotetraose


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8NRQ7 and applied mutation signature H12A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q8NRQ7 and applied mutation signature D141A to reconstruct the assayed variant sequence.


organism: Mycobacterium smegmatis


substrate_name: MSmB; H2O

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

substrate: MSmB; H2O


enzyme_display_name: homoaconitate hydratase

organism: Methanocaldococcus jannaschii

substrate_name: Homocitrate

enzyme: homoaconitate hydratase

substrate: Homocitrate


substrate_name: Maleate

substrate: Maleate


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


organism: Thermus thermophilus


substrate_name: homoisocitrate

substrate: homoisocitrate


substrate_name: H2O; But-1-ene-1,2,4-tricarboxylate

substrate: H2O; But-1-ene-1,2,4-tricarboxylate


organism: Arachis hypogaea

substrate_name: agmatine

substrate: agmatine


organism: Cucumis sativus


organism: Evernia prunastri


organism: Glycine max


organism: Listeria monocytogenes


organism: Oryza sativa


organism: Pseudomonas aeruginosa

substrate_name: H2O; Agmatine

substrate: H2O; Agmatine


organism: Zea mays


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

proof_lines: mutant R26K, pH 7.0, temperature not specified in the publication


proof_lines: pH 7.0, temperature not specified in the publication


proof_lines: mutant T27A, pH 7.0, temperature not specified in the publication


proof_lines: mutant R26V, pH 7.0, temperature not specified in the publication


enzyme_display_name: GTP diphosphokinase

organism: Bacillus subtilis

substrate_name: GTP; guanosine 3'-diphosphate 5'-triphosphate; GDP; guanosine 3'-diphosphate 5'-diphosphate

enzyme: GTP diphosphokinase


organism: Francisella tularensis subsp. tularensis

substrate_name: ATP; GTP

assay_conditions_summary: pH 8; 303.15 K; cofactor ATP

substrate: ATP; GTP


organism: Mycobacterium tuberculosis

substrate_name: ATP

substrate: ATP


substrate_name: GTP; ATP; GTP; ATP; AMP; Guanosine 3'-diphosphate 5'-triphosphate; ATP; GTP

assay_conditions_summary: cofactor ATP


substrate_name: GTP

substrate: GTP


organism: Streptococcus equisimilis

substrate_name: GTP; ATP; GTP; ATP; Guanosine 3'-diphosphate 5'-triphosphate; AMP


organism: Flammeovirga pacifica

substrate_name: beta-1,3-xylan; glycol beta-1,3-xylan

proof_lines:
20°C, pH 7.5, 0 mM NaCl
20°C, pH 7.5, 1.5 mM NaCl

substrate: beta-1,3-xylan; glycol beta-1,3-xylan


mutation_signature: recombinant truncated enzyme

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

proof_lines: recombinant truncated enzyme, pH 7.5, 45°C, no NaCl added

proof_lines: recombinant truncated enzyme, pH 7.5, 45°C, 1.5 M NaCl added


proof_lines: recombinant wild-type enzyme, pH 7.5, 45°C, no NaCl added

proof_lines: recombinant wild-type enzyme, pH 7.5, 45°C, 1.5 M NaCl added


proof_lines: recombinant enzyme, pH 7.5, 45°C, no NaCl added

proof_lines: recombinant enzyme, pH 7.5, 45°C, 1.5 M NaCl added


organism: Thermotoga neapolitana


organism: Vibrio sp.

source_db: brenda; skid

proof_lines:
at pH 7.5 and 37°C
Raw SKiD Env: Temp=37°C, pH=7.5

source: brenda; skid


organism: Campylobacter jejuni subsp. jejuni serotype O:2


organism: Enterococcus faecalis

substrate_name: H2O; Agmatine; H2O; Agmatine; NH3; N-Carbamoylputrescine; Agmatine; H2O

source_db: sabio_rk; brenda

source: sabio_rk; brenda


organism: Helicobacter pylori

substrate_name: agmatine; L-arginine; streptomycin; Ac-SGRGK; N-alpha-benzoyl-L-arginine amide; guanidine; N-alpha-benzoyl-L-arginine ethyl ester; N-alpha-benzoyl-L-arginine methyl ester


substrate_name: agmatine; streptomycin; L-arginine; Ac-SGRGK; N-alpha-benzoyl-L-arginine amide; guanidine; N-alpha-benzoyl-L-arginine ethyl ester; N-alpha-benzoyl-L-arginine methyl ester

sequence_variant_note: Resolved canonical sequence from reconstructed_from_uniprot_accession and applied mutation signature D198A to reconstruct the assayed variant sequence.


enzyme_display_name: [methionine synthase] reductase

organism: Homo sapiens

substrate_name: 3-acetylpyridine adenine dinucleotide phosphate

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/Q9UBK8.json retrieved 2026-06-15

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

enzyme: [methionine synthase] reductase


substrate_name: NADPH; Ferricytochrome c

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

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

substrate: NADPH; Ferricytochrome c


substrate_name: NADPH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: Unknown

sequence_variant_note: Resolved canonical sequence from UniProtKB REST https://rest.uniprot.org/uniprotkb/Q9UBK8.json retrieved 2026-06-15 and applied mutation signature W697F to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant W697F, with cytochrome c3+

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB REST https://rest.uniprot.org/uniprotkb/Q9UBK8.json retrieved 2026-06-15 and applied mutation signature W697Y to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, mutant W697Y, with cytochrome c3+


sequence_variant_note: Resolved canonical sequence from UniProtKB REST https://rest.uniprot.org/uniprotkb/Q9UBK8.json retrieved 2026-06-15 and applied mutation signature A312H to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from UniProtKB REST https://rest.uniprot.org/uniprotkb/Q9UBK8.json retrieved 2026-06-15 and applied mutation signature A312Q to reconstruct the assayed variant sequence.


proof_lines: pH 7.5, 25°C, recombinant wild-type enzyme


enzyme_display_name: cellobionic acid phosphorylase

organism: Neurospora crassa

substrate_name: D-Gluconate

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/Q7S0S2.json retrieved 2026-06-15

enzyme: cellobionic acid phosphorylase

substrate: D-Gluconate


substrate_name: Cellobionic acid; Phosphate

substrate: Cellobionic acid; Phosphate


substrate_name: Phosphate

smiles: O=P(O)(O)O

substrate: Phosphate


organism: Saccharophagus degradans

sequence_source: UniProtKB REST https://rest.uniprot.org/uniprotkb/Q21MB1.json retrieved 2026-06-15


sequence_variant_note: Resolved canonical sequence from UniProtKB REST https://rest.uniprot.org/uniprotkb/Q21MB1.json retrieved 2026-06-15 and applied mutation signature Q190A to reconstruct the assayed variant sequence.


substrate_name: D-gluconate

substrate: D-gluconate


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


substrate_name: D-Glucuronate

substrate: D-Glucuronate


verification_status: verified

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Printed page 11839, Table 2, NADPH row, Km column: 2.89 +/- 0.18 micromolar.

normalized_value_unit_evidence: 2.89 micromolar = 0.00289 mM; exact match to the current row.

raw_value_unit_evidence: NADPH Km = 2.89 +/- 0.18 micromolar.

row_label: NADPH

table_label: Table 2

status: verified


enzyme_display_name: long-chain alkane monooxygenase

organism: Geobacillus thermodenitrificans

substrate_name: hexadecane

sequence_variant_note: Resolved canonical sequence from UniProtKB A4IU28 REST/FASTA direct check on 2026-06-15 and applied mutation signature F146E/N376I to reconstruct the assayed variant sequence.

enzyme: long-chain alkane monooxygenase

substrate: hexadecane


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A4IU28 and applied mutation signature A102E to reconstruct the assayed variant sequence.

smiles: CCCCCCCCCCCCCCCC

assay_conditions_summary: pH 7.5; 333.15 K; cofactor NADPH

column_label: Table 1 (Kinetic parameters of wild-type and mutant LadA), row label 'A102E' in the 'LadA' column; column 'Km (mM)' = 1.5; column 'kcat (min-1)' = 2.8; column 'Fold activity' = 2.2; column 'kcat/Km (min-1 mM-1)' = 1.89; column 'Coupling rate' = 75.3 %.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.5 mM is already in mM, so no unit conversion applies and the canonical value is 1.5 mM. kcat: printed Table 1 cell 2.8 min^-1; min^-1 to s^-1 is a division by 60, so 2.8 / 60 = 0.04666666666666666 s^-1. kcat/Km: printed Table 1 cell 1.89 min^-1 mM^-1; min^-1 mM^-1 to s^-1 mM^-1 is a division by 60, so 1.89 / 60 = 0.0315 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 (Kinetic parameters of wild-type and mutant LadA), row 'A102E': printed Km = 1.5 mM; printed kcat = 2.8 min^-1; printed kcat/Km = 1.89 min^-1 mM^-1.

