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

proof_lines: native wild type enzyme, at pH 7.5 and 37°C

proof_lines: recombinant wild type enzyme, at pH 7.5 and 37°C


enzyme_display_name: tyrosine 3-monooxygenase

organism: Bos taurus

substrate_name: tyrosine

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

proof_lines:
bovine adrenal gland
bovine adrenal
versus tetrahydrobiopterin

enzyme: tyrosine 3-monooxygenase

substrate: tyrosine

source: brenda


organism: Heteropneustes fossilis

proof_lines: hypothalamus extract, 1 microM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C

proof_lines: telencephalon extract, 1 fM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C

proof_lines: hypothalamus extract, 1 fM estadriol-17beta, 0.1-0.5 mM L-tyrosine, 1-8 mM 6,7-dimethyl-2-amino-4-hydroxy-5,6,7,8-tetrahydopteridine, PBS buffer pH 6.2, 2-mercaptoethanol, catalase, 30°C


organism: Homo sapiens

substrate_name: L-tyrosine

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

mutation_type: substitution

substrate: L-tyrosine


protein_accession_database: UniProt

sequence_variant_note: Resolved canonical sequence from UniProtKB P07101-3 FASTA plus PMID 15468323/PMCID PMC1945158 mutation-construct evidence and applied mutation signature T245P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07101-3 FASTA plus PMID 15468323/PMCID PMC1945158 mutation-construct evidence and applied mutation signature T283M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P07101-3 FASTA plus PMID 15468323/PMCID PMC1945158 mutation-construct evidence and applied mutation signature T463M to reconstruct the assayed variant sequence.


proof_lines: 0.1 mM L-tyrosine, 0.1 mg/ml catalase, 50 mM HEPES pH 7.0, 0.01 mM ferrous ammonium sulfate, 1 mM dithiothreitol, 25°C

proof_lines: recombinant isoform hTH1, with 6-methyltetrahydropterin

proof_lines: recombinant phosphorylated hTH1, L-dopa-oxidase activity


organism: Mucuna pruriens var. utilis

substrate_name: O2; Tetrahydrobiopterin; L-Tyrosine

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

substrate: O2; Tetrahydrobiopterin; L-Tyrosine


organism: Portulaca grandiflora


enzyme_display_name: adenosylmethionine decarboxylase

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

substrate_name: S-adenosyl-L-methionine

source_db: uniprot

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

proof_lines: The turnover number increases 30-fold when temperature is increased from 22 to 70 degrees Celsius, whereas the Km increases 3-fold.

data_origin: experimental

enzyme: adenosylmethionine decarboxylase

substrate: S-adenosyl-L-methionine

source: uniprot


enzyme_display_name: L-fuculose-phosphate aldolase

organism: Escherichia coli (strain K12)

substrate_name: L-fuculose 1-phosphate

proof_lines: kcat is 19.3 sec(-1) for L-fuculose 1-phosphate (Fuc1P) as substrate.

enzyme: L-fuculose-phosphate aldolase

substrate: L-fuculose 1-phosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 0.0276 sec(-1) with 4-hydroxy-4-methyl-2-oxoglutarate as substrate and 3.91 sec(-1) with oxaloacetate as substrate.


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

proof_lines: kcat is 0.356 sec(-1) with 4-hydroxy-4-methyl-2-oxoglutarate as substrate and 1.06 sec(-1) with oxaloacetate as substrate.


enzyme_display_name: nitrile hydratase

organism: Caldalkalibacillus thermarum (strain TA2.A1)

substrate_name: 3-cyanopyridine (at pH 7.4 and 30 degrees Celsius)

proof_lines: Measured for the whole complex (PubMed:34363653, PubMed:34454178). kcat is 352.1 sec(-1) with 3-cyanopyridine as substrate (at pH 7.4 and 30 degrees Celsius) (PubMed:34454178). kcat is 119.4 sec(-1) with 3-cyanopyridine as substrate (at pH

enzyme: nitrile hydratase


organism: Pseudonocardia thermophila

substrate_name: acrylonitrile (at pH 7.6 and 25 degrees Celsius)

proof_lines: Measured for the whole complex (PubMed:14717710, PubMed:24383915, PubMed:35919716, PubMed:38677005, PubMed:39447484, Ref.6). kcat is 1910 sec(-1) (at pH 7.6 and 25 degrees Celsius) with acrylonitrile as substrate (PubMed:14717710). kcat is


