organism: Burkholderia plantarii

substrate_name: oil emulsion

substrate: oil emulsion


enzyme_display_name: triacylglycerol lipase

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

substrate_name: p-NP-butyrate

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

enzyme: triacylglycerol lipase

substrate: p-NP-butyrate

source: uniprot


organism: Homo sapiens

substrate_name: diacylglycerol

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

substrate: diacylglycerol


substrate_name: flutamide

substrate: flutamide


substrate_name: triacylglycerol

assay_conditions_summary: cofactor CoA

substrate: triacylglycerol


organism: Sus scrofa

substrate_name: olive oil

source_db: brenda

proof_lines:
pH 7.0, 37°C, immobilized lipase
pH 7.0, 37°C, free lipase

substrate: olive oil

source: brenda


organism: uncultured bacterium

substrate_name: 4-nitrophenyl butyrate

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

substrate: 4-nitrophenyl butyrate


substrate_name: 4-nitrophenyl laurate

substrate: 4-nitrophenyl laurate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: p-nitrophenyl butyrate (PNB)

substrate: p-nitrophenyl butyrate (PNB)


organism: Sodiomyces alcalophilus

substrate_name: p-nitrophenol acetate

substrate: p-nitrophenol acetate


organism: Rattus norvegicus


organism: Rhizopus oryzae

substrate_name: triolein

substrate: triolein


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Moesziomyces aphidis

substrate_name: tributyrin

substrate: tributyrin


organism: Mus musculus

substrate_name: oleoyl-CoA

substrate: oleoyl-CoA


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: triolein (glyceryl trioleate)

substrate: triolein (glyceryl trioleate)


organism: Pseudomonas fragi


enzyme_display_name: acetyl-CoA C-acyltransferase

substrate_name: acetoacetyl-CoA

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

mutation_type: substitution

assay_conditions_summary: pH 8.2; cofactor CoA

enzyme: acetyl-CoA C-acyltransferase

substrate: acetoacetyl-CoA


substrate_name: CoA

assay_conditions_summary: pH 7.4; cofactor CoA

proof_lines: pH 7.4, competitive versus acetyl-CoA hydrolysis

substrate: CoA


organism: Thermus thermophilus

assay_conditions_summary: pH 8; 338.15 K; cofactor CoA


substrate_name: Unknown

km_display: Not reported

ki_unit: mM

substrate: Unknown


substrate_name: nicotinamide

substrate: nicotinamide


organism: Plasmodium falciparum

substrate_name: [histone H4]-N6-acetyl-L-lysine

sequence_source: UniProtKB reviewed Q8IE47 (SIR2A_PLAF7), anchored by PMID 18729382 cloning of PF13_0152

proof_lines: with [histone H3]-N6-acetyl-L-lysine as substrate, at pH 8.0 and 37°C

proof_lines: with [peptide p300]-N6-acetyl-L-lysine as substrate, at pH 8.0 and 37°C

substrate: [histone H4]-N6-acetyl-L-lysine


organism: Saccharomyces cerevisiae


substrate_name: KSTGGAcKAPRKQ

sequence_variant_note: Resolved canonical sequence from UniProtKB P53686 canonical HST2 sequence with H135A reconstructed from PMID 16388603 identity note and applied mutation signature H135A to reconstruct the assayed variant sequence.

substrate: KSTGGAcKAPRKQ


sequence_source: UniProtKB P53686 canonical HST2 sequence anchored by PMID 16388603


organism: Thermotoga maritima

substrate_name: K382KAc-containing p53 peptide

sequence_source: UniProtKB Q9WYW0 Sir2Tm sequence, checked by EC 2.3.1.286 and Thermotoga maritima search plus PMID 22352831 Sir2Tm context

proof_lines: at 37°C, pH not specified in the publication

substrate: K382KAc-containing p53 peptide


enzyme_display_name: 8-amino-7-oxononanoate synthase

organism: Aquifex aeolicus

substrate_name: L-alanine

sequence_source: UniProtKB O66875 Aquifex aeolicus VF5 BioF sequence, checked against PMID 22484932 AqBioF context

assay_conditions_summary: pH 6; 333.15 K; cofactor CoA

enzyme: 8-amino-7-oxononanoate synthase

substrate: L-alanine


organism: Escherichia coli

substrate_name: pimeloyl-CoA

sequence_source: UniProtKB P12998 E. coli K12 BioF/AONS sequence, checked against PMID 10642176 structural/kinetic paper context

assay_conditions_summary: pH 8.6; 310.15 K; buffer 100 mM N-(2-hydroxyethyl)piperazine-N-(2-propanesulfonic acid; cofactor CoA

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

proof_lines: uncompetitive constant, pyridoxal 5-phosphate form of enzyme, coupled assay at 37°C with 100 mM N-(2-hydroxyethyl)piperazine-N-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM py

proof_lines: competitive constant, pyridoxal 5-phosphate form of enzyme, coupled assay at 37°C with 100 mM N-(2-hydroxyethyl)piperazine-N-(2-propanesulfonic acid) buffer (pH 8.6), 10 mM ATP, 50 mM NaHCO3, 10 mM MgCl2, dithiobiotin syntetase, 0.1 mM pyri

substrate: pimeloyl-CoA


organism: Geobacillus kaustophilus

sequence_source: UniProtKB Q5KY23 Geobacillus kaustophilus HTA426 BioF sequence, checked against PMID 22484932 GkBioF context and HTA426/JCM12893 strain alias


enzyme_display_name: histone acetyltransferase

substrate_name: spermidine

proof_lines:
enzyme form B
+ spermidine, enzyme form A
+ spermidine, enzyme form B

enzyme: histone acetyltransferase

substrate: spermidine


substrate_name: histone H3

substrate: histone H3


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: histone

proof_lines:
Esa1 in piccolo NuA4-complex
Gcn5
Rtt109 in complex with chaperone Vps75

substrate: histone


assay_conditions_summary: pH 7.5; 298.15 K; cofactor CoA

proof_lines: mutant E374A/E378A, presence of chaperone Vps75, pH 7.5, 25°C


enzyme_display_name: cyclomaltodextrin glucanotransferase

organism: Anaerobranca gottschalkii

substrate_name: beta-cyclodextrin

enzyme: cyclomaltodextrin glucanotransferase

substrate: beta-cyclodextrin


organism: Bacillus cereus

substrate_name: soluble starch

proof_lines: dextran-conjugated enzyme, at pH 6.5 and 60°C

substrate: soluble starch


organism: Bacillus sp. (in: firmicutes)

substrate_name: gamma-cyclodextrin

proof_lines: coupling activity, mutant Y195F and F283L

substrate: gamma-cyclodextrin


proof_lines: strain 1011, acceptor maltose, mutant Y195F

proof_lines: strain 1011, beta-cyclodextrin-forming activity, mutant Y195F


proof_lines: strain 1011, acceptor glucose, mutant Y195L and F183L/F259L


proof_lines: strain 1011, acceptor maltose, mutant Y195L

proof_lines: strain 1011, beta-cyclodextrin-forming activity, mutant Y195L


organism: Lysinibacillus sphaericus


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.7; 298.15 K; buffer 100 mM N-(2-hydroxyethyl)piperazine-N-(2-propanesulfonic acid; cofactor CoA

proof_lines: pH 7.7, 25°C, recombinant enzyme, with pimeloyl-CoA

proof_lines: calculated from the competitive and uncompetitive constants and the substrate concentration determined in inhibitor experiments, 37°C, pH 8.6


organism: Symbiobacterium thermophilum


organism: Bos taurus

proof_lines:
enzyme form B
enzyme form DB
below


organism: Homo sapiens

substrate_name: histone H3-peptide p27

proof_lines:
PCAF catalytic domain
PCAF
PCAF protein

substrate: histone H3-peptide p27


substrate_name: histone H3-peptide p20

proof_lines: PCAF catalytic domain, recombinant mutant Y638A

proof_lines: recombinant PCAF catalytic domain mutant Y638A

substrate: histone H3-peptide p20


proof_lines: pH 7.5, 25°C, wild-type P/CAF enzyme, and mutants L503P, D601G, D639E, Y612C/P655R, and L503P/D601G/Y612C

proof_lines: PCAF catalytic domain, recombinant wild-type

proof_lines: pH 7.5, 25°C, wild-type P/CAF enzyme and mutant V582A


substrate_name: histone H4

substrate: histone H4


proof_lines: pH 7.5, 25°C, mutant L503P, with substrate histone H3


proof_lines: pH 7.5, 25°C, mutant V582A, with substrate histone H3


proof_lines: mutant E374K/E378K, presence of chaperone Vps75, pH 7.5, 25°C


proof_lines: mutant E374A/E378A/D301K, presence of chaperone Vps75, pH 7.5, 25°C


proof_lines: wild-type, presence of 0.4 equivalents of chaperone Vps75, pH 7.5, 25°C

proof_lines: wild-type, presence of 8 equivalents of chaperone Vps75, pH 7.5, 25°C

proof_lines: wild-type, presence of 1 equivalent of chaperone Vps75, pH 7.5, 25°C


organism: Sus scrofa

proof_lines:
enzyme form type I
enzyme form type II


organism: Tetrahymena thermophila


proof_lines: recombinant o-fluorophenylalanine-substituted wild-type tGCN5

proof_lines: recombinant m-fluorophenylalanine-substituted wild-type tGCN5


proof_lines: pH 7.5, 25°C, mutants D601G and V582A/D639E, with substrate histone H3