row_label: Table 1, row 'A102E' of the 'LadA' column

table_label: Table 1: Kinetic parameters of wild-type and mutant LadA (Appl Microbiol Biotechnol 2012, 94:1019-1029)


sequence_source: UniProtKB A4IU28 REST/FASTA direct check on 2026-06-15


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A4IU28 and applied mutation signature A102D to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of wild-type and mutant LadA), row label 'A102D' in the 'LadA' column; column 'Km (mM)' = 1.8; column 'kcat (min-1)' = 2.7; column 'Fold activity' = 2.1; column 'kcat/Km (min-1 mM-1)' = 1.47; column 'Coupling rate' = 86.3 %.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.8 mM is already in mM, so no unit conversion applies and the canonical value is 1.8 mM. kcat: printed Table 1 cell 2.7 min^-1; min^-1 to s^-1 is a division by 60, so 2.7 / 60 = 0.045000000000000005 s^-1. kcat/Km: printed Table 1 cell 1.47 min^-1 mM^-1; min^-1 mM^-1 to s^-1 mM^-1 is a division by 60, so 1.47 / 60 = 0.0245 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 (Kinetic parameters of wild-type and mutant LadA), row 'A102D': printed Km = 1.8 mM; printed kcat = 2.7 min^-1; printed kcat/Km = 1.47 min^-1 mM^-1.

row_label: Table 1, row 'A102D' of the 'LadA' column


sequence_variant_note: Resolved canonical sequence from UniProtKB A4IU28 REST/FASTA direct check on 2026-06-15 and applied mutation signature F146C/N376I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A4IU28 REST/FASTA direct check on 2026-06-15 and applied mutation signature F146Q/N376I to reconstruct the assayed variant sequence.


column_label: Table 1 (Kinetic parameters of wild-type and mutant LadA), row label 'WT' in the 'LadA' column; column 'Km (mM)' = 9.1; column 'kcat (min-1)' = 1.3; column 'Fold activity' = 1.0; column 'kcat/Km (min-1 mM-1)' = 0.15; column 'Coupling rate' = 95.8 %.

normalized_value_unit_evidence: Km: printed Table 1 cell 9.1 mM is already in mM, so no unit conversion applies and the canonical value is 9.1 mM. kcat: printed Table 1 cell 1.3 min^-1; min^-1 to s^-1 is a division by 60, so 1.3 / 60 = 0.021666666666666667 s^-1. kcat/Km: printed Table 1 cell 0.15 min^-1 mM^-1; min^-1 mM^-1 to s^-1 mM^-1 is a division by 60, so 0.15 / 60 = 0.0025 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 (Kinetic parameters of wild-type and mutant LadA), row 'WT': printed Km = 9.1 mM; printed kcat = 1.3 min^-1; printed kcat/Km = 0.15 min^-1 mM^-1.

row_label: Table 1, row 'WT' of the 'LadA' column


sequence_variant_note: Resolved canonical sequence from UniProtKB A4IU28 REST/FASTA direct check on 2026-06-15 and applied mutation signature L320V to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A4IU28 REST/FASTA direct check on 2026-06-15 and applied mutation signature L320A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A4IU28 REST/FASTA direct check on 2026-06-15 and applied mutation signature F146R/N376I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A4IU28 REST/FASTA direct check on 2026-06-15 and applied mutation signature A102D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB A4IU28 REST/FASTA direct check on 2026-06-15 and applied mutation signature F146N/N376I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A4IU28 and applied mutation signature F146R/N376I to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of wild-type and mutant LadA), row label 'F146R/N376I' in the 'LadA' column; column 'Km (mM)' = 2.0; column 'kcat (min-1)' = 3.3; column 'Fold activity' = 2.5; column 'kcat/Km (min-1 mM-1)' = 1.77; column 'Coupling rate' = 86.7 %.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.0 mM is already in mM, so no unit conversion applies and the canonical value is 2.0 mM. kcat: printed Table 1 cell 3.3 min^-1; min^-1 to s^-1 is a division by 60, so 3.3 / 60 = 0.05499999999999999 s^-1. kcat/Km: printed Table 1 cell 1.77 min^-1 mM^-1; min^-1 mM^-1 to s^-1 mM^-1 is a division by 60, so 1.77 / 60 = 0.0295 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 (Kinetic parameters of wild-type and mutant LadA), row 'F146R/N376I': printed Km = 2.0 mM; printed kcat = 3.3 min^-1; printed kcat/Km = 1.77 min^-1 mM^-1.

row_label: Table 1, row 'F146R/N376I' of the 'LadA' column


organism: Xanthomonas campestris pv. campestris (strain ATCC 33913 / DSM 3586 / NCPPB 528 / LMG 568 / P 25)

proof_lines: kcat is 173 sec(-1) for D-gluconate. kcat is 43 sec(-1) for D-glucuronate. kcat is 127 sec(-1) for alpha-D-glucose 1-phosphate.


enzyme_display_name: kaempferol 3-O-galactosyltransferase

organism: Petunia hybrida

substrate_name: kaempferol

sequence_source: UniProtKB REST exact accession lookup: Q9SBQ8

enzyme: kaempferol 3-O-galactosyltransferase

substrate: kaempferol


substrate_name: Quercetin 3-O-beta-D-galactoside

substrate: Quercetin 3-O-beta-D-galactoside


substrate_name: UDP-D-galactose

substrate: UDP-D-galactose


substrate_name: quercetin

substrate: quercetin


substrate_name: UDP

substrate: UDP


substrate_name: Kaempferol 3-O-beta-D-galactoside

substrate: Kaempferol 3-O-beta-D-galactoside


sequence_source: UniProtKB REST exact accession lookup: Q21MB1


organism: Xanthomonas campestris

substrate_name: alpha-D-glucose 1-phosphate

sequence_source: UniProtKB REST exact accession lookup: Q8P3J4

substrate: alpha-D-glucose 1-phosphate


substrate_name: Cellobionic acid

substrate: Cellobionic acid


organism: Xanthomonas campestris pv. campestris

substrate_name: D-glucuronate

substrate: D-glucuronate


substrate_name: NADPH

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

proof_lines: inhibition of reduction of cytochrome c3+

substrate: NADPH


organism: Brevibacillus brevis

substrate_name: GDP

assay_conditions_summary: pH 8.1; 303.15 K; cofactor ATP

proof_lines:
30°C, pH 8.1
cosubstrate GDP, pH 8.1, 30°C
cosubstrate GTP, pH 8.1, 30°C

substrate: GDP


organism: Geobacillus stearothermophilus

substrate_name: ATP

assay_conditions_summary: pH 7.8; 310.15 K; cofactor ATP

proof_lines:
synthetase II, pH 7.8, 37°C
synthetase I, pH 7.8, 37°C

substrate: ATP


organism: Mycobacterium tuberculosis

substrate_name: GTP

proof_lines:
full length enzyme
full length enzyme + tRNA
fragment 87-394

substrate: GTP


organism: Mycolicibacterium smegmatis


organism: Aspergillus nidulans


organism: Candida albicans

substrate_name: (R)-homocitrate

proof_lines: in 50 mM Tris-HCl (pH 8.5), 50 mM KCl, 5 mM MgCl2, 20 mM dithiothreitol, at 20°C

substrate: (R)-homocitrate


organism: Methanocaldococcus jannaschii

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

proof_lines: mutant R26V/T27Y, pH 7.0, temperature not specified in the publication


proof_lines: wild-type HACNMj, pH 7.0, temperature not specified in the publication


enzyme_display_name: bacillolysin

organism: Bacillus subtilis

substrate_name: Benzyloxycarbonyl-Phe-Leu-Ala

enzyme: bacillolysin

substrate: Benzyloxycarbonyl-Phe-Leu-Ala


sequence_source: UniProtKB:P68736 REST lookup checked 2026-06-15


substrate_name: Benzyloxycarbonyl-Gly-Leu-Ala

substrate: Benzyloxycarbonyl-Gly-Leu-Ala


substrate_name: H2O; Benzyloxycarbonyl-Phe-Leu-Ala

proof_lines: SABIO-RK modifier species: bacillolysin(Enzyme) mutant G189A (aa 222-521)

substrate: H2O; Benzyloxycarbonyl-Phe-Leu-Ala


substrate_name: Benzyloxycarbonyl-Ala-Leu-Ala

substrate: Benzyloxycarbonyl-Ala-Leu-Ala


substrate_name: Benzyloxycarbonyl-Phe-Leu-Ala; H2O

proof_lines: SABIO-RK modifier species: bacillolysin(Enzyme) mutant G147A (aa 222-521)

substrate: Benzyloxycarbonyl-Phe-Leu-Ala; H2O


substrate_name: H2O; Z-Phe-Leu-Ala-OH

proof_lines: SABIO-RK modifier species: bacillolysin(Enzyme) mutant aa188 - 194 replaced by aa192 - 201 of thermolysin (Uniprot_ID: P00800)

substrate: H2O; Z-Phe-Leu-Ala-OH


substrate_name: Z-Phe-Leu-Ala-OH; H2O

substrate: Z-Phe-Leu-Ala-OH; H2O


substrate_name: kaempferol

substrate: kaempferol


organism: Neurospora crassa (strain ATCC 24698 / 74-OR23-1A / CBS 708.71 / DSM 1257 / FGSC 987)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: ppGpp (at 30 degrees Celsius and pH 8)

assay_conditions_summary: pH 8

substrate: ppGpp (at 30 degrees Celsius and pH 8)