organism: Rattus norvegicus


substrate_name: L-Tyr

substrate: L-Tyr


proof_lines: pH 7.0, 30°C, mutant enzyme S19A, cosubstrate 0.3 mM tetrahydropterin

proof_lines: pH 7.0, 30°C, mutant enzyme S19A, cosubstrate 0.4 mM 6-methyltetrahydropterin


proof_lines: pH 7.0, 30°C, mutant enzyme S19E, cosubstrate 0.3 mM tetrahydropterin

proof_lines: pH 7.0, 30°C, mutant enzyme S19E, cosubstrate 0.4 mM 6-methyltetrahydropterin


proof_lines: pH 7.0, 30°C, mutant enzyme S31E, cosubstrate 0.3 mM tetrahydropterin

proof_lines: pH 7.0, 30°C, mutant enzyme S31E, cosubstrate 0.4 mM 6-methyltetrahydropterin


proof_lines: pH 7.0, 30°C, mutant enzyme S19E/S40E, cosubstrate 0.3 mM tetrahydropterin

proof_lines: pH 7.0, 30°C, mutant enzyme S19E/S40E, cosubstrate 0.4 mM 6-methyltetrahydropterin


proof_lines: pH 7.0, 30°C, mutant enzyme S31A, cosubstrate 0.3 mM tetrahydropterin

proof_lines: pH 7.0, 30°C, mutant enzyme S31A, cosubstrate 0.4 mM 6-0.053 methyltetrahydropterin


proof_lines: pH 7.0, 30°C, mutant enzyme S40A, cosubstrate 0.4 mM 6-methyltetrahydropterin

proof_lines: pH 7.0, 30°C, mutant enzyme S40A, cosubstrate 0.3 mM tetrahydropterin


proof_lines: pH 7.0, 30°C, mutant enzyme S8E, cosubstrate 0.3 mM tetrahydropterin

proof_lines: pH 7.0, 30°C, mutant enzyme S8E, cosubstrate 0.4 mM 6-methyltetrahydropterin


proof_lines: pH 7.0, 30°C, mutant enzyme S8A, cosubstrate 0.4 mM 6-methyltetrahydropterin

proof_lines: pH 7.0, 30°C, mutant enzyme S8A, cosubstrate 0.3 mM tetrahydropterin


proof_lines: pH 7.0, 30°C, mutant enzyme S40E, cosubstrate 0.3 mM tetrahydropterin

proof_lines: pH 7.0, 30°C, mutant enzyme S40E, cosubstrate 0.4 mM 6-methyltetrahydropterin


enzyme_display_name: soluble epoxide hydrolase

organism: Caenorhabditis elegans

substrate_name: trans-1,3-diphenylpropene oxide

proof_lines: kcat is 12 sec(-1) with trans-1,3-diphenylpropene oxide as substrate. kcat is 0.11 sec(-1) with 12,13-epoxy-9-octadecenoate as substrate. kcat is 0.22 sec(-1) with 9,10-epoxy-12-octadecenoate as substrate.

enzyme: soluble epoxide hydrolase

substrate: trans-1,3-diphenylpropene oxide


proof_lines: kcat are 14 sec(-1), 354 sec(-1), 167 sec(-1), 125 sec(-1), 177 sec(-1), 250 sec(-1), 18 sec(-1) and 136 sec(-1) for farnesyl pyro-phosphate, 1-myristoyl-2-hydroxy-3-glycerophosphate, 1-palmityl-2-hydroxy-3-glycerophosphate, 1-stearyl-2-hyd


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: PHOME

proof_lines: kcat is 18.45 sec(-1) with PHOME as substrate.

substrate: PHOME


enzyme_display_name: 2-hydroxy-dATP diphosphatase

substrate_name: CoA

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 4.6 sec(-1) with CoA as substrate (PubMed:10922370). kcat is 5.0 sec(-1) with CoASSCoA as substrate (PubMed:10922370). kcat is 0.133 sec(-1) with 8-oxo-dGTP as substrate using a GST-fused enzyme (PubMed:15475388).

enzyme: 2-hydroxy-dATP diphosphatase

substrate: CoA


enzyme_display_name: oxaloacetate decarboxylase

organism: Bacillus subtilis (strain 168)

substrate_name: enol-oxaloacetate

proof_lines: kcat is 237 sec(-1) with enol-oxaloacetate as substrate (PubMed:38287013). kcat is 0.52 sec(-1) with oxaloacetate as substrate for koxaloacetate decarboxylase activity (PubMed:38287013).