proof_lines: pH 7.5, 25°C, mutant Y612C/P655R, with substrate histone H3


proof_lines: pH 7.5, 25°C, mutants D639E and L503P/D601G/Y612C, with substrate histone H3


proof_lines: pH 7.5, 25°C, mutant Y612C, with substrate histone H3


substrate_name: starch

proof_lines: strain 1011, beta-cyclodextrin-forming activity, mutant F183L

proof_lines: strain 1011, acceptor maltose, mutant F183L

substrate: starch


substrate_name: alpha-cyclodextrin

proof_lines: strain 1011, beta-cyclodextrin-forming activity, mutant F259L

substrate: alpha-cyclodextrin


proof_lines: strain 1011, acceptor maltose, mutant F183L/F259L

proof_lines: strain 1011, beta-cyclodextrin-forming activity, mutant F183L/F259L

proof_lines: strain 1011, acceptor maltose, disproportionation, F183L/F259L


proof_lines: strain 1011, beta-cyclodextrin-forming activity, mutant F283L

proof_lines: strain 1011, acceptor maltose, mutant F283L


proof_lines: mutant strain F183L/F259L, acceptor glucose, wild-type

proof_lines: mutant strain Y195F, acceptor glucose, wild-type


organism: Rhodococcus erythropolis

substrate_name: Gly-para-nitroanilide

substrate: Gly-para-nitroanilide


organism: Burkholderia sp. LP5_18B

substrate_name: laurate

substrate: laurate


substrate_name: N-acetyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03154 canonical sequence with selected-row mutation L372G applied at offset 0 and applied mutation signature L372G to reconstruct the assayed variant sequence.

proof_lines: kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372G-mutant

substrate: N-acetyl-L-methionine


substrate_name: N-hexanoyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03154 canonical sequence with selected-row mutation I177L applied at offset 0 and applied mutation signature I177L to reconstruct the assayed variant sequence.

proof_lines: kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177L-mutant

substrate: N-hexanoyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03154 canonical sequence with selected-row mutation I177A applied at offset 0 and applied mutation signature I177A to reconstruct the assayed variant sequence.

proof_lines: kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-I177A-mutant


substrate_name: N-isopentanoyl-L-methionine

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03154 canonical sequence with selected-row mutation L372I applied at offset 0 and applied mutation signature L372I to reconstruct the assayed variant sequence.

proof_lines: kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372I-mutant

substrate: N-isopentanoyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03154 canonical sequence with selected-row mutation T347F applied at offset 0 and applied mutation signature T347F to reconstruct the assayed variant sequence.

proof_lines: kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347F-mutant


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03154 canonical sequence with selected-row mutation T347G applied at offset 0 and applied mutation signature T347G to reconstruct the assayed variant sequence.

proof_lines: kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347G-mutant


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q03154 canonical sequence with selected-row mutation L372A applied at offset 0 and applied mutation signature L372A to reconstruct the assayed variant sequence.

proof_lines: kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372A-mutant


organism: Rattus norvegicus

substrate_name: N-formyl-L-methionine (f-Met) (at pH 7)

assay_conditions_summary: pH 7

proof_lines: kcat is 7.9 sec(-1) with N-formyl-L-methionine (f-Met) as substrate (at pH 7). kcat is 2.3 sec(-1) with N-acetyl-L-methionine (Ac-Met) as substrate (at pH 7).

substrate: N-formyl-L-methionine (f-Met) (at pH 7)


substrate_name: N-Acetyl-L-methionine; H2O

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

proof_lines: SABIO-RK modifier species: aminoacylase(Enzyme) mutant H79A

substrate: N-Acetyl-L-methionine; H2O


proof_lines: SABIO-RK modifier species: aminoacylase(Enzyme) mutant N261A


substrate_name: H2O; N-Acetyl-L-methionine

proof_lines: SABIO-RK modifier species: aminoacylase(Enzyme) mutant D112A

substrate: H2O; N-Acetyl-L-methionine


proof_lines: SABIO-RK modifier species: aminoacylase(Enzyme) mutant E146A


proof_lines: SABIO-RK modifier species: aminoacylase(Enzyme) mutant E147A


proof_lines: SABIO-RK modifier species: aminoacylase(Enzyme) mutant E174A


proof_lines: SABIO-RK modifier species: aminoacylase(Enzyme) mutant R274A


substrate_name: N-alpha-acetyl-L-methionine

sequence_source: Direct UniProtKB FASTA lookup for reviewed accession P37111 / ACY1_PIG

substrate: N-alpha-acetyl-L-methionine


substrate_name: N-acetyl-L-glutamate

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup Q03154; row-specific T347S reconstruction from the Q03154 canonical sequence and applied mutation signature T347S to reconstruct the assayed variant sequence.

proof_lines: kcat for the hydrolysis of N-acyl-L-glutamate substrates by hAcy1-T347S-mutant

proof_lines: kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1-T347S-mutant

proof_lines: kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-T347S-mutant

substrate: N-acetyl-L-glutamate


substrate_name: N-benzoyl-L-methionine

sequence_source: UniProtKB direct accession lookup Q03154

proof_lines: hydrolysis of N-acetyl-L-methionine substrates by wild-type human Acy1

proof_lines: hydrolysis of N-acetyl-L-glutamate substrates by wild-type human Acy1

substrate: N-benzoyl-L-methionine


sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup Q03154; row-specific L372V reconstruction from the Q03154 canonical sequence and applied mutation signature L372V to reconstruct the assayed variant sequence.

proof_lines: kcat for the hydrolysis of NAM and selected N-acyl-L-methionine substrates by hAcy1-L372V-mutant


substrate_name: N-Chloroacetyl-L-norleucine; H2O

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

proof_lines: kcat for the hydrolysis of N-acyl-L-methionine substrates by hAcy1

proof_lines: kcat the hydrolysis of N-acyl-L-methionine substrates by hAcy1

source_databases_merged: sabio_rk brenda skid

substrate: N-Chloroacetyl-L-norleucine; H2O


organism: Lactococcus lactis subsp. cremoris

substrate_name: H2O; N-Acetyl-L-alanine

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

substrate: H2O; N-Acetyl-L-alanine


organism: Mus musculus

sequence_source: UniProtKB direct accession lookup Q99JW2


organism: Paraburkholderia monticola

substrate_name: N-lauroyl-L-Ala

substrate: N-lauroyl-L-Ala


organism: Pyrococcus horikoshii

substrate_name: Unknown

substrate: Unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB:P37111 direct FASTA/JSON lookup and applied mutation signature H371A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: aminoacylase(Enzyme) mutant H371A


substrate_name: N-acetyl-L-Cys

source_db: oed

verification_status: unverified

sequence_source: UniProtKB:P37111 direct FASTA/JSON lookup

data_origin: experimental

substrate: N-acetyl-L-Cys

status: unverified

source: oed


kcat_over_km_origin: calculated


substrate_name: N-acetyl-L-Met

substrate: N-acetyl-L-Met


substrate_name: N-acetyl-L-Val

substrate: N-acetyl-L-Val


proof_lines: analysis by TNBS (2,4,6-trinitrobenzenesulphonic acid) assay, pH 7.6, 37°C


substrate_name: N-acetyl-L-phenylalanine

sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession O58754 with E367Q substitution reconstructed during review and applied mutation signature E367Q to reconstruct the assayed variant sequence.

substrate: N-acetyl-L-phenylalanine


sequence_source: UniProtKB REST accession O58754 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB REST accession O58754 with C102S substitution reconstructed during review and applied mutation signature C102S to reconstruct the assayed variant sequence.


substrate_name: N-acetyl-L-methionine

sequence_source: UniProtKB REST accession O58453 canonical sequence

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

substrate: N-acetyl-L-methionine


organism: Stenotrophomonas geniculata

substrate_name: N-acetyl-L-phosphinothricin

sequence_source: UniProtKB REST accession A0A0L8A662 canonical sequence

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

substrate: N-acetyl-L-phosphinothricin


organism: Streptomyces mobaraensis

sequence_source: UniProtKB REST accession C9K2Z6 canonical sequence

proof_lines: recombinant enzyme, at 37°C, pH not specified in the publication


sequence_source: UniProtKB REST accession P37111 canonical sequence; variant sequence not reconstructed

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

proof_lines: SABIO-RK modifier species: aminoacylase(Enzyme) mutant E309H


proof_lines: SABIO-RK modifier species: aminoacylase(Enzyme) mutant H205L


enzyme_display_name: aminobutyraldehyde dehydrogenase

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

proof_lines:
E2 isozyme
E3 isozyme
E1 isozyme

enzyme: aminobutyraldehyde dehydrogenase


organism: Zea mays

sequence_source: UniProtKB reviewed accession G5DDC2 / ADH1B_MAIZE


substrate_name: Betaine aldehyde

substrate: Betaine aldehyde


organism: Arabidopsis thaliana


organism: Escherichia coli (strain K12)


substrate_name: NAD

substrate: NAD


substrate_name: NAD (at pH 8.0)

assay_conditions_summary: pH 8

substrate: NAD (at pH 8.0)


organism: Malus domestica


organism: Solanum lycopersicum

verification_status: corrected

sequence_source: UniProtKB reviewed accession B6ECN9, AADH2_SOLLC, direct REST lookup; UniProt cites PMID:23408433 for sequence/function/catalytic activity.