organism: Streptococcus dysgalactiae subsp. equisimilis


organism: Emericella nidulans (strain FGSC A4 / ATCC 38163 / CBS 112.46 / NRRL 194 / M139)

substrate_name: homoisocitric acid

substrate: homoisocitric acid


organism: Thermus thermophilus (strain ATCC BAA-163 / DSM 7039 / HB27)

substrate_name: cis-homoaconitate (at 60 degrees Celsius and pH 8)


substrate: cis-homoaconitate (at 60 degrees Celsius and pH 8)


organism: Geobacillus thermodenitrificans (strain NG80-2)

substrate_name: hexadecane

sequence_source: source_record; confirmed against UniProtKB A4IU28 FASTA/TSV

assay_conditions_summary: pH 8; 333.15 K; cofactor NADPH

substrate: hexadecane


substrate_name: Z-Phe-Leu-Ala-OH

sequence_source: UniProtKB:P68736 direct lookup

substrate: Z-Phe-Leu-Ala-OH


organism: Listeria monocytogenes serotype 1/2a

substrate_name: agmatine

sequence_source: UniProtKB:A0A0H3G8U9 direct lookup

substrate: agmatine


organism: Pseudomonas aeruginosa PA14


organism: Selenomonas ruminantium

sequence_source: UniProtKB:Q5KR05 direct lookup


substrate_name: But-1-ene-1,2,4-tricarboxylate; H2O

substrate: But-1-ene-1,2,4-tricarboxylate; H2O


enzyme_display_name: quercetin 2,3-dioxygenase

organism: Bacillus subtilis (strain 168)

substrate_name: quercetin

assay_conditions_summary: pH 6; buffer pH 6

enzyme: quercetin 2,3-dioxygenase

substrate: quercetin


enzyme_display_name: squalene synthase

organism: Botryococcus braunii

substrate_name: geranylgeranyl diphosphate

enzyme: squalene synthase

substrate: geranylgeranyl diphosphate


organism: Geobacillus thermodenitrificans

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A4IU28 and applied mutation signature F146C/N376I to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of wild-type and mutant LadA), row label 'F146C/N376I' in the 'LadA' column; column 'Km (mM)' = 2.8; column 'kcat (min-1)' = 3.8; column 'Fold activity' = 2.9; column 'kcat/Km (min-1 mM-1)' = 1.33; column 'Coupling rate' = 83.4 %.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.8 mM is already in mM, so no unit conversion applies and the canonical value is 2.8 mM. kcat: printed Table 1 cell 3.8 min^-1; min^-1 to s^-1 is a division by 60, so 3.8 / 60 = 0.06333333333333332 s^-1. kcat/Km: printed Table 1 cell 1.33 min^-1 mM^-1; min^-1 mM^-1 to s^-1 mM^-1 is a division by 60, so 1.33 / 60 = 0.022166666666666668 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 (Kinetic parameters of wild-type and mutant LadA), row 'F146C/N376I': printed Km = 2.8 mM; printed kcat = 3.8 min^-1; printed kcat/Km = 1.33 min^-1 mM^-1.

row_label: Table 1, row 'F146C/N376I' of the 'LadA' column


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB canonical accession A4IU28 using selected batch mutation signature F146Q/N376I and applied mutation signature F146Q/N376I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:A4IU28 and applied mutation signature L320A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters of wild-type and mutant LadA), row label 'L320A' in the 'LadA' column; column 'Km (mM)' = 7.1; column 'kcat (min-1)' = 2.8; column 'Fold activity' = 2.2; column 'kcat/Km (min-1 mM-1)' = 0.40; column 'Coupling rate' = 64.5 %.

normalized_value_unit_evidence: Km: printed Table 1 cell 7.1 mM is already in mM, so no unit conversion applies and the canonical value is 7.1 mM. kcat: printed Table 1 cell 2.8 min^-1; min^-1 to s^-1 is a division by 60, so 2.8 / 60 = 0.04666666666666666 s^-1. kcat/Km: printed Table 1 cell 0.40 min^-1 mM^-1; min^-1 mM^-1 to s^-1 mM^-1 is a division by 60, so 0.40 / 60 = 0.006666666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 (Kinetic parameters of wild-type and mutant LadA), row 'L320A': printed Km = 7.1 mM; printed kcat = 2.8 min^-1; printed kcat/Km = 0.40 min^-1 mM^-1.

row_label: Table 1, row 'L320A' of the 'LadA' column


organism: Arabidopsis thaliana

substrate_name: glutathione

sequence_source: UniProtKB REST direct accession lookup for P92979 on 2026-06-15

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

proof_lines: holoenzyme APR1p with substrate 5-adenylyl sulfate, pH 8.5, 30°C

proof_lines: about, holoenzyme APR1p and C-domain with substrate dehydroascorbate, pH 6.9, 24°C

proof_lines: about, holoenzyme APR1p and C-domain with substrates hydroxyethyldisulfide, or cystine, pH 8.0, 24°C

substrate: glutathione


organism: Lemna minor

substrate_name: Adenylylsulfate; Reduced glutathione

sequence_source: UniProtKB REST direct accession lookup for Q9SCA0 on 2026-06-15

substrate: Adenylylsulfate; Reduced glutathione


substrate_name: adenylylsulfate

substrate: adenylylsulfate


organism: Aspergillus flavus

substrate_name: NADPH

assay_conditions_summary: pH 7.4; cofactor NADPH

proof_lines: pH 7.4, temperature not specified in the publication

substrate: NADPH


organism: Homo sapiens

substrate_name: NADPH; trans,trans-Farnesyl diphosphate; H+

sequence_source: UniProtKB REST direct accession lookup for P37268 on 2026-06-15

assay_conditions_summary: cofactor NADPH

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


organism: Leishmania donovani

substrate_name: (2E,6E)-farnesyl diphosphate

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

substrate: (2E,6E)-farnesyl diphosphate


organism: Methylococcus capsulatus

sequence_source: UniProtKB REST direct accession lookup for Q60AN4 on 2026-06-15

assay_conditions_summary: pH 8; 306.15 K; cofactor NADPH


organism: Mortierella alpina

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


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB canonical accession A0A0K2F2K4 using selected batch mutation signature E186K and applied mutation signature E186K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.2; 310.15 K; cofactor NADPH

proof_lines: pH 7.2, 37°C, recombinant mutant E186K enzyme


organism: Siraitia grosvenorii

sequence_source: UniProtKB REST direct accession lookup for A0A192YD12 on 2026-06-15


organism: Bacillus intermedius

substrate_name: azocasein

sequence_source: UniProtKB REST direct accession lookup for B3V4Z0 on 2026-06-15

proof_lines: recombinant wild-type enzyme, pH 8.0, 37°C

substrate: azocasein


organism: Bacillus subtilis

substrate_name: Benzyloxycarbonyl-Phe-Leu-Ala; H2O

proof_lines: SABIO-RK modifier species: bacillolysin(Enzyme) mutant G147A/G189A (aa 222-521)

substrate: Benzyloxycarbonyl-Phe-Leu-Ala; H2O


organism: Nicotiana tabacum

substrate_name: farnesyl diphosphate

substrate: farnesyl diphosphate


organism: Rattus norvegicus

substrate_name: trans-farnesyl diphosphate

substrate: trans-farnesyl diphosphate


organism: Saccharomyces cerevisiae

proof_lines:
in presence of 1% Tween 80 and Mg2+
cosubstrate + NAD(P)H


organism: Sus scrofa


organism: Tabernaemontana divaricata


organism: Thermosynechococcus vestitus


organism: Trypanosoma cruzi

assay_conditions_summary: pH 7.4; 310.15 K; buffer 50 mM morpholinepropanesulfonic acid-NaOH; cofactor NADPH

proof_lines: in 50 mM morpholinepropanesulfonic acid-NaOH buffer (pH 7.4), 20 mM MgCl2, 5 mM 3-[(3-cholamidopropyl)-dimethylammonio]-1-propanesulfonate, 1% Tween 80, 10 mM dithiothreitol, 0.025 mg/ml bovine serum albumin, 0.25 mM NADPH, at 37°C


organism: Bacillus cereus

substrate_name: casein

substrate: casein


proof_lines: pH 9.0, 60°C, recombinant wild-type enzyme


organism: Catharanthus roseus

proof_lines:
with DTT as reductant
with glutathione as reductant
with 5-adenylylsulfate as substrate


organism: Glycine max

substrate_name: 5'-adenylyl sulfate

proof_lines: 30°C, pH 8.5, cosubstrate: dithiothreitol

substrate: 5'-adenylyl sulfate


organism: Lemna minor

proof_lines:
with 40 mM glutathione as reductant
with 0.04 mM adenylylsulfate
with 10 mM glutathione as reductant