enzyme: oxaloacetate decarboxylase

substrate: enol-oxaloacetate


substrate_name: KDPG

proof_lines: kcat is 83 sec(-1) with KDPG as substrate (PubMed:17962400). kcat is 80 sec(-1) with KDPG as substrate (PubMed:17981470). kcat is 11 sec(-1) with KHPB as substrate (PubMed:17962400). kcat is 0.0063 sec(-1) with KDPGal as substrate (PubMed:1

substrate: KDPG


substrate_name: Tetrahydropterin

proof_lines: recombinant enzyme, value is pH-dependent

substrate: Tetrahydropterin


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_paper_mutagenesis and applied mutation signature W166F/W233F/W372F/F74W to reconstruct the assayed variant sequence.

proof_lines: W166F/W233F/W372F/F74W mutant protein, pH 7, 25°C


proof_lines: pH 7.0, 30°C, wild-type enzyme, cosubstrate 0.3 mM tetrahydropterin


sequence_variant_note: Resolved canonical sequence from uniprot_accession_plus_paper_mutagenesis and applied mutation signature W166F/W233F/W372F/F34W to reconstruct the assayed variant sequence.

proof_lines: W166F/W233F/W372F/F34W mutant protein, pH 7, 25°C


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -1, so it is treated as a source-provided variant sequence.

proof_lines: W166F/W233F/W372F/F14W mutant protein, pH 7, 25°C


organism: Schistosoma japonicum

substrate_name: tetrahydrobiopterin

substrate: tetrahydrobiopterin


enzyme_display_name: dTMP kinase

organism: Bacillus anthracis

substrate_name: dTMP

sequence_source: UniProt REST accession Q81W11 FASTA/TSV retrieved 2026-06-04

enzyme: dTMP kinase

substrate: dTMP


organism: Candida albicans

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

sequence_source: UniProt REST accession Q59TV7 FASTA/TSV retrieved 2026-06-04

assay_conditions_summary: pH 7.4; cofactor NADH

proof_lines: pH 7.4, temperature not specified in the publication, NMR assay

proof_lines: pH 7.4, temperature not specified in the publication, NADH coupled assay

source_databases_merged: brenda skid


organism: Escherichia coli

substrate_name: dTMP; ATP

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

sequence_source: UniProt REST accession P0A720 FASTA/TSV retrieved 2026-06-04

assay_conditions_summary: cofactor ATP

substrate: dTMP; ATP


source_db: oed

source: oed


organism: Homo sapiens

substrate_name: Thiamine monophosphate; ATP

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

sequence_source: UniProt REST accession P23919 FASTA/TSV retrieved 2026-06-04

assay_conditions_summary: pH 7.4; 310.15 K; cofactor ATP

proof_lines: at 37°C in 50 mM Tris-HCl, pH 7.4, containing 50 mM KCl and 5 mM MgCl2

proof_lines: pH 7.5, 25°C, reaction with 3-fluoro-3-deoxythymidine 5-monophosphate

source_databases_merged: sabio_rk brenda skid

substrate: Thiamine monophosphate; ATP


substrate_name: dUMP

kcat_over_km_origin: calculated

substrate: dUMP


verification_status: verified

assay_conditions_summary: pH 7.4; 310.15 K; buffer Tris-HCl 50 mM pH = 7.4; cofactor NADH

column_label: Table 1 (Enzymatic Parameters for [E]-C5-Substituted Uracil Acyclic Phosphonates with Human TMP Kinase), series 'B- Butenyl', row 'F- 9b (E)-5F-UbutP'; column 'KM (mM)' = 1; column 'kcat (s-1)' = 0.73; column 'kcat/KM (M-1 s-1)' = 730.

normalized_value_unit_evidence: Km: printed Table 1 cell 1 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 1.0 mM. kcat: printed Table 1 cell 0.73 s-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 0.73 s^(-1). kcat/Km: printed Table 1 cell 730 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 730 / 1000 = 0.73 s^-1 mM^-1; the paper value carried here is 0.73 s^(-1)*mM^(-1)..

raw_value_unit_evidence: Table 1, series 'B- Butenyl', row 'F- 9b (E)-5F-UbutP': column 'KM (mM)' = 1; column 'kcat (s-1)' = 0.73; column 'kcat/KM (M-1 s-1)' = 730.