assay_conditions_summary: pH 9; 310.15 K; buffer 0.15 M Tris-HCl; cofactor NAD+

column_label: Table 3; row TMABAL; SlAMADH2; kcat column 7, km column 6

raw_value_unit_evidence: Table 3; SlAMADH2 / TMABAL; captured cells: kcat 2.0 +/- 0.1 s^-1; km 141 +/- 17 uM

row_label: SlAMADH2 / TMABAL

table_label: Table 3

status: corrected


substrate_name: 4-pyridine carboxaldehyde

verification_status: verified

assay_conditions_summary: pH 9; 310.15 K; cofactor NAD+

column_label: Table 3. Kinetic parameters of ALDH10 family from tomato for selected substrates and NAD+; SlAMADH1 row 4-PCAL; literal cells Km 50 uM, kcat 1.4 s^-1, kcat/Km 2.8 × 10^4 M^-1 s^-1. No SlAMADH2 cell supplies the accepted top tuple.

normalized_value_unit_evidence: Printed kcat 1.4 s^-1 is stored as 1.4; printed Km 50 uM / 1000 is stored as 0.05 mM; current stored quotient is 27.999999999999996 s^-1*mM^-1 and the printed SlAMADH1 ratio is 2.8 × 10^4 M^-1 s^-1.

raw_value_unit_evidence: Table 3, SlAMADH1, 4-PCAL: Km 50 uM; kcat 1.4 s^-1; kcat/Km 2.8 × 10^4 M^-1 s^-1. Every value comes from the SlAMADH1 column group.

row_label: SlAMADH1 | 4-PCAL

substrate: 4-pyridine carboxaldehyde

status: verified


smiles: C[N+](C)(C)CCCC=O


sequence_source: UniProtKB reviewed accession C6KEM4, AADH2_MAIZE, direct REST lookup; UniProt cites PMID:23408433 for sequence/function/catalytic activity.

column_label: Table 4; row GBAL; ZmAMADH2; kcat column 12, km column 11

raw_value_unit_evidence: Table 4; ZmAMADH2 / GBAL; captured cells: kcat 5.0 +/- 0.4 s^-1; km 11 +/- 1.2 uM

row_label: ZmAMADH2 / GBAL

table_label: Table 4


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

sequence_source: UniProtKB reviewed accession C0P9J6, ADH1A_MAIZE, direct REST lookup; UniProt cites PMID:23408433 and cross-references PDB 4I8P.

column_label: Table 4; row GBAL; ZmAMADH1a; kcat column 2, km column 1

raw_value_unit_evidence: Table 4; ZmAMADH1a / GBAL; captured cells: kcat 1.6 +/- 0.2 s^-1; km 3 +/- 0.7 uM

row_label: ZmAMADH1a / GBAL

source_databases_merged: brenda skid


smiles: NCCCC=O


smiles: NCCC=O


smiles: N=C(N)NCCCC=O


organism: Lathyrus oleraceus

sequence_source: UniProtKB REST direct accession lookup: Q93YB2

assay_conditions_summary: pH 9; 303.15 K; buffer 0.15 M Tris-HCl

proof_lines: isozyme AMADH2, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C


sequence_source: UniProtKB REST direct accession lookup: Q8VWZ1

proof_lines: isozyme AMADH1, in 0.15 M Tris-HCl buffer (pH 9.0), at 20°C


organism: Lycium ruthenicum

sequence_source: UniProtKB REST direct accession lookup: A0A1P8VFW6

proof_lines: pH 8.0, 30°C, recombinant isozyme LrAMADH1


sequence_source: UniProtKB REST direct accession lookup: A0A1P8VFW8


sequence_source: UniProtKB REST direct accession lookup: A0A0E3T552

assay_conditions_summary: pH 9.8; cofactor NAD+

proof_lines: pH 9.8, temperature not specified in the publication, isozyme MdAMADH1


sequence_source: UniProtKB REST direct accession lookup: A0A0E3T3B5

proof_lines: pH 9.8, temperature not specified in the publication, isozyme MdAMADH2


organism: Pisum sativum

source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB reviewed entry Q8VWZ1

proof_lines:
Raw SKiD Env: Temp=30°C, pH=9
Raw SKiD Env: Temp=20°C, pH=9

source: skid


substrate_name: H2O; NAD+; 4-Aminobutanal

sequence_source: UniProtKB reviewed entry Q9JLJ3

assay_conditions_summary: cofactor NAD+

substrate: H2O; NAD+; 4-Aminobutanal


sequence_source: UniProtKB reviewed entry B6ECN9


column_label: Table 3. Kinetic parameters of ALDH10 family from tomato for selected substrates and NAD+; SlAMADH1 row BAL; literal cells Km 2051 uM, kcat 1.0 s^-1, kcat/Km 4.6 × 10^2 M^-1 s^-1. No SlAMADH2 cell supplies the accepted top tuple.

normalized_value_unit_evidence: Printed kcat 1.0 s^-1 is stored as 1; printed Km 2051 uM / 1000 is stored as 2.051 mM; current stored quotient is 0.4875670404680643 s^-1*mM^-1 and the printed SlAMADH1 ratio is 4.6 × 10^2 M^-1 s^-1.

raw_value_unit_evidence: Table 3, SlAMADH1, BAL: Km 2051 uM; kcat 1.0 s^-1; kcat/Km 4.6 × 10^2 M^-1 s^-1. Every value comes from the SlAMADH1 column group.

row_label: SlAMADH1 | BAL


substrate_name: 3-pyridine carboxaldehyde

column_label: Table 3. Kinetic parameters of ALDH10 family from tomato for selected substrates and NAD+; SlAMADH1 row 3-PCAL; literal cells Km 316 uM, kcat 2.2 s^-1, kcat/Km 6.9 × 10^3 M^-1 s^-1. No SlAMADH2 cell supplies the accepted top tuple.

normalized_value_unit_evidence: Printed kcat 2.2 s^-1 is stored as 2.2; printed Km 316 uM / 1000 is stored as 0.316 mM; current stored quotient is 6.962025316455697 s^-1*mM^-1 and the printed SlAMADH1 ratio is 6.9 × 10^3 M^-1 s^-1.

raw_value_unit_evidence: Table 3, SlAMADH1, 3-PCAL: Km 316 uM; kcat 2.2 s^-1; kcat/Km 6.9 × 10^3 M^-1 s^-1. Every value comes from the SlAMADH1 column group.

row_label: SlAMADH1 | 3-PCAL

substrate: 3-pyridine carboxaldehyde


assay_conditions_summary: pH 8.5; 295.15 K; cofactor NAD+

proof_lines: with 4-aminobutanal, pH 8.5, 22°C, recombinant enzyme

proof_lines: with 3-aminopropanal, pH 8.5, 22°C, recombinant enzyme


assay_conditions_summary: pH 9.5; 295.15 K; cofactor NAD+

proof_lines: with 3-aminopropanal, pH 9.5, 22°C, recombinant enzyme

proof_lines: with 4-aminobutanal, pH 9.5, 22°C, recombinant enzyme


organism: Escherichia coli

substrate_name: NAD+; H2O; 4-Aminobutanal

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADP+

proof_lines:
0.1 M Tris-HCl pH 7.5, 1 mM NAD+, 25°C
Raw SKiD Env: Temp=25°C, pH=7.5

substrate: NAD+; H2O; 4-Aminobutanal


substrate_name: NAD+

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADP+

substrate: NADP+


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


substrate_name: NAD+; 1-Pyrroline; H2O

proof_lines: SABIO-RK modifier species: aminobutyraldehyde dehydrogenase(Enzyme) mutant putrescine+

substrate: NAD+; 1-Pyrroline; H2O


organism: Homo sapiens

substrate_name: H2O; 4-Aminobutanal; NAD+

substrate: H2O; 4-Aminobutanal; NAD+


organism: Rattus norvegicus


organism: Arthrobacter sp.


organism: Avena sativa

assay_conditions_summary: pH 8.7; 310.15 K; cofactor NAD+


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


organism: Glycine max


organism: Pseudomonas putida

assay_conditions_summary: pH 8; cofactor NAD+


organism: Spinacia oleracea

substrate_name: betaine aldehyde

substrate: betaine aldehyde


organism: Paenibacillus barengoltzii

substrate_name: soluble potato starch

proof_lines: mutant enzyme A144V, beta-cyclizing activity, at pH 6.4 and 55°C

substrate: soluble potato starch


proof_lines: native wild type enzyme, beta-cyclizing activity, at pH 6.4 and 55°C

proof_lines: recombinant wild type enzyme, beta-cyclizing activity, at pH 6.4 and 55°C


proof_lines: mutant enzyme M329I, beta-cyclizing activity, at pH 6.4 and 55°C


organism: Paenibacillus campinasensis

substrate_name: maltodextrin

substrate: maltodextrin


organism: Paenibacillus macerans

substrate_name: starch

proof_lines:
authentic CGTase
cyclodextrin opening
at pH 5.5 and 37°C

substrate: starch


proof_lines: same value with benzaldehyde, constant substrate 1 mM NAD+

proof_lines: 250 mM phosphate preparation, constant substrate 1 mM NAD+


organism: Cytobacillus firmus


organism: Geobacillus stearothermophilus

substrate_name: alpha-cyclodextrin

substrate: alpha-cyclodextrin


organism: Heyndrickxia coagulans

proof_lines:
coupling
cyclodextrin opening


organism: Lysinibacillus sphaericus


proof_lines:
wild-type
wild type enzyme, at pH 5.5 and 37°C


proof_lines: mutant enzyme Q265K/Y195S, at pH 5.5 and 37°C


substrate_name: L-ascorbic acid

substrate: L-ascorbic acid


proof_lines: mutant enzyme Y260R/Q265K, at pH 5.5 and 37°C


organism: Bos taurus

substrate_name: all-trans retinal

proof_lines: Has a much higher catalytic efficiency toward all-trans retinal.