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

proof_lines: assay conditions: APS reductase (0.0009 mM), EST (0.10 unit/ml), thioredoxin (0.037 mM), MgCl2 (3.0 mM), DTT (2.0 mM), pNPS (10 mM), GSH (5.0 mM), and Hepes (50 mM, pH 8.0), at 25°C

proof_lines: assay conditions: APS reductase (0.00021 mM), PK (8.4 units/ml), LDH (18.0 units/ml), adenylate kinase (10 units/ml), thioredoxin (0.0373 mM), MgCl2 (3.0 mM), DTT (2.0 mM), ATP (1.0 mM), PEP (1.0 mM), EDTA (1.0 mM), GSH (5.0 mM), NADH (0.03


organism: Physcomitrium patens

substrate_name: adenosine 5'-phosphosulfate

substrate: adenosine 5'-phosphosulfate


organism: Pseudomonas aeruginosa

proof_lines:
in the presence of 0.001 mM thioredoxin
in the presence of 0.01 mM thioredoxin


organism: Ulva intestinalis

proof_lines:
with 5-adenylylsulfate as substrate
with glutathione as reductant


organism: Homo sapiens

substrate_name: Unknown

substrate: Unknown


organism: Bacillus subtilis

sequence_source: UniProtKB:P42106 direct accession lookup; canonical sequence reused from live UniProt record on 2026-06-15


smiles: O=O


organism: Bacillus thermodenitrificans

substrate_name: NADPH; H+; O2; Hexadecane

sequence_variant_note: Resolved canonical sequence from UniProtKB:A4IU28 direct accession lookup; canonical sequence reused from live UniProt record on 2026-06-15 and applied mutation signature F146R/N376I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: long-chain alkane monooxygenase(Enzyme) mutant F146R/N376I N-terminal His6-tag

substrate: NADPH; H+; O2; Hexadecane


substrate_name: NADPH; H+; Hexadecane; O2

sequence_variant_note: Resolved canonical sequence from UniProtKB:A4IU28 direct accession lookup; canonical sequence reused from live UniProt record on 2026-06-15 and applied mutation signature L320V to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: long-chain alkane monooxygenase(Enzyme) mutant L320V N-terminal His6-tag

substrate: NADPH; H+; Hexadecane; O2


substrate_name: O2; Hexadecane; NADPH; H+

sequence_variant_note: Resolved canonical sequence from UniProtKB:A4IU28 direct accession lookup; canonical sequence reused from live UniProt record on 2026-06-15 and applied mutation signature F146N/N376I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: long-chain alkane monooxygenase(Enzyme) mutant F146N/N376I N-terminal His6-tag

substrate: O2; Hexadecane; NADPH; H+


sequence_variant_note: Resolved canonical sequence from UniProtKB:A4IU28 direct accession lookup; canonical sequence reused from live UniProt record on 2026-06-15 and applied mutation signature F146C/N376I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: long-chain alkane monooxygenase(Enzyme) mutant F146C/N376I N-terminal His6-tag


substrate_name: Hexadecane; NADPH; O2; H+

sequence_variant_note: Resolved canonical sequence from UniProtKB:A4IU28 direct accession lookup; canonical sequence reused from live UniProt record on 2026-06-15 and applied mutation signature L320A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: long-chain alkane monooxygenase(Enzyme) mutant L320A N-terminal His6-tag

substrate: Hexadecane; NADPH; O2; H+


substrate_name: NADPH; O2; H+; Hexadecane

sequence_variant_note: Resolved canonical sequence from UniProtKB:A4IU28 direct accession lookup; canonical sequence reused from live UniProt record on 2026-06-15 and applied mutation signature F146E/N376I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: long-chain alkane monooxygenase(Enzyme) mutant F146E/N376I N-terminal His6-tag

substrate: NADPH; O2; H+; Hexadecane


substrate_name: O2; NADPH; H+; Hexadecane

sequence_variant_note: Resolved canonical sequence from UniProtKB:A4IU28 direct accession lookup; canonical sequence reused from live UniProt record on 2026-06-15 and applied mutation signature A102D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: long-chain alkane monooxygenase(Enzyme) mutant A102D N-terminal His6-tag

substrate: O2; NADPH; H+; Hexadecane


substrate_name: H+; O2; NADPH; Hexadecane

sequence_source: UniProtKB:A4IU28 direct accession lookup; canonical sequence reused from live UniProt record on 2026-06-15

substrate: H+; O2; NADPH; Hexadecane


substrate_name: O2; H+; NADPH; Hexadecane

sequence_variant_note: Resolved canonical sequence from UniProtKB:A4IU28 direct accession lookup; canonical sequence reused from live UniProt record on 2026-06-15 and applied mutation signature A102E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: long-chain alkane monooxygenase(Enzyme) mutant A102E N-terminal His6-tag

substrate: O2; H+; NADPH; Hexadecane


sequence_variant_note: Resolved canonical sequence from UniProtKB:A4IU28 direct accession lookup; canonical sequence reused from live UniProt record on 2026-06-15 and applied mutation signature F146Q/N376I to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: long-chain alkane monooxygenase(Enzyme) mutant F146Q/N376I N-terminal His6-tag


organism: Geobacillus thermodenitrificans

substrate_name: hexadecane

substrate: hexadecane


enzyme_display_name: pentalenolactone synthase

organism: Streptomyces arenae

substrate_name: pentalenolactone F

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup E3VWI3; UniProtKB reviewed (Swiss-Prot) and applied mutation signature M81A to reconstruct the assayed variant sequence.

enzyme: pentalenolactone synthase

substrate: pentalenolactone F


sequence_source: UniProtKB REST direct lookup E3VWI3; UniProtKB reviewed (Swiss-Prot)

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


enzyme_display_name: L-methionine (R)-S-oxide reductase

organism: Escherichia coli

substrate_name: L-Methionine (R)-S-oxide

sequence_source: UniProtKB REST direct lookup P76270; UniProtKB reviewed (Swiss-Prot)

enzyme: L-methionine (R)-S-oxide reductase

substrate: L-Methionine (R)-S-oxide


substrate_name: Reduced thioredoxin

substrate: Reduced thioredoxin


organism: Neisseria meningitidis

substrate_name: L-methionine (R)-S-oxide

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

substrate: L-methionine (R)-S-oxide


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


organism: Thermoplasma acidophilum

sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q9HJW5; UniProtKB unreviewed (TrEMBL) and applied mutation signature C15S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct lookup Q9HJW5; UniProtKB unreviewed (TrEMBL) and applied mutation signature C60S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB REST direct lookup Q9HJW5; UniProtKB unreviewed (TrEMBL)

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


enzyme_display_name: cholestanetriol 26-monooxygenase

organism: Pseudonocardia autotrophica

substrate_name: O2; NADPH; H+; Vitamin D3

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession C4B644, checked directly during this review and applied mutation signature T70R/V156L/E216M/E384R to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NADP+

proof_lines: SABIO-RK modifier species: cholestanetriol 26-monooxygenase(Enzyme) mutant Vdh-K1 (T70R/V156L/E216M/E384R)

enzyme: cholestanetriol 26-monooxygenase

substrate: O2; NADPH; H+; Vitamin D3


substrate_name: O2; Vitamin D3; H+; NADPH

sequence_source: UniProtKB reviewed accession C4B644, checked directly during this review

substrate: O2; Vitamin D3; H+; NADPH


organism: Rattus norvegicus

substrate_name: NADPH; H+; 3alpha,7alpha,12alpha-Trihydroxy-5beta-cholestane; O2

sequence_source: UniProtKB reviewed accession P17178, checked directly during this review


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession E3VWI3, checked directly during this review and applied mutation signature M77S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession E3VWI3, checked directly during this review

proof_lines: recombinant wild-type enzyme, pH 8.0, 30°C


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession E3VWI3, checked directly during this review and applied mutation signature F232L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession E3VWI3, checked directly during this review and applied mutation signature M81A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession E3VWI3, checked directly during this review and applied mutation signature F232A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession E3VWI3, checked directly during this review and applied mutation signature M81C to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant M81C-2-mercaptoethanol conjugate, pH 8.0, 30°C


organism: Mus musculus

substrate_name: t-Butylhydroperoxide

sequence_source: UniProtKB:Q9DB60 direct REST lookup on 2026-06-15

smiles: CC(C)(C)OO

substrate: t-Butylhydroperoxide


smiles: OO


substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


substrate_name: Prostamide H2

substrate: Prostamide H2


substrate_name: Reduced thioredoxin; Prostamide H2

proof_lines:
pH 7.0, 24°C
in 0.1 M KPB (pH 7.0), at 24°C
pH 7.0, 24°C, i.e. prostaglandin H2

substrate: Reduced thioredoxin; Prostamide H2


organism: Sus scrofa

substrate_name: Prostamide H2; Reduced thioredoxin

sequence_source: UniProtKB:A9CQL8 direct REST lookup on 2026-06-15

proof_lines:
i.e. prostamide H2, pH 7.0, 24°C
i.e. prostaglandin H2, pH 7.0, 24°C

substrate: Prostamide H2; Reduced thioredoxin


organism: Penicillium olsonii

substrate_name: fisetin

sequence_source: UniProtKB:A7Y9J1 direct REST lookup on 2026-06-15

substrate: fisetin


organism: Streptomyces sp.

substrate_name: quercetin

sequence_source: UniProtKB:A2VA43 direct REST lookup on 2026-06-15

substrate: quercetin


enzyme_display_name: pentachlorophenol monooxygenase

organism: Sphingobium chlorophenolicum

substrate_name: Pentachlorophenol

sequence_variant_note: Resolved canonical sequence from UniProtKB:P42535 direct REST lookup on 2026-06-15 and applied mutation signature R235K to reconstruct the assayed variant sequence.