table_label: Table 1: Enzymatic Parameters for [E]-C5-Substituted Uracil Acyclic Phosphonates with Human TMP Kinase (J. Med. Chem. 2011, 54(1):222-232)

status: verified


column_label: Table 1 (Enzymatic Parameters for [E]-C5-Substituted Uracil Acyclic Phosphonates with Human TMP Kinase), references block, row 'dTMP'; column 'KM (mM)' = 0.02; column 'kcat (s-1)' = 3; column 'kcat/KM (M-1 s-1)' = 150 000.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.02 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 0.02 mM. kcat: printed Table 1 cell 3 s-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 3.0 s^(-1). kcat/Km: printed Table 1 cell 150,000 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 150000 / 1000 = 150.0 s^-1 mM^-1; the paper value carried here is 150.0 s^(-1)*mM^(-1)..

raw_value_unit_evidence: Table 1, references block, row 'dTMP': column 'KM (mM)' = 0.02; column 'kcat (s-1)' = 3; column 'kcat/KM (M-1 s-1)' = 150 000.

row_label: Table 1, references block, row 'dTMP'


organism: Unknown

substrate_name: dGMP

substrate: dGMP


sequence_source: source_record; direct UniProt Q5SIP7 check

proof_lines: kcat is 0.356 sec(-1) with 4-hydroxy-4-methyl-2-oxoglutarate as substrate and 1.06 sec(-1) with oxaloacetate as substrate.


organism: Drosophila melanogaster

substrate_name: dTMP; dUMP; dGMP; ATP

substrate: dTMP; dUMP; dGMP; ATP


substrate_name: ATP (at pH 7.4 and 30 degrees Celsius); dTMP (at pH 7.4 and 30 degrees Celsius)

assay_conditions_summary: pH 7.4; cofactor ATP


substrate_name: AZTMP; dTMP

substrate: AZTMP; dTMP


substrate_name: ATP (at pH 7.4 and 30 degrees Celsius); dTMP (at pH 7.4 and 30 degrees Celsius); dehydro-TMP (at pH 7.4 and 30 degrees Celsius); dUMP (at pH 7.4 and 30 degrees Celsius)


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: dTMP (at pH 7.2 and 30 degrees Celsius)

assay_conditions_summary: pH 7.2; cofactor ATP

proof_lines: kcat is 3.4 sec(-1) with dTMP as substrate (at pH 7.2 and 30 degrees Celsius) (PubMed:18477629). kcat is 3.2 sec(-1) with dTMP as substrate (at pH 7.2 and 30 degrees Celsius) (PubMed:19126267). kcat is 3.1 sec(-1) with dTMP as substrate (Pu

substrate: dTMP (at pH 7.2 and 30 degrees Celsius)


proof_lines: kcat is 31.1 sec(-1) with enol-oxaloacetate as substrate.


organism: Mus musculus

substrate_name: oxaloacetate

proof_lines: kcat is 210 nmol/min/mg for the decarboxylation of oxaloacetate. kcat is 140 nmol/min/mg for the hydrolysis of acetylpyruvate.

substrate: oxaloacetate


substrate_name: Unknown

km_display: Not reported

substrate: Unknown


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

proof_lines: The turnover number for the oxaloacetate decarboxylation is equal to 7500 per second.


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

proof_lines: kcat is 0.0276 sec(-1) with 4-hydroxy-4-methyl-2-oxoglutarate as substrate and 3.91 sec(-1) with oxaloacetate as substrate.


verification_status: unverified

sequence_source: UniProtKB:P23919 direct accession lookup, reviewed entry KTHY_HUMAN

status: unverified


column_label: Table 1 (Enzymatic Parameters for [E]-C5-Substituted Uracil Acyclic Phosphonates with Human TMP Kinase), references block, row '5Br-dUMP'; column 'KM (mM)' = 0.01; column 'kcat (s-1)' = 1.2; column 'kcat/KM (M-1 s-1)' = 120 000.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.01 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 0.01 mM. kcat: printed Table 1 cell 1.2 s-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 1.2 s^(-1). kcat/Km: printed Table 1 cell 120,000 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 120000 / 1000 = 120.0 s^-1 mM^-1; the paper value carried here is 120.0 s^(-1)*mM^(-1)..

raw_value_unit_evidence: Table 1, references block, row '5Br-dUMP': column 'KM (mM)' = 0.01; column 'kcat (s-1)' = 1.2; column 'kcat/KM (M-1 s-1)' = 120 000.


substrate_name: TMP

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

substrate: TMP


sequence_variant_note: Resolved canonical sequence from UniProtKB:P23919 canonical sequence with reviewer-reconstructed F105Y substitution and applied mutation signature F105Y to reconstruct the assayed variant sequence.