substrate: all-trans retinal


organism: Macaca fascicularis

substrate_name: all-trans retinal (at pH 7.5 and 25 degrees Celsius)

proof_lines: Has a nearly 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans and 13-cis retinal.


organism: Oryctolagus cuniculus


substrate_name: 9-cis retinal (at pH 7.5 and 25 degrees Celsius)

proof_lines: Has more than 2-fold higher catalytic efficiency for 9-cis retinal compared to all-trans retinal and 11-cis retinal.


enzyme_display_name: 3-deoxy-8-phosphooctulonate synthase

organism: Neisseria meningitidis

substrate_name: phosphoenolpyruvate

sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9JZ55; variant reconstructed from PMID 19447118 mutation labels and applied mutation signature D247E to reconstruct the assayed variant sequence.

enzyme: 3-deoxy-8-phosphooctulonate synthase

substrate: phosphoenolpyruvate


proof_lines: N23C/C247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O

proof_lines: N23C/C247E/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9JZ55; variant reconstructed from PMID 19447118 mutation labels and applied mutation signature D247E/P249A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9JZ55; variant reconstructed from PMID 19447118 mutation labels and applied mutation signature N23C/C246S/D247E to reconstruct the assayed variant sequence.

proof_lines: N23C/C246S/D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O


proof_lines: wild type, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA


sequence_source: uniprot_accession:Q9JZ55; variant reconstructed from PMID 19447118 mutation labels

proof_lines: D247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA


sequence_variant_note: Resolved canonical sequence from uniprot_accession:Q9JZ55; variant reconstructed from PMID 19447118 mutation labels and applied mutation signature N23C/C246S/D247E/P249A to reconstruct the assayed variant sequence.


organism: Aquifex pyrophilus

substrate_name: Phosphoenolpyruvate; H2O; D-Arabinose 5-phosphate

sequence_source: UniProtKB:Q8GLK7 direct accession lookup


organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q9AV97 direct accession lookup

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


organism: Escherichia coli

substrate_name: D-Ribose 5-phosphate

sequence_source: UniProtKB:P0A715 direct accession lookup

substrate: D-Ribose 5-phosphate


substrate_name: D-Arabinose 5-phosphate; H2O; Phosphoenolpyruvate

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

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=7.3


substrate_name: 2-Deoxy-D-ribose 5-phosphate

substrate: 2-Deoxy-D-ribose 5-phosphate


substrate_name: D-Erythrose 4-phosphate

substrate: D-Erythrose 4-phosphate


substrate_name: H2O; Phosphoenolpyruvate; D-Arabinose 5-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A715 direct accession lookup with N26C reconstruction and applied mutation signature N26C to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-deoxy-8-phosphooctulonate synthase(Enzyme) mutant KdsA N26C

proof_lines: pH 7.5, 37°C, mutant enzyme N26C, EDTA-treated


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence with D247E/P249A reconstructed during review and applied mutation signature D247E/P249A to reconstruct the assayed variant sequence.

proof_lines: D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA


sequence_source: UniProtKB Q9JZ55 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence with P249A reconstructed during review and applied mutation signature P249A to reconstruct the assayed variant sequence.

proof_lines: P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence with N23C/C246S reconstructed during review and applied mutation signature N23C/C246S to reconstruct the assayed variant sequence.

proof_lines: N23C/C246S mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA

proof_lines: N23C/C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence with N23C reconstructed during review and applied mutation signature N23C to reconstruct the assayed variant sequence.

proof_lines: N23C mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O

proof_lines: N23C mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence with N23C/C246S/D247E/P249A reconstructed during review and applied mutation signature N23C/C246S/D247E/P249A to reconstruct the assayed variant sequence.

proof_lines: N23C/C246S/D247E/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O


sequence_source: UniProtKB Q9JZ55 canonical sequence with N23C reconstructed during review


organism: Aquifex aeolicus

sequence_source: UniProtKB O66496 direct accession lookup


substrate_name: D-arabinose 5-phosphate

substrate: D-arabinose 5-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB O66496 direct accession lookup plus single substitution reconstruction and applied mutation signature R106G to reconstruct the assayed variant sequence.


proof_lines: enzyme preparation 1, substitution with 50 microM Cd2+, 100 mM Tris-acetate, pH 7.5, 40°C

proof_lines: enzyme preparation 1, substitution with 5 microM Cu2+, 100 mM Tris-acetate, pH 7.5, 40°C

proof_lines: enzyme preparation 1, substitution with 50 microM Zn2+, 100 mM Tris-acetate, pH 7.5, 40°C


substrate_name: H2O; D-Arabinose 5-phosphate; Phosphoenolpyruvate

sequence_variant_note: Resolved canonical sequence from UniProtKB Q8GLK7 direct accession lookup plus single substitution reconstruction and applied mutation signature C11N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: 3-deoxy-8-phosphooctulonate synthase(Enzyme) mutant KdsA C11N

proof_lines: pH 7.5, 60°C, mutant enzyme C11N, EDTA-treated


sequence_source: UniProtKB Q8GLK7 direct accession lookup

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


sequence_source: UniProtKB Q8GLK7 direct accession lookup plus single substitution reconstruction


substrate_name: Phosphoenolpyruvate

substrate: Phosphoenolpyruvate


substrate_name: D-Arabinose 5-phosphate

substrate: D-Arabinose 5-phosphate


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:P0A715 by applying N26C and applied mutation signature N26C to reconstruct the assayed variant sequence.


sequence_source: Reconstructed from UniProtKB:P0A715 by applying N26C


organism: Helicobacter pylori

sequence_source: UniProtKB:Q9ZN55 direct accession lookup

substrate: D-Arabinose 5-phosphate; H2O; Phosphoenolpyruvate


substrate_name: Phosphoenolpyruvate; D-Arabinose 5-phosphate; H2O

sequence_source: UniProtKB:P56060 direct accession lookup


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence fetched from UniProt REST during review; N23C and C246S substitutions applied by direct residue check. and applied mutation signature N23C/C246S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 canonical sequence fetched from UniProt REST during review; N23C, C246S, and D247E substitutions applied by direct residue check. and applied mutation signature N23C/C246S/D247E to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9JZ55 canonical sequence fetched from UniProt REST during review; row-specific N23C/C247E was not reconstructed.

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

proof_lines: N23C/C247E mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA

proof_lines: N23C/C247E mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O


organism: Unknown

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


substrate_name: L-xylose 5-phosphate

sequence_source: UniProtKB Q9JZ55 direct REST/FASTA lookup

proof_lines: in the presence of L-xylose 5-phosphate, at 30°C

proof_lines: Km less than 0.001 mM, in the presence of D-arabinose 5-phosphate, at 30°C

substrate: L-xylose 5-phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature and applied mutation signature C246S to reconstruct the assayed variant sequence.


sequence_source: UniProtKB Q9JZ55 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature

proof_lines: C246S mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature and applied mutation signature P249A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature and applied mutation signature N23C/P249A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9JZ55 direct REST/FASTA lookup; variant reconstructed from selected mutation_signature and applied mutation signature N23C/C246S/P249A to reconstruct the assayed variant sequence.

proof_lines: N23C/C246S/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O


proof_lines: N23C/P249A mutant control, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 20 microM EDTA

proof_lines: N23C/P249A mutant, 37°C, 50 mM 1,3-bis[tris(hydroxymethyl)-methylamino]propane (BTP) buffer, pH 7.4, 90 microM MnSO4.H2O


organism: Thermococcus sp.

substrate_name: starch

sequence_source: UniProtKB Q9UWN2 direct check; entry references PMID 10548490 and Thermococcus sp. B1001 cgtA.

proof_lines:
unheated CGTase
heated CGTase


substrate_name: biotinylated citronellyl-lipid I

proof_lines:
in the absence of additional metal ions
in the presence of Mg2+
in the presence of Mn2+

substrate: biotinylated citronellyl-lipid I


substrate_name: tRNA

sequence_source: UniProtKB P0A847 direct check; EC 2.4.2.29 and catalytic/biophysical evidence cite PMID 11714265.

proof_lines: histidine-tagged wild-type enzyme, pH 8.5

proof_lines: histidine-tagged wild-type enzyme, pH 7.3

substrate: tRNA


substrate_name: guanine

sequence_variant_note: Resolved canonical sequence from UniProtKB P0A847 canonical sequence plus UniProt mutagenesis feature for D89E citing PMID 11714265; residue 89 was D in the fetched sequence and was substituted to E. and applied mutation signature D89E to reconstruct the assayed variant sequence.

proof_lines: histidine-tagged mutant enzyme D89E, pH 7.3

proof_lines: histidine-tagged mutant enzyme D89E, pH 8.5

substrate: guanine


substrate_name: [RNAECYMA]-guanine

proof_lines:
inactivation
,competitive inhibition

substrate: [RNAECYMA]-guanine


substrate_name: tRNA(Tyr)

sequence_variant_note: Resolved canonical sequence from UniProtKB P0A847 canonical sequence plus UniProt mutagenesis feature for S90C citing PMID 8003468; residue 90 was S in the fetched sequence and was substituted to C. and applied mutation signature S90C to reconstruct the assayed variant sequence.