enzyme: pentachlorophenol monooxygenase

substrate: Pentachlorophenol


substrate_name: Pentachlorophenol; H+; NADPH; O2

sequence_variant_note: Resolved canonical sequence from UniProtKB:P42535 direct REST lookup on 2026-06-15 and applied mutation signature Y397F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pentachlorophenol monooxygenase(Enzyme) mutant Y397F

substrate: Pentachlorophenol; H+; NADPH; O2


sequence_variant_note: Resolved canonical sequence from UniProtKB:P42535 direct REST lookup on 2026-06-15 and applied mutation signature F85A to reconstruct the assayed variant sequence.


substrate_name: Pentachlorophenol; O2; NADPH; H+

sequence_source: UniProtKB:P42535 direct REST lookup on 2026-06-15

proof_lines: SABIO-RK modifier species: pentachlorophenol monooxygenase(Enzyme) mutant F85A

substrate: Pentachlorophenol; O2; NADPH; H+


substrate_name: NADPH; Pentachlorophenol; H+; O2

sequence_variant_note: Resolved canonical sequence from UniProtKB:P42535 direct REST lookup on 2026-06-15 and applied mutation signature Y216F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pentachlorophenol monooxygenase(Enzyme) mutant Y216F

substrate: NADPH; Pentachlorophenol; H+; O2


substrate_name: NADPH; O2; H+; Pentachlorophenol

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P42535 (PCPB_SPHCR), retrieved 2026-06-15 from https://rest.uniprot.org/uniprotkb/P42535.json and applied mutation signature R235K to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: pentachlorophenol monooxygenase(Enzyme) mutant R235K

substrate: NADPH; O2; H+; Pentachlorophenol


substrate_name: H+; Pentachlorophenol; O2; NADPH

sequence_source: UniProtKB reviewed accession P42535 (PCPB_SPHCR), retrieved 2026-06-15 from https://rest.uniprot.org/uniprotkb/P42535.json

assay_conditions_summary: pH 7; 295.15 K; cofactor NADPH

substrate: H+; Pentachlorophenol; O2; NADPH


enzyme_display_name: vitamin D 25-hydroxylase

substrate_name: Vitamin D2

sequence_source: UniProtKB reviewed accession Q6VVX0 (CP2R1_HUMAN), retrieved 2026-06-15 from https://rest.uniprot.org/uniprotkb/Q6VVX0.json

enzyme: vitamin D 25-hydroxylase

substrate: Vitamin D2


substrate_name: H+; O2; NADPH; Vitamin D3

proof_lines: pH and temperature not specified in the publication

substrate: H+; O2; NADPH; Vitamin D3


substrate_name: Vitamin D3

substrate: Vitamin D3


substrate_name: 1alpha-hydroxyvitamin D3

sequence_source: UniProtKB reviewed accession P51589 (CP2J2_HUMAN), retrieved 2026-06-15 from https://rest.uniprot.org/uniprotkb/P51589.json

substrate: 1alpha-hydroxyvitamin D3


substrate_name: vitamin D3

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession C4B644 (CPVDH_PSEAH), retrieved 2026-06-15 from https://rest.uniprot.org/uniprotkb/C4B644.json and applied mutation signature T70R/V156L/E216M/E384R to reconstruct the assayed variant sequence.

proof_lines: mutant T70R/V156L/E216M/E384R, 30°C, pH not specified in the publication

substrate: vitamin D3


substrate_name: 25-hydroxy-vitamin D3

sequence_source: UniProtKB reviewed accession C4B644 (CPVDH_PSEAH), retrieved 2026-06-15 from https://rest.uniprot.org/uniprotkb/C4B644.json

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

substrate: 25-hydroxy-vitamin D3


sequence_source: UniProtKB reviewed accession P51590 (CP2J3_RAT), retrieved 2026-06-15 from https://rest.uniprot.org/uniprotkb/P51590.json


substrate_name: 1alpha-hydroxyvitamin D2

sequence_source: UniProtKB reviewed accession P08683 (CP2CB_RAT), retrieved 2026-06-15 from https://rest.uniprot.org/uniprotkb/P08683.json

proof_lines:
pH 7.4, 37°C, 25-hydroxylation
pH 7.4, 37°C, 26-hydroxylation
pH 7.4, 37°C, 24-hydroxylation

substrate: 1alpha-hydroxyvitamin D2


substrate_name: 1-alpha-Hydroxyvitamin D2

substrate: 1-alpha-Hydroxyvitamin D2


substrate_name: H+; Vitamin D3; O2; NADPH

substrate: H+; Vitamin D3; O2; NADPH


substrate_name: 1alpha-Hydroxyvitamin D3

smiles: O

substrate: 1alpha-Hydroxyvitamin D3


sequence_source: UniProtKB reviewed accession Q02318 (CP27A_HUMAN), retrieved 2026-06-15 from https://rest.uniprot.org/uniprotkb/Q02318.json


enzyme_display_name: anthocyanidin 3-O-glucosyltransferase

organism: Vitis labrusca

substrate_name: cyanidin

sequence_source: UniProtKB REST accession lookup A6N928 (2026-06-15)

enzyme: anthocyanidin 3-O-glucosyltransferase

substrate: cyanidin


substrate_name: UDP-glucose

substrate: UDP-glucose


organism: Vitis vinifera

sequence_source: UniProtKB REST accession lookup P51094 (2026-06-15)


organism: Zea mays

substrate_name: UDP-D-glucose

sequence_source: UniProtKB REST accession lookup Q8W2B7 (2026-06-15)

substrate: UDP-D-glucose


substrate_name: DIBOA

sequence_source: UniProtKB REST accession lookup B4G072 (2026-06-15)

substrate: DIBOA


substrate_name: UDP-D-glucose; DIMBOA

substrate: UDP-D-glucose; DIMBOA


substrate_name: DIMBOA

substrate: DIMBOA


organism: Petunia hybrida

substrate_name: UDP-D-galactose; Kaempferol

sequence_source: UniProtKB REST accession lookup Q9SBQ8 (2026-06-15)

substrate: UDP-D-galactose; Kaempferol


organism: Petunia x hybrida

substrate_name: quercetin 3-O-galactoside

proof_lines: pH 7.5, 43°C, cosubstrate quercetin, forward reaction

proof_lines: pH 6, 43°C, cosubstrate kaempferol 3-O-galactoside, reverse reaction

substrate: quercetin 3-O-galactoside


organism: Prunus persica

substrate_name: quercetin

sequence_source: UniProtKB REST accession lookup A0A251QUJ4 (2026-06-15)

substrate: quercetin


organism: Aspergillus terreus

sequence_source: UniProtKB REST accession lookup A0A1B0UHJ4 (2026-06-15)


organism: Streptomyces fradiae

sequence_variant_note: Resolved canonical sequence from UniProtKB:P95748 canonical sequence with H123N reconstructed from selected mutation signature; REST lookup 2026-06-15 release 2026_02. and applied mutation signature H123N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P95748 canonical sequence with H123A reconstructed from selected mutation signature; REST lookup 2026-06-15 release 2026_02. and applied mutation signature H123A to reconstruct the assayed variant sequence.


enzyme_display_name: salicylate carboxymethyltransferase

organism: Antirrhinum majus

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProtKB:Q8H6N2 canonical sequence, REST lookup 2026-06-15 release 2026_02.

proof_lines:
with salicylic acid, pH 7.5, 20°C
pH 7.5, 20°C

enzyme: salicylate carboxymethyltransferase

substrate: S-adenosyl-L-methionine


organism: Arabidopsis lyrata

substrate_name: salicylic acid

sequence_source: UniProtKB:Q6XMI1 REST lookup 2026-06-15 reported Inactive/DELETED; no accepted sequence used.