proof_lines: pH and temperature not specified in the publication, mutant enzyme F105Y


sequence_source: UniProtKB:P97930 direct accession lookup, reviewed entry KTHY_MOUSE

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


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:P9WKE1 direct accession lookup, reviewed entry KTHY_MYCTU

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: pH and temperature not specified in the publication


organism: Orthopoxvirus vaccinia

sequence_source: UniProtKB:P68693 direct accession lookup, reviewed entry KTHY_VACCC


sequence_source: UniProtKB reviewed accession P23919 (KTHY_HUMAN), direct REST/FASTA check on 2026-06-04

column_label: Table 1 (Enzymatic Parameters for [E]-C5-Substituted Uracil Acyclic Phosphonates with Human TMP Kinase), series 'C-Pentenyl', row 'F- 15b (E)-5F-UpenP'; column 'KM (mM)' = 1.9; column 'kcat (s-1)' = 0.09; column 'kcat/KM (M-1 s-1)' = 47.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.9 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 1.9 mM. kcat: printed Table 1 cell 0.09 s-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 0.09 s^(-1). kcat/Km: printed Table 1 cell 47 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 47 / 1000 = 0.047 s^-1 mM^-1; the exported 0.04736842105263158 s^(-1)*mM^(-1) is the full-precision quotient 0.09 / 1.9 of the same Table 1 row, and that quotient expressed in the printed unit is 47.368 M^-1 s^-1, which lies inside the rounding interval of the printed cell 47 M-1 s-1..

raw_value_unit_evidence: Table 1, series 'C-Pentenyl', row 'F- 15b (E)-5F-UpenP': column 'KM (mM)' = 1.9; column 'kcat (s-1)' = 0.09; column 'kcat/KM (M-1 s-1)' = 47.


verification_status: corrected

column_label: Table 1 (Enzymatic Parameters for [E]-C5-Substituted Uracil Acyclic Phosphonates with Human TMP Kinase), series 'C-Pentenyl', row 'Cl- 15c (E)-5Cl-UpenP'; column 'KM (mM)' = 0.15; column 'kcat (s-1)' = 0.1; column 'kcat/KM (M-1 s-1)' = 660.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.15 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 0.15 mM. kcat: printed Table 1 cell 0.1 s-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 0.1 s^(-1). kcat/Km: printed Table 1 cell 660 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 660 / 1000 = 0.66 s^-1 mM^-1; the paper value carried here is 0.66 s^(-1)*mM^(-1)..

raw_value_unit_evidence: Table 1, series 'C-Pentenyl', row 'Cl- 15c (E)-5Cl-UpenP': column 'KM (mM)' = 0.15; column 'kcat (s-1)' = 0.1; column 'kcat/KM (M-1 s-1)' = 660.

status: corrected


column_label: Table 1 (Enzymatic Parameters for [E]-C5-Substituted Uracil Acyclic Phosphonates with Human TMP Kinase), series 'C-Pentenyl', row 'CH3- 15e (E)-TpenP'; column 'KM (mM)' = 0.10; column 'kcat (s-1)' = 0.32; column 'kcat/KM (M-1 s-1)' = 3200.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.10 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 0.1 mM. kcat: printed Table 1 cell 0.32 s-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 0.32 s^(-1). kcat/Km: printed Table 1 cell 3200 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3200 / 1000 = 3.2 s^-1 mM^-1; the paper value carried here is 3.2 s^(-1)*mM^(-1)..

raw_value_unit_evidence: Table 1, series 'C-Pentenyl', row 'CH3- 15e (E)-TpenP': column 'KM (mM)' = 0.10; column 'kcat (s-1)' = 0.32; column 'kcat/KM (M-1 s-1)' = 3200.


column_label: Table 1 (Enzymatic Parameters for [E]-C5-Substituted Uracil Acyclic Phosphonates with Human TMP Kinase), series 'B- Butenyl', row 'CH3- 9e (E)-TbutP'; column 'KM (mM)' = 0.024; column 'kcat (s-1)' = 0.84; column 'kcat/KM (M-1 s-1)' = 35 000.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.024 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 0.024 mM. kcat: printed Table 1 cell 0.84 s-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 0.84 s^(-1). kcat/Km: printed Table 1 cell 35,000 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 35000 / 1000 = 35.0 s^-1 mM^-1; the paper value carried here is 35.0 s^(-1)*mM^(-1)..

raw_value_unit_evidence: Table 1, series 'B- Butenyl', row 'CH3- 9e (E)-TbutP': column 'KM (mM)' = 0.024; column 'kcat (s-1)' = 0.84; column 'kcat/KM (M-1 s-1)' = 35 000.