substrate: tRNA(Tyr)


substrate_name: L-ascorbic acid

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

proof_lines: mutant enzyme Y260R/Y195S, at pH 5.5 and 37°C


substrate_name: maltodextrin

proof_lines: mutant enzyme Y260R/Q265K/Y195S, at pH 5.5 and 37°C

substrate: maltodextrin


substrate_name: maltose

substrate: maltose


organism: Zymomonas mobilis

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: uracil phosphoribosyltransferase

organism: Acholeplasma laidlawii

substrate_name: Uracil

enzyme: uracil phosphoribosyltransferase

substrate: Uracil


organism: Bacillus subtilis

proof_lines:
forward reaction
reverse reaction


organism: Candida albicans

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

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


organism: Giardia duodenalis

proof_lines: competitive versus 5-phosphoribose 1-diphosphate


organism: Lactobacillus bifidus


organism: Lactobacillus gasseri


organism: Lactobacillus leichmannii


organism: Niallia circulans

proof_lines: pH 6.4, 55°C, formation of beta-cyclodextrin


substrate_name: soluble potato starch

sequence_source: UniProtKB C4MH58; PMID:21993482; EMBL ACF42340.2

proof_lines: wild-type, pH 6.4, 56°C, calculated as production of beta-cyclodextrin

substrate: soluble potato starch


sequence_source: Reconstructed from UniProtKB C4MH58 canonical sequence using PMID:21993482 mutation Q179G; paper mature residue 179 maps to full precursor residue 213.

sequence_variant_note: Mutation signature Q179G matches the mutant residue at offset +10 and the reference residue at offset +3; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: mutant Q179G, pH 6.4, 56°C, calculated as production of beta-cyclodextrin


sequence_source: Reconstructed from UniProtKB C4MH58 canonical sequence using PMID:21993482 mutation Q179L; paper mature residue 179 maps to full precursor residue 213.

sequence_variant_note: Mutation signature Q179L matches the mutant residue at offset +12 and the reference residue at offset +3; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: mutant Q179L, pH 6.4, 56°C, calculated as production of beta-cyclodextrin


organism: Paenibacillus barengoltzii

proof_lines: mutant enzyme A137V, beta-cyclizing activity, at pH 6.4 and 55°C


proof_lines: mutant enzyme L280A, beta-cyclizing activity, at pH 6.4 and 55°C


enzyme_display_name: orotate phosphoribosyltransferase

organism: Salmonella typhimurium

substrate_name: diphosphate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K103Q to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K103Q; column kcat (s^-1) = 0.05 ± 0.004; column KM (uM) under PPi = 144; column kcat/KM (mM^-1 s^-1) under PPi = 0.3.

normalized_value_unit_evidence: kcat: printed cell 0.05 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.05 s^-1. Km: printed cell 144 uM; 144 / 1000 = 0.144 mM. kcat/Km: printed cell 0.3 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 0.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K103Q, PPi column group: kcat = 0.05 ± 0.004 s^-1; Km = 144 uM; printed kcat/Km = 0.3 mM^-1 s^-1.

enzyme: orotate phosphoribosyltransferase

substrate: diphosphate


substrate_name: Orotate

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K100A to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K100A; column kcat (s^-1) = 12 ± 0.2; column KM (uM) under orotate = 72; column kcat/KM (mM^-1 s^-1) under orotate = 160.

normalized_value_unit_evidence: kcat: printed cell 12 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 12.0 s^-1. Km: printed cell 72 uM; 72 / 1000 = 0.072 mM. kcat/Km: printed cell 160 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 160.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K100A, orotate column group: kcat = 12 ± 0.2 s^-1; Km = 72 uM; printed kcat/Km = 160 mM^-1 s^-1.

substrate: Orotate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K103A to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K103A; column kcat (s^-1) = 0.05 ± 0.002; column KM (uM) under orotate = 42; column kcat/KM (mM^-1 s^-1) under orotate = 1.

normalized_value_unit_evidence: kcat: printed cell 0.05 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.05 s^-1. Km: printed cell 42 uM; 42 / 1000 = 0.042 mM. kcat/Km: printed cell 1 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 1.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K103A, orotate column group: kcat = 0.05 ± 0.002 s^-1; Km = 42 uM; printed kcat/Km = 1 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K26A to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K26A; column kcat (s^-1) = 8.7±0.2; column KM (uM) under orotate = 70; column kcat/KM (mM^-1 s^-1) under orotate = 125.

normalized_value_unit_evidence: kcat: printed cell 8.7 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 8.7 s^-1. Km: printed cell 70 uM; 70 / 1000 = 0.07 mM. kcat/Km: printed cell 125 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 125.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K26A, orotate column group: kcat = 8.7±0.2 s^-1; Km = 70 uM; printed kcat/Km = 125 mM^-1 s^-1.


substrate_name: Imidodiphosphate

sequence_source: UniProt REST/FASTA direct accession check: P08870

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

column_label: Table 5: Pyrophosphate Analogs as Substrates or Inhibitors of Wild-Type OPRTase (Biochemistry 1995, 34(34):10755-10763); enzyme row WT; column kcat (s^-1) = 35; column Km (uM) under imidodiphosphate = 940; column kcat/KM (mM^-1 s^-1) under imidodiphosphate = 38.

normalized_value_unit_evidence: kcat: printed cell 35 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 35.0 s^-1. Km: printed cell 940 uM; 940 / 1000 = 0.94 mM. kcat/Km: printed cell 38 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 38.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 5, Pyrophosphate Analogs as Substrates or Inhibitors of Wild-Type OPRTase, enzyme row WT, imidodiphosphate column group: kcat = 35 s^-1; Km = 940 uM; printed kcat/Km = 38 mM^-1 s^-1.

substrate: Imidodiphosphate


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row WT; column kcat (s^-1) = 18 ± 0.3; column KM (uM) under PPi = 33; column kcat/KM (mM^-1 s^-1) under PPi = 550.

normalized_value_unit_evidence: kcat: printed cell 18 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 18.0 s^-1. Km: printed cell 33 uM; 33 / 1000 = 0.033 mM. kcat/Km: printed cell 550 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 550.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row WT, PPi column group: kcat = 18 ± 0.3 s^-1; Km = 33 uM; printed kcat/Km = 550 mM^-1 s^-1.


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

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K26Q to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K26Q; column kcat (s^-1) = 3.1 ± 0.03; column KM (uM) under PRPP = 55; column kcat/KM (mM^-1 s^-1) under PRPP = 56.

normalized_value_unit_evidence: kcat: printed cell 3.1 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 3.1 s^-1. Km: printed cell 55 uM; 55 / 1000 = 0.055 mM. kcat/Km: printed cell 56 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 56.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K26Q, PRPP column group: kcat = 3.1 ± 0.03 s^-1; Km = 55 uM; printed kcat/Km = 56 mM^-1 s^-1.

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


sequence_variant_note: Resolved canonical sequence from UniProt REST/FASTA direct accession check: P08870 and applied mutation signature K26A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: orotate phosphoribosyltransferase(Enzyme) mutant K26A


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K73Q to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K73Q; column kcat (s^-1) = 0.6 ± 0.02; column KM (uM) under orotate = 31; column kcat/KM (mM^-1 s^-1) under orotate = 19.

normalized_value_unit_evidence: kcat: printed cell 0.6 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.6 s^-1. Km: printed cell 31 uM; 31 / 1000 = 0.031 mM. kcat/Km: printed cell 19 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 19.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K73Q, orotate column group: kcat = 0.6 ± 0.02 s^-1; Km = 31 uM; printed kcat/Km = 19 mM^-1 s^-1.


substrate_name: orotidine 5'-phosphate

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K103Q; column kcat (s^-1) = 0.05 ± 0.004; column KM (uM) under OMP = 3.4; column kcat/KM (mM^-1 s^-1) under OMP = 15.

normalized_value_unit_evidence: kcat: printed cell 0.05 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.05 s^-1. Km: printed cell 3.4 uM; 3.4 / 1000 = 0.0034 mM. kcat/Km: printed cell 15 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 15.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K103Q, OMP column group: kcat = 0.05 ± 0.004 s^-1; Km = 3.4 uM; printed kcat/Km = 15 mM^-1 s^-1.

substrate: orotidine 5'-phosphate


substrate_name: Phosphonoacetate

sequence_variant_note: Resolved canonical sequence from UniProtKB P08870 REST/FASTA direct lookup; reconstructed by applying K26Q to the canonical sequence after direct residue check. and applied mutation signature K26Q to reconstruct the assayed variant sequence.

smiles: O=C(O)CP(=O)(O)O

substrate: Phosphonoacetate


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K73A to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K73A; column kcat (s^-1) = 0.3 ± 0.003; column KM (uM) under orotate = 29; column kcat/KM (mM^-1 s^-1) under orotate = 9.

normalized_value_unit_evidence: kcat: printed cell 0.3 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.3 s^-1. Km: printed cell 29 uM; 29 / 1000 = 0.029 mM. kcat/Km: printed cell 9 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 9.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K73A, orotate column group: kcat = 0.3 ± 0.003 s^-1; Km = 29 uM; printed kcat/Km = 9 mM^-1 s^-1.


sequence_source: UniProtKB P08870 REST/FASTA direct lookup.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row WT; column kcat (s^-1) = 34 ± 0.6; column KM (uM) under orotate = 26; column kcat/KM (mM^-1 s^-1) under orotate = 1300.