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

proof_lines:
pH 7.7, 30°C
apparent Km-value, pH 7.7, 30°C

substrate: salicylic acid


organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q6XMI3 canonical sequence, REST lookup 2026-06-15 release 2026_02.


organism: Clarkia breweri

substrate_name: salicylate

sequence_source: UniProtKB:Q9SPV4 canonical sequence, REST lookup 2026-06-15 release 2026_02.

substrate: salicylate


substrate_name: S-Adenosyl-L-methionine; Salicylate

proof_lines:
nontagged protein, pH 7.5, 20°C
His-tagged protein, pH 7.5, 20°C
pH 7.5, 30°C

substrate: S-Adenosyl-L-methionine; Salicylate


enzyme_display_name: selenocysteine Se-methyltransferase

organism: Astragalus bisulcatus

substrate_name: DL-selenohomocysteine

sequence_source: UniProtKB:P56707 canonical sequence, REST lookup 2026-06-15 release 2026_02.

smiles: NC(CC[SeH])C(=O)O

enzyme: selenocysteine Se-methyltransferase

substrate: DL-selenohomocysteine


substrate_name: L-selenocysteine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P56707 canonical sequence with A184T reconstructed from selected mutation signature; REST lookup 2026-06-15 release 2026_02. and applied mutation signature A184T to reconstruct the assayed variant sequence.

substrate: L-selenocysteine


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

proof_lines: mutant enzyme A184T, wild-type enzyme is not active with L-homocysteine


proof_lines: pH 6, 30°C, cosubstrate: S-adenosyl-L-methionine


organism: Escherichia coli

substrate_name: L-homocysteine

sequence_source: UniProtKB:Q47690 canonical sequence, REST lookup 2026-06-15 release 2026_02; context only because EC annotation contradicts selected row.

substrate: L-homocysteine


substrate_name: L-Selenocysteine

sequence_source: UniProtKB Q47690 canonical sequence from direct REST lookup on 2026-06-15

substrate: L-Selenocysteine


proof_lines: app. Km-value with [methyl-14C]S-adenosyl-L-methionine, pH 6.5, 30°C


substrate_name: Selenohomocysteine

substrate: Selenohomocysteine


substrate_name: Acetyl-CoA; Benzyl alcohol

sequence_source: UniProtKB O64988 canonical sequence from direct REST lookup on 2026-06-15

assay_conditions_summary: cofactor CoA

substrate: Acetyl-CoA; Benzyl alcohol


sequence_source: UniProtKB Q9SPU3 canonical sequence from direct REST lookup on 2026-06-15


sequence_source: UniProtKB Q8GT21 canonical sequence from direct REST lookup on 2026-06-15


substrate_name: Acetyl-CoA

assay_conditions_summary: pH 7.7; 295.15 K; cofactor CoA

substrate: Acetyl-CoA


organism: Clarkia concinna

substrate_name: Benzyl alcohol; Acetyl-CoA

sequence_source: UniProtKB Q9SQ01 canonical sequence from direct REST lookup on 2026-06-15

substrate: Benzyl alcohol; Acetyl-CoA


sequence_source: UniProtKB Q9SQ00 canonical sequence from direct REST lookup on 2026-06-15


sequence_source: UniProtKB Q9SQ02 canonical sequence from direct REST lookup on 2026-06-15


organism: Salvia splendens

substrate_name: monodemalonylsalvianin

sequence_source: UniProtKB Q6TXD2 canonical sequence from direct REST lookup on 2026-06-15

assay_conditions_summary: pH 7; 303.15 K; cofactor CoA

substrate: monodemalonylsalvianin


substrate_name: malonyl-CoA

proof_lines:
native enzyme, at pH 7.0 and 30°C
recombinant enzyme, at pH 7.0 and 30°C

substrate: malonyl-CoA


organism: Glycine max

substrate_name: kaempferol

sequence_source: UniProtKB D3Y5N8 canonical sequence from direct REST lookup on 2026-06-15

substrate: kaempferol


organism: Vitis labrusca

sequence_source: UniProtKB A6N928 canonical sequence from direct REST lookup on 2026-06-15


enzyme_display_name: inositol-tetrakisphosphate 1-kinase

organism: Homo sapiens

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

proof_lines: SABIO-RK modifier species: inositol-tetrakisphosphate 1-kinase(Enzyme) mutant ITPK1 G163A

enzyme: inositol-tetrakisphosphate 1-kinase


proof_lines: SABIO-RK modifier species: inositol-tetrakisphosphate 1-kinase(Enzyme) mutant ITPK1 K157A


proof_lines: SABIO-RK modifier species: inositol-tetrakisphosphate 1-kinase(Enzyme) mutant ITPK1 D281A


proof_lines: SABIO-RK modifier species: inositol-tetrakisphosphate 1-kinase(Enzyme) mutant ITPK1 R106A


enzyme_display_name: mevalonate 3-kinase

organism: Picrophilus oshimae

substrate_name: (R)-mevalonate

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

enzyme: mevalonate 3-kinase

substrate: (R)-mevalonate


organism: Picrophilus torridus

sequence_source: UniProt REST Q6KZB1 FASTA/JSON direct lookup, release 2026_02


organism: Thermoplasma acidophilum

sequence_source: UniProt REST Q9HIN1 FASTA/JSON direct lookup, release 2026_02

proof_lines:
pH 8.5, 55°C
Raw SKiD Env: Temp=55°C, pH=8.5


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9HIN1 FASTA/JSON direct lookup, release 2026_02 and applied mutation signature L18A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9HIN1 FASTA/JSON direct lookup, release 2026_02 and applied mutation signature T275A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9HIN1 FASTA/JSON direct lookup, release 2026_02 and applied mutation signature R185K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9HIN1 FASTA/JSON direct lookup, release 2026_02 and applied mutation signature S105A to reconstruct the assayed variant sequence.


sequence_source: UniProtKB A0A1B0UHJ4 direct accession sequence, retrieved 2026-06-15

proof_lines: with farnesyl diphosphate as cosubstrate, at pH 7.5 and 37°C

proof_lines: with 1 as cosubstrate, at pH 7.5 and 37°C

proof_lines: with 2-methyl-1-(2,4,6-trihydroxyphenyl)propan-1-one as cosubstrate, at pH 7.5 and 37°C


substrate_name: geranyl diphosphate

smiles: CC(C)=CCC/C(C)=C/COP(=O)(O)OP(=O)(O)O

substrate: geranyl diphosphate


substrate_name: dimethylallyl diphosphate

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

substrate: dimethylallyl diphosphate


organism: Humulus lupulus

mutation_signature: truncated recombinant protein

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

proof_lines: truncated recombinant protein, pH 7.0, 30°C


substrate_name: Dimethylallyl diphosphate; Naringenin chalcone


sequence_source: UniProtKB A0A0B5A051 direct accession sequence, retrieved 2026-06-15

proof_lines: presence of prenyltransferase PT2, pH 7.0, 30°C

substrate: Dimethylallyl diphosphate; Naringenin chalcone


enzyme_display_name: spermine synthase

substrate_name: spermidine

sequence_variant_note: Resolved canonical sequence from UniProtKB P52788 direct accession sequence with row-specific E353Q substitution reconstructed on 2026-06-15 and applied mutation signature E353Q to reconstruct the assayed variant sequence.

proof_lines:
mutant E353Q, pH 7.5, 37°C
mutant E353Q

enzyme: spermine synthase

substrate: spermidine


sequence_variant_note: Resolved canonical sequence from UniProtKB P52788 direct accession sequence with row-specific D201N substitution reconstructed on 2026-06-15 and applied mutation signature D201N to reconstruct the assayed variant sequence.

proof_lines:
mutant D201N, pH 7.5, 37°C
mutant D201N


sequence_variant_note: Resolved canonical sequence from UniProtKB P52788 direct accession sequence with row-specific D276N substitution reconstructed on 2026-06-15 and applied mutation signature D276N to reconstruct the assayed variant sequence.

proof_lines:
mutant D276N, pH 7.5, 37°C
mutant D276N


sequence_variant_note: Resolved canonical sequence from UniProtKB P52788 direct accession sequence with row-specific D201A substitution reconstructed on 2026-06-15 and applied mutation signature D201A to reconstruct the assayed variant sequence.

proof_lines:
mutant D201A, pH 7.5, 37°C
mutant D201A


sequence_source: UniProtKB P52788 direct accession sequence, retrieved 2026-06-15

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


substrate_name: S-Adenosylmethioninamine; Spermidine

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

substrate: S-Adenosylmethioninamine; Spermidine


substrate_name: ATP

sequence_source: UniProtKB Q9SBA5 direct accession sequence, retrieved 2026-06-15

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

substrate: ATP


organism: Bos taurus

sequence_source: UniProtKB P0C0T1 direct accession sequence, retrieved 2026-06-15

assay_conditions_summary: cofactor ATP


sequence_source: UniProtKB Q13572 direct accession sequence, retrieved 2026-06-15

assay_conditions_summary: pH 7.2; 310.15 K; cofactor ATP

proof_lines:
pH 7.2, 37°C, recombinant enzyme
Raw SKiD Env: Temp=37°C, pH=7.2


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q9HIN1 on 2026-06-15 and applied mutation signature T275A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST direct accession lookup for Q9HIN1 on 2026-06-15 and applied mutation signature R185K to reconstruct the assayed variant sequence.