column_label: Table 1 (Enzymatic Parameters for [E]-C5-Substituted Uracil Acyclic Phosphonates with Human TMP Kinase), series 'A- Propenyl', row 'CH3- 6f (E)-TproP'; column 'KM (mM)' = 1; column 'kcat (s-1)' = 0.6; column 'kcat/KM (M-1 s-1)' = 600.

normalized_value_unit_evidence: Km: printed Table 1 cell 1 mM; the printed unit is already mM, so no unit conversion applies; the paper value is 1.0 mM. kcat: printed Table 1 cell 0.6 s-1; the printed unit is already s^(-1), so no unit conversion applies; the paper value is 0.6 s^(-1). kcat/Km: printed Table 1 cell 600 M-1 s-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 600 / 1000 = 0.6 s^-1 mM^-1; the paper value carried here is 0.6 s^(-1)*mM^(-1)..

raw_value_unit_evidence: Table 1, series 'A- Propenyl', row 'CH3- 6f (E)-TproP': column 'KM (mM)' = 1; column 'kcat (s-1)' = 0.6; column 'kcat/KM (M-1 s-1)' = 600.


organism: Plasmodium falciparum

ki_unit: mM


organism: Vaccinia virus

source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Wolbachia endosymbiont of Brugia malayi

substrate_name: ATP; dTMP

proof_lines: pH 7.4, temperature not specified in the publication

substrate: ATP; dTMP


organism: Schistosoma mansoni

sequence_source: UniProt O17446 (TY3H_SCHMA), reviewed entry; direct EC+organism lookup and exact lead-title match to PMID 9751167.


enzyme_display_name: arsenate reductase (thioredoxin)

organism: Oleidesulfovibrio alaskensis

substrate_name: arsenate

proof_lines:
pH 7.6, 37°C, presence of 150 mM NaCl
pH 7.6, 37°C, presence of 150 mM KCl
pH 7.6, 37°C, presence of 50 mM K2SO4

enzyme: arsenate reductase (thioredoxin)

substrate: arsenate


organism: Salinispora tropica

proof_lines: pH 7.5, temperature not specified in the publication


enzyme_display_name: lactaldehyde dehydrogenase

organism: Bacillus subtilis

substrate_name: L-lactaldehyde

assay_conditions_summary: cofactor NAD+

enzyme: lactaldehyde dehydrogenase

substrate: L-lactaldehyde


organism: Escherichia coli

substrate_name: phenylacetaldehyd

assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: 100 mM H2NaPO4 pH 7.5, 100 mM NaCl, 20 mM 2-mercaptoethanol, 2 mM NAD+

substrate: phenylacetaldehyd


substrate_name: propionaldehyde

sequence_source: UniProt P25553 (ALDA_ECOLI), reviewed entry; direct lookup found lactaldehyde dehydrogenase EC 1.2.1.22 and the PMID 18218709 lead title in UniProt references.

substrate: propionaldehyde


enzyme_display_name: triacylglycerol lipase

organism: Burkholderia cepacia

substrate_name: 4-nitrophenyl palmitate

sequence_source: UniProtKB REST FASTA https://rest.uniprot.org/uniprotkb/A9QXC9.fasta retrieved 2026-06-04

enzyme: triacylglycerol lipase

substrate: 4-nitrophenyl palmitate


organism: Homo sapiens

substrate_name: H2O; Flutamide

sequence_source: UniProtKB REST FASTA https://rest.uniprot.org/uniprotkb/P22760.fasta retrieved 2026-06-04

substrate: H2O; Flutamide


substrate_name: Flutamide; H2O

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: triacylglycerol lipase(Enzyme) mutant V310I

substrate: Flutamide; H2O


substrate_name: Phenacetin; H2O

sequence_variant_note: Resolved canonical sequence from Reviewer reconstruction from UniProtKB P22760 canonical sequence with source mutation N282Q applied and applied mutation signature N282Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant N282Q

substrate: Phenacetin; H2O


substrate_name: H2O; Phenacetin

sequence_variant_note: Resolved canonical sequence from Reviewer reconstruction from UniProtKB P22760 canonical sequence with source mutation N78Q/N282Q applied and applied mutation signature N78Q/N282Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant N78Q/N282Q

substrate: H2O; Phenacetin


sequence_variant_note: Resolved canonical sequence from Reviewer reconstruction from UniProtKB P22760 canonical sequence with source mutation N78Q applied and applied mutation signature N78Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant N78Q