normalized_value_unit_evidence: kcat: printed cell 34 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 34.0 s^-1. Km: printed cell 26 uM; 26 / 1000 = 0.026 mM. kcat/Km: printed cell 1300 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 1300.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row WT, orotate column group: kcat = 34 ± 0.6 s^-1; Km = 26 uM; printed kcat/Km = 1300 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB P08870 REST/FASTA direct lookup; reconstructed by applying K73Q to the canonical sequence after direct residue check. and applied mutation signature K73Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: orotate phosphoribosyltransferase(Enzyme) mutant K73Q


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row WT; column kcat (s^-1) = 34 ± 0.6; column KM (uM) under PRPP = 49; column kcat/KM (mM^-1 s^-1) under PRPP = 690.

normalized_value_unit_evidence: kcat: printed cell 34 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 34.0 s^-1. Km: printed cell 49 uM; 49 / 1000 = 0.049 mM. kcat/Km: printed cell 690 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 690.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row WT, PRPP column group: kcat = 34 ± 0.6 s^-1; Km = 49 uM; printed kcat/Km = 690 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB P08870 REST/FASTA direct lookup; reconstructed by applying K103A to the canonical sequence after direct residue check. and applied mutation signature K103A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: orotate phosphoribosyltransferase(Enzyme) mutant K103A


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K100A; column kcat (s^-1) = 12 ± 0.2; column KM (uM) under PRPP = 179; column kcat/KM (mM^-1 s^-1) under PRPP = 64.

normalized_value_unit_evidence: kcat: printed cell 12 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 12.0 s^-1. Km: printed cell 179 uM; 179 / 1000 = 0.179 mM. kcat/Km: printed cell 64 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 64.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K100A, PRPP column group: kcat = 12 ± 0.2 s^-1; Km = 179 uM; printed kcat/Km = 64 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08870 canonical FASTA plus row-specific K103Q reconstruction and applied mutation signature K103Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08870 canonical FASTA plus row-specific K73A reconstruction and applied mutation signature K73A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: orotate phosphoribosyltransferase(Enzyme) mutant K73A


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K73A; column kcat (s^-1) = 0.3 ± 0.003; column KM (uM) under PRPP = 394; column kcat/KM (mM^-1 s^-1) under PRPP = 0.7.

normalized_value_unit_evidence: kcat: printed cell 0.3 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.3 s^-1. Km: printed cell 394 uM; 394 / 1000 = 0.394 mM. kcat/Km: printed cell 0.7 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 0.7 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K73A, PRPP column group: kcat = 0.3 ± 0.003 s^-1; Km = 394 uM; printed kcat/Km = 0.7 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K73Q; column kcat (s^-1) = 0.3 ± 0.004; column KM (uM) under OMP = 13; column kcat/KM (mM^-1 s^-1) under OMP = 24.

normalized_value_unit_evidence: kcat: printed cell 0.3 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.3 s^-1. Km: printed cell 13 uM; 13 / 1000 = 0.013 mM. kcat/Km: printed cell 24 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 24.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K73Q, OMP column group: kcat = 0.3 ± 0.004 s^-1; Km = 13 uM; printed kcat/Km = 24 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08870 canonical FASTA plus row-specific K100A reconstruction and applied mutation signature K100A to reconstruct the assayed variant sequence.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K26A; column kcat (s^-1) = 9.6 ± 0.1; column KM (uM) under PPi = 74; column kcat/KM (mM^-1 s^-1) under PPi = 130.

normalized_value_unit_evidence: kcat: printed cell 9.6 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 9.6 s^-1. Km: printed cell 74 uM; 74 / 1000 = 0.074 mM. kcat/Km: printed cell 130 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 130.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K26A, PPi column group: kcat = 9.6 ± 0.1 s^-1; Km = 74 uM; printed kcat/Km = 130 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K103A; column kcat (s^-1) = 0.05 ± 0.002; column KM (uM) under PRPP = 285; column kcat/KM (mM^-1 s^-1) under PRPP = 0.2.

normalized_value_unit_evidence: kcat: printed cell 0.05 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.05 s^-1. Km: printed cell 285 uM; 285 / 1000 = 0.285 mM. kcat/Km: printed cell 0.2 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 0.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K103A, PRPP column group: kcat = 0.05 ± 0.002 s^-1; Km = 285 uM; printed kcat/Km = 0.2 mM^-1 s^-1.


organism: Burkholderia cenocepacia

sequence_source: UniProtKB exact accession B4E589


organism: Escherichia coli

sequence_source: UniProtKB exact accession P0A7E3


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB exact accession P9WHK9


proof_lines: mixed type inhibition, 5-phospho-alpha-D-ribose 1-diphosphate varied substrate, orotate unsaturated, pH 8.0, 25°C


organism: Plasmodium falciparum

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

proof_lines: 37 °C, pH 8.0, mixture of recombinant enzyme subunits

proof_lines: 37 °C, pH 8.0, recombinant monofunctional enzyme


sequence_source: UniProtKB exact accession Q8N0R1

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

proof_lines: pH and temperature not specified in the publication, recombinant multienzyme complex, OPRT activity


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K73A; column kcat (s^-1) = 0.3 ± 0.006; column KM (uM) under OMP = 11; column kcat/KM (mM^-1 s^-1) under OMP = 28.

normalized_value_unit_evidence: kcat: printed cell 0.3 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.3 s^-1. Km: printed cell 11 uM; 11 / 1000 = 0.011 mM. kcat/Km: printed cell 28 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 28.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K73A, OMP column group: kcat = 0.3 ± 0.006 s^-1; Km = 11 uM; printed kcat/Km = 28 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K73Q; column kcat (s^-1) = 0.6 ± 0.02; column KM (uM) under PRPP = 576; column kcat/KM (mM^-1 s^-1) under PRPP = 1.

normalized_value_unit_evidence: kcat: printed cell 0.6 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.6 s^-1. Km: printed cell 576 uM; 576 / 1000 = 0.576 mM. kcat/Km: printed cell 1 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 1.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K73Q, PRPP column group: kcat = 0.6 ± 0.02 s^-1; Km = 576 uM; printed kcat/Km = 1 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K73A; column kcat (s^-1) = 0.3 ± 0.006; column KM (uM) under PPi = 182; column kcat/KM (mM^-1 s^-1) under PPi = 2.

normalized_value_unit_evidence: kcat: printed cell 0.3 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.3 s^-1. Km: printed cell 182 uM; 182 / 1000 = 0.182 mM. kcat/Km: printed cell 2 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 2.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K73A, PPi column group: kcat = 0.3 ± 0.006 s^-1; Km = 182 uM; printed kcat/Km = 2 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K73Q; column kcat (s^-1) = 0.3 ± 0.004; column KM (uM) under PPi = 102; column kcat/KM (mM^-1 s^-1) under PPi = 3.

normalized_value_unit_evidence: kcat: printed cell 0.3 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.3 s^-1. Km: printed cell 102 uM; 102 / 1000 = 0.102 mM. kcat/Km: printed cell 3 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 3.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K73Q, PPi column group: kcat = 0.3 ± 0.004 s^-1; Km = 102 uM; printed kcat/Km = 3 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K103Q; column kcat (s^-1) = 0.13 ± 0.001; column KM (uM) under PRPP = 120; column kcat/KM (mM^-1 s^-1) under PRPP = 1.

normalized_value_unit_evidence: kcat: printed cell 0.13 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.13 s^-1. Km: printed cell 120 uM; 120 / 1000 = 0.12 mM. kcat/Km: printed cell 1 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 1.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K103Q, PRPP column group: kcat = 0.13 ± 0.001 s^-1; Km = 120 uM; printed kcat/Km = 1 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K26Q; column kcat (s^-1) = 1.3 ± 0.01; column KM (uM) under OMP = 37; column kcat/KM (mM^-1 s^-1) under OMP = 34.

normalized_value_unit_evidence: kcat: printed cell 1.3 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 1.3 s^-1. Km: printed cell 37 uM; 37 / 1000 = 0.037 mM. kcat/Km: printed cell 34 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 34.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K26Q, OMP column group: kcat = 1.3 ± 0.01 s^-1; Km = 37 uM; printed kcat/Km = 34 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K19Q to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K19Q; column kcat (s^-1) = 12 ± 0.3; column KM (uM) under PPi = 50; column kcat/KM (mM^-1 s^-1) under PPi = 300.

normalized_value_unit_evidence: kcat: printed cell 12 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 12.0 s^-1. Km: printed cell 50 uM; 50 / 1000 = 0.05 mM. kcat/Km: printed cell 300 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 300.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K19Q, PPi column group: kcat = 12 ± 0.3 s^-1; Km = 50 uM; printed kcat/Km = 300 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K100A; column kcat (s^-1) = 12 ± 0.2; column KM (uM) under PPi = 958; column kcat/KM (mM^-1 s^-1) under PPi = 11.

normalized_value_unit_evidence: kcat: printed cell 12 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 12.0 s^-1. Km: printed cell 958 uM; 958 / 1000 = 0.958 mM. kcat/Km: printed cell 11 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 11.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K100A, PPi column group: kcat = 12 ± 0.2 s^-1; Km = 958 uM; printed kcat/Km = 11 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB P08870 canonical sequence; K26Q reconstructed after direct residue check and UniProt mutagenesis feature. and applied mutation signature K26Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P08870 canonical sequence; K19Q reconstructed after direct residue check and UniProt mutagenesis feature. and applied mutation signature K19Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: orotate phosphoribosyltransferase(Enzyme) mutant K19Q


sequence_source: UniProtKB P08870 FASTA/REST canonical sequence.