enzyme_display_name: hydroxymethylpyrimidine kinase

organism: Bacillus subtilis

enzyme: hydroxymethylpyrimidine kinase


sequence_source: UniProtKB REST direct accession lookup for P76422 on 2026-06-15

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


organism: Salmonella enterica subsp. enterica serovar Typhimurium

sequence_source: UniProtKB REST direct accession lookup for P55882 on 2026-06-15

assay_conditions_summary: pH 8; 298.15 K; cofactor ATP

proof_lines:
pH 8.0, 25°C
pH 7.0, 25°C, recombinant enzyme, MgATP
pH 7.0, 25°C, recombinant enzyme


organism: Staphylococcus aureus

substrate_name: pyridoxine

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

substrate: pyridoxine


proof_lines: mutant C110A, pH not specified in the publication, temperature not specified in the publication


substrate_name: pyridoxal

proof_lines: mutant C214D, pH not specified in the publication, temperature not specified in the publication

substrate: pyridoxal


organism: Thermus thermophilus

sequence_source: UniProtKB REST direct accession lookup for Q5SKG3 on 2026-06-15


organism: Zea mays

sequence_source: UniProtKB REST direct accession lookup for Q2UVH9 on 2026-06-15


enzyme_display_name: inositol-hexakisphosphate 5-kinase

substrate_name: myo-Inositol hexakisphosphate; ATP

sequence_source: UniProtKB REST direct accession lookup for Q9UHH9 on 2026-06-15

enzyme: inositol-hexakisphosphate 5-kinase

substrate: myo-Inositol hexakisphosphate; ATP


substrate_name: Inositol hexakisphosphate

sequence_source: UniProtKB REST direct accession lookup for Q96PC2 on 2026-06-15

substrate: Inositol hexakisphosphate


proof_lines: isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C

proof_lines: isoform PPIP5K2, using 1D-myo-inositol hexakisphosphate as cosubstrate, in 20 mM HEPES-NaOH pH 7.2, 50 mM KCl, at 37°C

proof_lines: isoform PPIP5K2, in 20 mM HEPES-NaOH pH 7.2, 50 m MKCl, at 37°C


substrate_name: myo-Inositol hexakisphosphate

sequence_source: UniProtKB reviewed accession Q6PFW1

substrate: myo-Inositol hexakisphosphate


substrate_name: ATP; myo-Inositol hexakisphosphate

substrate: ATP; myo-Inositol hexakisphosphate


substrate_name: 1D-myo-inositol hexakisphosphate

sequence_source: UniProtKB reviewed accession O43314

substrate: 1D-myo-inositol hexakisphosphate


sequence_source: UniProtKB reviewed accession Q92551

assay_conditions_summary: pH 6.95; 310.15 K; cofactor ATP


organism: Mus musculus

sequence_source: UniProtKB reviewed accession Q6PD10


sequence_source: UniProtKB reviewed accession Q6ZQB6


organism: Saccharomyces cerevisiae

sequence_source: UniProtKB reviewed accession Q12494


organism: Haemophilus influenzae

substrate_name: D-Ribitol 5-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession Q48230 canonical sequence with source-documented K386A substitution reconstructed and applied mutation signature K386A to reconstruct the assayed variant sequence.

substrate: D-Ribitol 5-phosphate


substrate_name: CTP

sequence_source: UniProtKB reviewed accession Q48230

column_label: Table label: Table 1: Steady State Kinetic Parameters Describing Substrate Specificity of Reductase and Cytidylyltransferase Activities of Bcs1. Row: CTP. Section: (2) cytidylyltransferase. Columns read: K m (uM) cell 99, k cat (s^-1) cell 13, k cat / K m (x10^-5 M^-1 s^-1) cell 1.3. metric: kcat; raw value: 13; raw unit: s^-1; normalized value: 13.0 s^(-1); metric: Km; raw value: 99; raw unit: uM; normalized value: 0.099 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 131.3131313131313 s^-1 mM^-1; assay condition: C-terminally His-tagged Bcs1 (CDP-ribitol synthase, cytidylyltransferase activity); all assays were carried out at 25 degrees C and were performed in triplicate; cytidylyltransferase activity was monitored in a continuous coupled assay for the detection of inorganic pyrophosphate in a mixture containing 25 mM HEPES (pH 7.2), 1 mM DTT, 0.01% Triton X-100, 10 mM MgCl2, and 200 uM MESG; steady state parameters were determined in the presence of saturating cosubstrate. Export row conditions: pH 7.2; 298.15 K.

normalized_value_unit_evidence: Table 1 section (2) cytidylyltransferase, row CTP: kcat 13 s^-1 = 13.0 s^(-1); Km 99 uM = 0.099 mM (1 uM = 0.001 mM); kcat/Km 131.3131313131313 s^-1 mM^-1 as the exact quotient of this row's own printed kcat and Km cells (13 s^-1 divided by 0.099 mM). The row's printed kcat/Km cell reads 1.3 in a column headed (x10-5 M-1 s-1), i.e. 1.3 x 10^5 M^-1 s^-1 = 130.0 s^-1 mM^-1; the exact quotient 131.3131313131313 rounds to 1.3 x 10^5 at the printed cell's own two-significant-figure precision, so the printed cell and the exported quotient agree and the difference is printed precision only. In the PDF text the plus-minus sign renders as ( and the header multiplication sign as x.

raw_value_unit_evidence: Table 1: Steady State Kinetic Parameters Describing Substrate Specificity of Reductase and Cytidylyltransferase Activities of Bcs1 | metric header row of Table 1: Kma (µM) kcata (s-1) kcat/Km (x10-5 M-1 s-1); section header: (2) cytidylyltransferase | row: CTP 99 ( 9.1 13 ( 0.5 1.3 | cells read: K m = 99 uM; k cat = 13 s^-1; k cat / K m = 1.3 x 10^5 M^-1 s^-1

row_label: (2) cytidylyltransferase | CTP

substrate: CTP


sequence_source: UniProtKB reviewed accession Q48230 canonical sequence with source-documented K386A substitution reconstructed


enzyme_display_name: apo-salmochelin esterase

organism: Escherichia coli

substrate_name: triglucosyl-enterobactin

sequence_source: UniProtKB:A0A0H2V871 direct lookup on 2026-06-15; reviewed Swiss-Prot entry IROE_ECOL6, 318 aa.

enzyme: apo-salmochelin esterase

substrate: triglucosyl-enterobactin


substrate_name: monoglucosyl-enterobactin

substrate: monoglucosyl-enterobactin


substrate_name: diglucosyl-enterobactin

substrate: diglucosyl-enterobactin


organism: Mycobacterium tuberculosis

substrate_name: 4-nitrophenyl phosphate

sequence_source: UniProtKB:O33194 direct lookup on 2026-06-15; reviewed Swiss-Prot entry G3PP_MYCTU, 353 aa.

substrate: 4-nitrophenyl phosphate


substrate_name: DL-glycerol 3-phosphate

smiles: O=P(O)(O)OCC(O)CO

substrate: DL-glycerol 3-phosphate


substrate_name: L-glycerol 3-phosphate

substrate: L-glycerol 3-phosphate


substrate_name: D-ribulose 5-phosphate

substrate: D-ribulose 5-phosphate


substrate_name: Glycerol 2-phosphate

smiles: O=P(O)(O)OC(CO)CO

substrate: Glycerol 2-phosphate


organism: Aspergillus saitoi

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature E411D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature E124D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature D269E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature E414D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E414D


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature E474D to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E411D


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct lookup on 2026-06-15; reviewed Swiss-Prot entry MNS1B_ASPPH, 513 aa. and applied mutation signature E273D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB Q48230 direct REST lookup on 2026-06-15 by applying R18A. and applied mutation signature R18A to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB Q48230 direct REST lookup on 2026-06-15 by applying R18A.


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


enzyme_display_name: [protein-PII] uridylyltransferase

substrate_name: UTP; [Protein-PII]

sequence_source: UniProtKB P27249 direct REST lookup on 2026-06-15

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

enzyme: [protein-PII] uridylyltransferase

substrate: UTP; [Protein-PII]


substrate_name: ATP

substrate: ATP


substrate_name: UTP

substrate: UTP


substrate_name: GTP

substrate: GTP


substrate_name: ferric monoglucosyl-enterobactin

sequence_source: UniProtKB A0A0H2V871 direct REST lookup on 2026-06-15

substrate: ferric monoglucosyl-enterobactin


substrate_name: enterobactin

substrate: enterobactin


substrate_name: ferric enterobactin

substrate: ferric enterobactin


substrate_name: ferric diglucosyl-enterobactin

substrate: ferric diglucosyl-enterobactin


proof_lines: turnover number above 0.13 1/sec, at pH 7.5 and 23°C


substrate_name: ferric triglucosyl-enterobactin

substrate: ferric triglucosyl-enterobactin


substrate_name: L-methionine (R)-S-oxide

sequence_variant_note: Resolved canonical sequence from UniProt REST Q9HJW5 canonical sequence with validated C60S substitution reconstruction and applied mutation signature C60S to reconstruct the assayed variant sequence.

substrate: L-methionine (R)-S-oxide


sequence_source: UniProt REST Q9HJW5 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProt REST Q9HJW5 canonical sequence with validated C15S substitution reconstruction and applied mutation signature C15S to reconstruct the assayed variant sequence.


enzyme_display_name: methionine synthase

organism: Sus scrofa

sequence_source: UniProt REST Q9MYZ4 canonical sequence

enzyme: methionine synthase


substrate_name: L-Homocysteine

substrate: L-Homocysteine


organism: Streptomyces fradiae

substrate_name: S-adenosyl-L-methionine

sequence_source: UniProt REST P95748 canonical sequence

substrate: S-adenosyl-L-methionine


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

proof_lines: pH 7.5, 24°C, cosubstrate: 0.89 mM dTDP-3-methylamino-3,6-dideoxy-alpha-D-glucopyranose

proof_lines: pH and temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProt REST P95748 canonical sequence with validated H123N substitution reconstruction and applied mutation signature H123N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST P95748 canonical sequence with validated H123A substitution reconstruction and applied mutation signature H123A to reconstruct the assayed variant sequence.