substrate_name: H2O; p-Nitrophenyl acetate

sequence_source: UniProtKB REST FASTA https://rest.uniprot.org/uniprotkb/P19835.fasta retrieved 2026-06-04

substrate: H2O; p-Nitrophenyl acetate


sequence_source: UniProtKB REST FASTA https://rest.uniprot.org/uniprotkb/Q99PG0.fasta retrieved 2026-06-04


assay_conditions_summary: cofactor NADP+


organism: Saccharomyces cerevisiae

substrate_name: NAD+; L-Lactaldehyde; H2O

substrate: NAD+; L-Lactaldehyde; H2O


enzyme_display_name: acetyl-CoA C-acyltransferase

organism: Candida tropicalis

enzyme: acetyl-CoA C-acyltransferase


organism: Cupriavidus necator

substrate_name: CoA

substrate: CoA


substrate_name: acetoacetyl-CoA

substrate: acetoacetyl-CoA


organism: Helianthus annuus


organism: Bacillus licheniformis

sequence_source: UniProtKB Q65HR4 direct REST/FASTA lookup on 2026-06-04


substrate_name: p-Nitrophenyl palmitate; H2O

sequence_source: UniProtKB P37957 direct REST/FASTA lookup on 2026-06-04

substrate: p-Nitrophenyl palmitate; H2O


sequence_source: UniProtKB Q79F14 direct REST/FASTA lookup on 2026-06-04


proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant 1 CEX


sequence_source: UniProtKB I6V559 direct REST/FASTA lookup on 2026-06-04


proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant 1 CEX L21G


proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant 1 CEX L21Q


organism: Bos taurus

sequence_source: UniProtKB Q2KI18 direct REST/FASTA lookup on 2026-06-04


organism: Mycobacterium tuberculosis

substrate_name: triolein

sequence_source: UniProtKB P77909 direct lookup; PMID 16354661 LipY paper context

substrate: triolein


organism: Rattus norvegicus

sequence_source: UniProtKB reviewed Q9QZH8 direct lookup; PMID 22207054 SABIO-RK context


organism: Rhizomucor miehei

substrate_name: 4-nitrophenyl octanoate

sequence_source: PMID 29101200 paper construct; NCBI GenBank KP164599.1 translation with T18K/T22I/S56C/N63C/V189C/E230I/D238C applied at +71 sequence offset

sequence_variant_note: Mutation signature T18K/T22I/S56C/N63C/V189C/E230I/D238C could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: 4-nitrophenyl octanoate


sequence_source: PMID 29101200 paper construct; NCBI GenBank KP164599.1 translation


sequence_source: PMID 29101200 paper construct; NCBI GenBank KP164599.1 translation with T18K/T22I/E230I applied at +71 sequence offset

sequence_variant_note: Mutation signature T18K/T22I/E230I could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Rhizopus oryzae

substrate_name: H2O; Trioleoylglycerol

proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant His143Ser

substrate: H2O; Trioleoylglycerol


substrate_name: Trioleoylglycerol; H2O

proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant Asp262Gly

substrate: Trioleoylglycerol; H2O


substrate_name: Trioleoylglycerol

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

substrate: Trioleoylglycerol


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

proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant Ala88Trp


proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant Thr82Ala


proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant Asp91Asn


proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant Glu265Asp


proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant Glu265Gln


proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant Asp203Ala


proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant Thr82Ser/Ala88Trp


sequence_source: UniProtKB Q12405 canonical sequence from direct REST accession lookup; row remains manual because kinetic/exact-EC blockers remain.


substrate_name: H2O; p-Nitrophenyl butyrate

sequence_source: UniProtKB P38139 canonical sequence from direct REST accession lookup

substrate: H2O; p-Nitrophenyl butyrate


sequence_source: UniProtKB Q06522 canonical sequence from direct REST accession lookup


organism: Staphylococcus xylosus

substrate_name: olive oil

sequence_variant_note: Resolved canonical sequence from UniProtKB Q2TPV1 canonical sequence from direct REST accession lookup, reconstructed with G311K from BRENDA/PMID 17521919 evidence and applied mutation signature G311K to reconstruct the assayed variant sequence.

substrate: olive oil


sequence_variant_note: Resolved canonical sequence from UniProtKB Q2TPV1 canonical sequence from direct REST accession lookup, reconstructed with G311L from BRENDA/PMID 17521919 evidence and applied mutation signature G311L to reconstruct the assayed variant sequence.