column_label: Table 5: Pyrophosphate Analogs as Substrates or Inhibitors of Wild-Type OPRTase (Biochemistry 1995, 34(34):10755-10763); enzyme row WT; column kcat (s^-1) = 0.04; column Km (uM) under phosphonoacetic acid = 1850; column kcat/KM (mM^-1 s^-1) under phosphonoacetic acid = 0.02.

normalized_value_unit_evidence: kcat: printed cell 0.04 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.04 s^-1. Km: printed cell 1850 uM; 1850 / 1000 = 1.85 mM. kcat/Km: printed cell 0.02 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 0.02 s^-1 mM^-1.

raw_value_unit_evidence: Table 5, Pyrophosphate Analogs as Substrates or Inhibitors of Wild-Type OPRTase, enzyme row WT, phosphonoacetic acid column group: kcat = 0.04 s^-1; Km = 1850 uM; printed kcat/Km = 0.02 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K19Q; column kcat (s^-1) = 12 ± 0.3; column KM (uM) under OMP = 18; column kcat/KM (mM^-1 s^-1) under OMP = 830.

normalized_value_unit_evidence: kcat: printed cell 12 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 12.0 s^-1. Km: printed cell 18 uM; 18 / 1000 = 0.018 mM. kcat/Km: printed cell 830 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 830.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K19Q, OMP column group: kcat = 12 ± 0.3 s^-1; Km = 18 uM; printed kcat/Km = 830 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K19Q; column kcat (s^-1) = 31 ± 0.9; column KM (uM) under PRPP = 96; column kcat/KM (mM^-1 s^-1) under PRPP = 320.

normalized_value_unit_evidence: kcat: printed cell 31 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 31.0 s^-1. Km: printed cell 96 uM; 96 / 1000 = 0.096 mM. kcat/Km: printed cell 320 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 320.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K19Q, PRPP column group: kcat = 31 ± 0.9 s^-1; Km = 96 uM; printed kcat/Km = 320 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K103Q to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K103Q; column kcat (s^-1) = 0.13 ± 0.001; column KM (uM) under orotate = 34; column kcat/KM (mM^-1 s^-1) under orotate = 4.

normalized_value_unit_evidence: kcat: printed cell 0.13 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.13 s^-1. Km: printed cell 34 uM; 34 / 1000 = 0.034 mM. kcat/Km: printed cell 4 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 4.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K103Q, orotate column group: kcat = 0.13 ± 0.001 s^-1; Km = 34 uM; printed kcat/Km = 4 mM^-1 s^-1.


column_label: Table 7: Kinetic Constants of Orotate, Orotate 6-Methyl Ester, and Uracil in Wild-Type and Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase (Biochemistry 1995, 34(34):10755-10763); enzyme row WT; column kcat (s^-1) = 0.9; column Km (uM) under uracil = 3160; column kcat/KM (mM^-1 s^-1) under uracil = 0.3.

normalized_value_unit_evidence: kcat: printed cell 0.9 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.9 s^-1. Km: printed cell 3160 uM; 3160 / 1000 = 3.16 mM. kcat/Km: printed cell 0.3 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 0.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 7, Kinetic Constants of Orotate, Orotate 6-Methyl Ester, and Uracil, enzyme row WT, uracil column group: kcat = 0.9 s^-1; Km = 3160 uM; printed kcat/Km = 0.3 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K19Q; column kcat (s^-1) = 31 ± 0.9; column KM (uM) under orotate = 78; column kcat/KM (mM^-1 s^-1) under orotate = 400.

normalized_value_unit_evidence: kcat: printed cell 31 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 31.0 s^-1. Km: printed cell 78 uM; 78 / 1000 = 0.078 mM. kcat/Km: printed cell 400 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 400.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K19Q, orotate column group: kcat = 31 ± 0.9 s^-1; Km = 78 uM; printed kcat/Km = 400 mM^-1 s^-1.


organism: Saccharomyces cerevisiae

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


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08870 + PMID:7545005 mutagenesis feature and applied mutation signature K100A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: orotate phosphoribosyltransferase(Enzyme) mutant K100A


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08870 + PMID:7545005 mutagenesis feature and applied mutation signature K26Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: orotate phosphoribosyltransferase(Enzyme) mutant K26Q


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K100A to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K100A; column kcat (s^-1) = 12 ± 0.2; column KM (uM) under OMP = 13; column kcat/KM (mM^-1 s^-1) under OMP = 830.

normalized_value_unit_evidence: kcat: printed cell 12 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 12.0 s^-1. Km: printed cell 13 uM; 13 / 1000 = 0.013 mM. kcat/Km: printed cell 830 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 830.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K100A, OMP column group: kcat = 12 ± 0.2 s^-1; Km = 13 uM; printed kcat/Km = 830 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K103A to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K103A; column kcat (s^-1) = 0.05 ± 0.0005; column KM (uM) under PPi = 146; column kcat/KM (mM^-1 s^-1) under PPi = 0.3.

normalized_value_unit_evidence: kcat: printed cell 0.05 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.05 s^-1. Km: printed cell 146 uM; 146 / 1000 = 0.146 mM. kcat/Km: printed cell 0.3 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 0.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K103A, PPi column group: kcat = 0.05 ± 0.0005 s^-1; Km = 146 uM; printed kcat/Km = 0.3 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K26Q to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K26Q; column kcat (s^-1) = 3.1 ± 0.03; column KM (uM) under orotate = 65; column kcat/KM (mM^-1 s^-1) under orotate = 48.

normalized_value_unit_evidence: kcat: printed cell 3.1 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 3.1 s^-1. Km: printed cell 65 uM; 65 / 1000 = 0.065 mM. kcat/Km: printed cell 48 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 48.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K26Q, orotate column group: kcat = 3.1 ± 0.03 s^-1; Km = 65 uM; printed kcat/Km = 48 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P08870 and applied mutation signature K26A to reconstruct the assayed variant sequence.

column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Forward Reaction block; enzyme row K26A; column kcat (s^-1) = 8.7±0.2; column KM (uM) under PRPP = 50; column kcat/KM (mM^-1 s^-1) under PRPP = 175.

normalized_value_unit_evidence: kcat: printed cell 8.7 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 8.7 s^-1. Km: printed cell 50 uM; 50 / 1000 = 0.05 mM. kcat/Km: printed cell 175 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 175.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Forward Reaction, enzyme row K26A, PRPP column group: kcat = 8.7±0.2 s^-1; Km = 50 uM; printed kcat/Km = 175 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P08870 direct REST lookup; reviewed Swiss-Prot entry PYRE_SALTY, sequence version 3 and applied mutation signature K103Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: orotate phosphoribosyltransferase(Enzyme) mutant K103Q


column_label: Table 7: Kinetic Constants of Orotate, Orotate 6-Methyl Ester, and Uracil in Wild-Type and Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase (Biochemistry 1995, 34(34):10755-10763); enzyme row K26A; column kcat (s^-1) = 0.7; column Km (uM) under uracil = 3710; column kcat/KM (mM^-1 s^-1) under uracil = 0.2.

normalized_value_unit_evidence: kcat: printed cell 0.7 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.7 s^-1. Km: printed cell 3710 uM; 3710 / 1000 = 3.71 mM. kcat/Km: printed cell 0.2 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 0.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 7, Kinetic Constants of Orotate, Orotate 6-Methyl Ester, and Uracil, enzyme row K26A, uracil column group: kcat = 0.7 s^-1; Km = 3710 uM; printed kcat/Km = 0.2 mM^-1 s^-1.


sequence_source: UniProtKB:P08870 direct REST lookup; reviewed Swiss-Prot entry PYRE_SALTY, sequence version 3


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K26Q; column kcat (s^-1) = 1.3 ± 0.01; column KM (uM) under PPi = 111; column kcat/KM (mM^-1 s^-1) under PPi = 11.

normalized_value_unit_evidence: kcat: printed cell 1.3 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 1.3 s^-1. Km: printed cell 111 uM; 111 / 1000 = 0.111 mM. kcat/Km: printed cell 11 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 11.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K26Q, PPi column group: kcat = 1.3 ± 0.01 s^-1; Km = 111 uM; printed kcat/Km = 11 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K103A; column kcat (s^-1) = 0.05 ± 0.0005; column KM (uM) under OMP = 20; column kcat/KM (mM^-1 s^-1) under OMP = 2.

normalized_value_unit_evidence: kcat: printed cell 0.05 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.05 s^-1. Km: printed cell 20 uM; 20 / 1000 = 0.02 mM. kcat/Km: printed cell 2 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 2.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K103A, OMP column group: kcat = 0.05 ± 0.0005 s^-1; Km = 20 uM; printed kcat/Km = 2 mM^-1 s^-1.


column_label: Table 4: Kinetic Parameters of the Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase for the Forward and Reverse Reactions (Biochemistry 1995, 34(34):10755-10763), Kinetic Parameters for the Reverse Reaction block; enzyme row K26A; column kcat (s^-1) = 9.6 ± 0.1; column KM (uM) under OMP = 19; column kcat/KM (mM^-1 s^-1) under OMP = 500.