enzyme_display_name: UDP-sugar diphosphatase

substrate_name: NADH

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADH

enzyme: UDP-sugar diphosphatase

substrate: NADH


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NMN

substrate: NMN


substrate_name: AMP

substrate: AMP


substrate_name: UDP-D-glucose

proof_lines: chimera UshA catalytic domain/CpdB specificity domain, pH not specified in the publication, temperature not specified in the publication

proof_lines: chimera CpdB catalytic domain/UshA specificity domain, pH not specified in the publication, temperature not specified in the publication

substrate: UDP-D-glucose


substrate_name: ADP-D-ribose

sequence_source: UniProtKB direct lookup Q9D142 on 2026-06-15

assay_conditions_summary: pH 8; 310.15 K; cofactor ADP

proof_lines: in 50 mM Tris-HCl, pH 8.0, 10 mM Mg2+, at 37°C

proof_lines: in 50 mM Tris-HCl, pH 8.0, 10 mM MgCl2, at 37°C

substrate: ADP-D-ribose


substrate_name: UDPglucose; H2O

sequence_source: UniProtKB direct lookup Q865Y9 on 2026-06-15

assay_conditions_summary: cofactor ADP

substrate: UDPglucose; H2O


organism: Yersinia intermedia

substrate_name: UDP-glucose

sequence_source: UniProtKB direct lookup A4URQ8 on 2026-06-15

substrate: UDP-glucose


enzyme_display_name: gamma-resorcylate decarboxylase

organism: Agrobacterium tumefaciens

sequence_source: UniProtKB direct lookup Q60FX6 on 2026-06-15

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

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

enzyme: gamma-resorcylate decarboxylase


organism: Polaromonas sp. JS666

sequence_source: UniProtKB direct lookup Q12BV1 on 2026-06-15

proof_lines:
pH 7.0, 30°C
Raw SKiD Env: Temp=30°C, pH=7


organism: Rhizobium sp.

sequence_source: UniProtKB direct lookup Q60GU1 on 2026-06-15


organism: Clostridioides difficile

proof_lines: isozyme toxin A, with MgCl2 and 150 mM KCl


enzyme_display_name: methylglutaconyl-CoA hydratase

organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed accession F4JML5 direct REST check, 2026-06-15

assay_conditions_summary: pH 8; 303.15 K; cofactor CoA

enzyme: methylglutaconyl-CoA hydratase


organism: Homo sapiens

substrate_name: trans-3-Methylglutaconyl-CoA; H2O

sequence_source: UniProtKB reviewed accession Q13825 direct REST check, 2026-06-15

substrate: trans-3-Methylglutaconyl-CoA; H2O


enzyme_display_name: galactarate dehydratase

substrate_name: D-Galactarate

sequence_source: UniProtKB reviewed accession P39829 direct REST check, 2026-06-15

column_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1). Table 1, row GalcD; column kcat (s^-1) = 22.0; column Km (uM) = 800; column kcat/Km (M^-1 s^-1) = 2.7 x 10^4. captured primary segment: GalcD | kcat 22.0 ± 0.7 s^-1 | Km 800 ± 9 uM | kcat/Km 2.7 x 10^4 M^-1 s^-1

normalized_value_unit_evidence: kcat: printed Table 1 cell 22.0 s^-1; the printed unit s^-1 is already the export unit, so no unit conversion applies and the paper value is 22.0 s^(-1); the exported value is 22.0 s^(-1). Km: printed Table 1 cell 800 uM; 1 uM is 1/1000 mM, so 800 / 1000 = 0.8 mM; the exported value is 0.8 mM. kcat/Km: printed Table 1 cell 2.7 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 2.7 x 10^4 / 1000 = 27.0 s^(-1)*mM^(-1); the exported value is 27.5 s^(-1)*mM^(-1), the full-precision quotient of the two printed component cells.

raw_value_unit_evidence: Table 1, row GalcD: kcat = 22.0 s^-1; Km = 800 uM; printed kcat/Km = 2.7 x 10^4 M^-1 s^-1.

row_label: Table 1, row GalcD

enzyme: galactarate dehydratase

substrate: D-Galactarate


table_label: Table 1: Kinetic Constants for Enzymes in the (D)-Glucarate/Galactarate Catabolic Pathway (Biochemistry 1998, volume 37, pages 14369-14375); printed column heads kcat (s^-1) | Km (uM) | kcat/Km (M^-1 s^-1)


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: galactarate

sequence_source: UniProtKB reviewed accession Q8ZL58 direct REST check, 2026-06-15

proof_lines: pH 8.0, 25°C, His6-tagged recombinant enzyme

substrate: galactarate


organism: Salmonella enterica subsp. enterica serovar Typhimurium str. LT2


sequence_source: UniProtKB:Q12563 direct accession lookup; checked 2026-06-15


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature E414D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature E124D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E124D


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature E124Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E124Q


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature E273D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E273D


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature D269E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant D269E


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q12563 direct accession lookup; checked 2026-06-15 and applied mutation signature E474D to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: mannosyl-oligosaccharide 1,2-alpha-mannosidase(Enzyme) mutant E474D


organism: Candida albicans

sequence_source: UniProtKB:Q8J0Q0 direct accession lookup; checked 2026-06-15


substrate_name: H2O; Man9GlcNAc; H2O

sequence_source: UniProtKB:Q9UKM7 direct accession lookup; checked 2026-06-15

substrate: H2O; Man9GlcNAc; H2O


organism: Neobacillus novalis

sequence_source: UniProtKB:A0A7R9KAR8 direct accession lookup; checked 2026-06-15

assay_conditions_summary: pH 6


organism: Streptococcus pneumoniae

substrate_name: Unknown

assay_conditions_summary: pH 9

proof_lines: in the coupled assay of SpGH92 and CfMan2A, with substrate 4-methylumbelliferyl alpha-D-mannopyranosyl-(1->2)-beta-D-mannopyranoside, pH 9.0-9.5, 22Â°C

substrate: Unknown


enzyme_display_name: beta-agarase

organism: Agarivorans albus

substrate_name: Agarose; H2O; Agarose

sequence: ASLVTSFEEA

wild_type_sequence: ASLVTSFEEA

sequence_source: UniProtKB:P85974 direct accession lookup; checked 2026-06-15

enzyme: beta-agarase

substrate: Agarose; H2O; Agarose


substrate_name: agarose

substrate: agarose


substrate_name: Neoagarotetraose

substrate: Neoagarotetraose


sequence_source: UniProtKB:A8W969 FASTA checked 2026-06-15


organism: Catenovulum agarivorans


organism: Cellvibrio sp. KY-GH-1


organism: Pseudoalteromonas sp. CY24

substrate_name: neoagarodecaose

sequence_source: UniProtKB:A1A3Y9 FASTA checked 2026-06-15

substrate: neoagarodecaose


organism: Wenyingzhuangia aestuarii

sequence_source: UniProtKB:A0A516RTC5 FASTA checked 2026-06-15


organism: Zobellia galactanivorans

sequence_source: UniProtKB:Q9RGX8 FASTA checked 2026-06-15


substrate_name: H2O; Agarose

sequence_source: UniProtKB:G0L322 FASTA checked 2026-06-15

substrate: H2O; Agarose


substrate_name: Agarose; H2O

sequence_source: UniProtKB:D7GXG4 FASTA checked 2026-06-15

substrate: Agarose; H2O


enzyme_display_name: creatininase

organism: Pseudomonas putida

substrate_name: creatinine

sequence_variant_note: Resolved canonical sequence from UniProtKB:P83772 FASTA checked 2026-06-15; reconstructed W174F from selected BRENDA mutation note and applied mutation signature W174F to reconstruct the assayed variant sequence.

proof_lines: mutant W174F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication

enzyme: creatininase

substrate: creatinine


sequence_variant_note: Resolved canonical sequence from UniProtKB:P83772 FASTA checked 2026-06-15; reconstructed E122Q from selected BRENDA mutation note and applied mutation signature E122Q to reconstruct the assayed variant sequence.

proof_lines: mutant E122Q, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication

proof_lines: mutant E122Q, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication


sequence_source: UniProtKB:P83772 FASTA checked 2026-06-15

proof_lines: wild-type, presence of Zn2+, pH not specified in the publication, temperature not specified in the publication

proof_lines: wild-type, presence of EDTA, semi-apo-enzyme, pH not specified in the publication, temperature not specified in the publication

proof_lines: wild-type, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P83772 FASTA checked 2026-06-15; reconstructed Y121A from selected BRENDA mutation note and applied mutation signature Y121A to reconstruct the assayed variant sequence.

proof_lines: mutant Y121A, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from UniProtKB:P83772 FASTA checked 2026-06-15; reconstructed W154F from selected BRENDA mutation note and applied mutation signature W154F to reconstruct the assayed variant sequence.

proof_lines: mutant W154F, presence of Mn2+, pH not specified in the publication, temperature not specified in the publication


substrate_name: Creatinine; H2O

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

substrate: Creatinine; H2O


enzyme_display_name: sulfinoalanine decarboxylase

sequence_source: UniProtKB:Q6ZQY3 canonical sequence, REST release 2026_02

enzyme: sulfinoalanine decarboxylase


organism: Tribolium castaneum

substrate_name: cysteine sulfinic acid

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

substrate: cysteine sulfinic acid