normalized_value_unit_evidence: kcat: printed cell 9.6 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 9.6 s^-1. Km: printed cell 19 uM; 19 / 1000 = 0.019 mM. kcat/Km: printed cell 500 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 500.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 4, Kinetic Parameters for the Reverse Reaction, enzyme row K26A, OMP column group: kcat = 9.6 ± 0.1 s^-1; Km = 19 uM; printed kcat/Km = 500 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB P08870 canonical sequence with selected-source mutation reconstruction and applied mutation signature K100A to reconstruct the assayed variant sequence.


column_label: Table 7: Kinetic Constants of Orotate, Orotate 6-Methyl Ester, and Uracil in Wild-Type and Lysine Mutants of S. typhimurium Orotate Phosphoribosyltransferase (Biochemistry 1995, 34(34):10755-10763); enzyme row K26Q; column kcat (s^-1) = 0.7; column Km (uM) under uracil = 1810; column kcat/KM (mM^-1 s^-1) under uracil = 0.4.

normalized_value_unit_evidence: kcat: printed cell 0.7 s^-1; the column head reads kcat (s^-1), so the printed cell is already in s^-1 and no unit conversion applies; the value is 0.7 s^-1. Km: printed cell 1810 uM; 1810 / 1000 = 1.81 mM. kcat/Km: printed cell 0.4 mM^-1 s^-1; the column head reads kcat/KM (mM^-1 s^-1), which is the canonical s^-1 mM^-1 written the other way round, so no unit conversion applies; the value is 0.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 7, Kinetic Constants of Orotate, Orotate 6-Methyl Ester, and Uracil, enzyme row K26Q, uracil column group: kcat = 0.7 s^-1; Km = 1810 uM; printed kcat/Km = 0.4 mM^-1 s^-1.


sequence_variant_note: Resolved canonical sequence from UniProtKB P08870 canonical sequence with selected-source mutation reconstruction and applied mutation signature K103A/K73Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: orotate phosphoribosyltransferase(Enzyme) mutant K103A/K73Q


sequence_source: UniProtKB P08870 canonical sequence


sequence_variant_note: Resolved canonical sequence from UniProtKB P08870 canonical sequence with selected-source mutation reconstruction and applied mutation signature K103A/K73A to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: orotate phosphoribosyltransferase(Enzyme) mutant K103A/K73A


sequence_variant_note: Resolved canonical sequence from UniProtKB P08870 canonical sequence with selected-source mutation reconstruction and applied mutation signature K103A/D125N to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: orotate phosphoribosyltransferase(Enzyme) mutant K103A/D125N


organism: Vigna mungo

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


organism: Unknown

substrate_name: Orotidine

substrate: Orotidine


organism: Homo sapiens

proof_lines: kcat is 0.75 sec(-1) with orotidine 5'-phosphate as substrate.


proof_lines: uncompetitive to 5-phospho-alpha-D-ribose 1-diphosphate, pH 8.0, 25°C


organism: Phaseolus vulgaris


proof_lines: in the presence of 20 mM phosphonoacetic acid, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2


organism: Rhizobium leguminosarum


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: Orotate methylester

substrate: Orotate methylester


organism: Corynebacterium ammoniagenes

sequence_source: UniProt A8CVW0, found by direct UniProt lit_pubmed:17921291 follow-up


sequence_source: UniProt P0A7E3, selected as E. coli K-12 OPRTase context after PubMed PMID 2419315 identified the wild-type K-12 enzyme


substrate_name: orotidine 5'-monophosphate

substrate: orotidine 5'-monophosphate


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


proof_lines: in the presence of 1 mM diphosphate, at 25°C, 50 mM Tris-HCl, pH 8.0, 5 mM MgCl2


organism: Mus musculus


organism: Thermus thermophilus


organism: Toxoplasma gondii


organism: Leishmania donovani

sequence_source: UniProtKB H9ABU0 mapped from RefSeq XP_003864273.1, which NCBI links to PMID 23986453

proof_lines: with uracil as cosubstrate, at pH 7.5 and 25°C


organism: Pisum sativum


organism: Saccharolobus shibatae

proof_lines:
pH 6.1, without GTP
pH 6.1, presence of 1 mM GTP
pH 8.0, presence of 1 mM GTP


organism: Saccharolobus solfataricus

proof_lines:
activated by 1 mM GTP
unactivated enzyme


organism: Tetrahymena pyriformis


organism: Acidithiobacillus ferrooxidans

substrate_name: D-arabinose 5-phosphate

substrate: D-arabinose 5-phosphate


enzyme_display_name: tannase

substrate_name: methyl gallate

enzyme: tannase

substrate: methyl gallate


organism: Hypocreales sp.

substrate_name: Tannic acid

proof_lines:
isozyme TAH I, pH 5.5, 20°C
isozyme TAH II, pH 5.5, 20°C

substrate: Tannic acid


organism: Streptomyces sviceus


proof_lines: pH 7.0, 37°C, recombinant flap domain lacking enzyme mutant


enzyme_display_name: Carboxylic ester hydrolase (EC 3.1.1.-)

organism: Aspergillus awamori

enzyme: Carboxylic ester hydrolase (EC 3.1.1.-)


organism: Aspergillus niger

proof_lines:
recombinant enzyme, pH 5.0, 30°C
recombinant enzyme, pH 5.0, 20°C


substrate_name: propyl gallate

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

substrate: propyl gallate


enzyme_display_name: Tannase (EC 3.1.1.20) [Cleaved into: Tannase 33 kDa subunit; Tannase 30 kDa subunit]

organism: Aspergillus oryzae

substrate_name: H2O; Methyl gallate

substrate: H2O; Methyl gallate


substrate_name: (-)-catechin gallate

substrate: (-)-catechin gallate


substrate_name: (-)-epigallocatechin gallate

substrate: (-)-epigallocatechin gallate


substrate_name: (-)-gallocatechin gallate

substrate: (-)-gallocatechin gallate


substrate_name: ethyl protocatechuate

substrate: ethyl protocatechuate


organism: Lactiplantibacillus plantarum

sequence_source: UniProtKB:B3Y018 FASTA/API direct check; RCSB 4J0C maps B3Y018 to Lactobacillus plantarum tannase.

proof_lines: wild type enzyme, in 25 mM Tris-HCl (pH 8.0), at 37°C

proof_lines: pH 7.0, 37°C, recombinant wild-type enzyme


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:B3Y018 FASTA/API direct check by applying E357A. and applied mutation signature E357A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:B3Y018 FASTA/API direct check by applying D421A. and applied mutation signature D421A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D421A, in 25 mM Tris-HCl (pH 8.0), at 37°C


sequence_source: UniProtKB:B3Y018 FASTA/API direct check; PubMed 24708557 identifies TanLpl from L. plantarum in a tannase comparison study.


substrate_name: catechin gallate

substrate: catechin gallate


proof_lines:
in 50 mM Tris-HCl (pH 8.0), at 37°C
at pH 8.0
Raw SKiD Env: Temp=37°C, pH=8


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:B3Y018 FASTA/API direct check by applying P356G. and applied mutation signature P356G to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:B3Y018 FASTA/API direct check; PubMed 23836494, 24708557, and 30232563 all support the L. plantarum tannase literature context.

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


sequence_source: UniProtKB accession Q2UII1 direct lookup


substrate_name: (-)-epicatechin gallate

substrate: (-)-epicatechin gallate


organism: Aureobasidium melanogenum

substrate_name: gallocatechin gallate

sequence_source: UniProtKB accession A0A5C2H0R5 direct lookup

substrate: gallocatechin gallate


organism: Blastobotrys adeninivorans

sequence_source: UniProtKB accession B7VFD0 direct lookup

proof_lines:
recombinant tannase, at 30°C, pH 6.0
endogenous tannase, at 30°C, pH 6.0
endogenous tannase


sequence_variant_note: Resolved canonical sequence from UniProtKB accession B3Y018 direct lookup and applied mutation signature K343A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme K343A, in 25 mM Tris-HCl (pH 8.0), at 37°C


sequence_variant_note: Resolved canonical sequence from UniProtKB accession B3Y018 direct lookup and applied mutation signature D421A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB accession B3Y018 direct lookup and applied mutation signature E357A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E357A, in 25 mM Tris-HCl (pH 8.0), at 37°C


sequence_source: UniProtKB:B3Y018 exact accession lookup; current entry names Lactiplantibacillus plantarum tannase and cross-references BRENDA 3.1.1.20.


proof_lines: pH 7.0, 37°C, recombinant flap domain-lacking enzyme mutant


organism: Lactobacillus plantarum

substrate_name: Methyl gallate; H2O

sequence_source: UniProtKB:B3Y018 exact accession lookup; current entry names Lactiplantibacillus plantarum tannase and cites PMID 18653299 for the nucleotide sequence.

substrate: Methyl gallate; H2O


sequence_source: UniProtKB:A0A077YGC3 exact accession lookup; current entry names Streptomyces sviceus tannase protein and cross-references BRENDA 3.1.1.20.


organism: Rhizobium leguminosarum bv. trifolii

substrate_name: orotate

substrate: orotate


enzyme_display_name: licheninase

organism: Fibrobacter succinogenes

substrate_name: lichenan

sequence_variant_note: Resolved canonical sequence from UniProt P17989 canonical sequence; row-specific substitution reconstructed with paper numbering mapped to UniProt position by +23 offset. and applied mutation signature R209M with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

proof_lines: mutant R209M, calculated as D-glucose units released from lichenan

enzyme: licheninase

substrate: lichenan