sequence_source: reconstructed from UniProtKB reviewed P19515 FASTA, direct lookup 2026-06-04 plus selected source mutation signature

sequence_variant_note: Mutation signature D156G/L258K/L267N/S83D could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme D156G/L258K/L267N/S83D, at pH 7.5 and 50°C


sequence_variant_note: Mutation signature D156S/L258K/L267N/S83D/L58K/R86K/W88V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme D156S/L258K/L267N/S83D/L58K/R86K/W88V, at pH 7.5 and 50°C


sequence_variant_note: Mutation signature D156G/L258K/L267N could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: mutant enzyme D156G/L258K/L267N, at pH 7.5 and 50°C


sequence_source: UniProtKB reviewed P19515 FASTA, direct lookup 2026-06-04

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


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +7, so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -27, so it is treated as a source-provided variant sequence.

proof_lines: mutant enzyme D156G/L258K, at pH 7.5 and 50°C


substrate_name: H2O; Trioleoylglycerol; H2O; Trioleoylglycerol; Oleate; sn-1,2-Dioleoylglycerol; Trioleoylglycerol; H2O; H2O; Butyl laurate; Butyl laurate; Dodecanoate; 1-Butanol

sequence_source: reconstructed from UniProtKB reviewed P61872 FASTA, direct lookup 2026-06-04 plus selected source mutation signature

sequence_variant_note: Mutation signature T82S could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant Thr82Ser


substrate_name: H2O; Trioleoylglycerol; H2O; Trioleoylglycerol; Oleate; sn-1,2-Dioleoylglycerol

sequence_variant_note: Mutation signature T82V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: triacylglycerol lipase(Enzyme) mutant Thr82Val


substrate_name: tributyrin

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

substrate: tributyrin


sequence_variant_note: Resolved canonical sequence from uniprot:Q2TPV1 and applied mutation signature G311D to reconstruct the assayed variant sequence.


substrate_name: 4-nitrophenyl butyrate

substrate: 4-nitrophenyl butyrate


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


organism: Amycolatopsis mediterranei (strain S699)

substrate_name: p-nitrophenyl palmitate (p-NPP) (at pH 8.0 and 60 degrees Celsius)

sequence_source: source_record; UniProt P0DX29 direct check

assay_conditions_summary: pH 8

proof_lines: kcat is 1468 sec(-1) with p-nitrophenyl palmitate (p-NPP) as substrate (at pH 8.0 and 60 degrees Celsius).


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: p-nitrophenyl acetate

sequence_source: source_record; UniProt Q06522 direct check

proof_lines: kcat is 0.87 sec(-1) with p-nitrophenyl acetat as substrate and 0.44 sec(-1) with p-nitrophenyl butyrate as substrate.

substrate: p-nitrophenyl acetate


organism: Arabidopsis thaliana

substrate_name: Unknown

substrate: Unknown


organism: Burkholderia plantarii

substrate_name: oil emulsion

substrate: oil emulsion


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

substrate_name: p-NP-butyrate

substrate: p-NP-butyrate


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

substrate: triacylglycerol


organism: Sus scrofa

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


organism: uncultured bacterium


substrate_name: 4-nitrophenyl laurate

substrate: 4-nitrophenyl laurate


substrate_name: p-nitrophenyl butyrate (PNB)

substrate: p-nitrophenyl butyrate (PNB)


organism: Sodiomyces alcalophilus

substrate_name: p-nitrophenol acetate

substrate: p-nitrophenol acetate


substrate_name: triolein

substrate: triolein


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Moesziomyces aphidis


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

substrate_name: tributyrin


organism: Rattus norvegicus

substrate_name: acetoacetyl-CoA

assay_conditions_summary: pH 8.2; cofactor CoA

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: 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: Unknown

substrate: Unknown


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

assay_conditions_summary: cofactor CoA

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

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

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

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

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

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

substrate: N-Chloroacetyl-L-norleucine; H2O


organism: Lactococcus lactis subsp. cremoris

substrate_name: H2O; N-Acetyl-L-alanine

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

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

sequence_source: UniProtKB:P37111 direct FASTA/JSON lookup

substrate: N-acetyl-L-Cys


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

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

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)

substrate: NAD (at pH 8.0)


organism: Malus domestica


organism: Solanum lycopersicum

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


substrate_name: 4-pyridine carboxaldehyde

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


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


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


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

sequence_source: UniProtKB reviewed entry Q8VWZ1

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


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+


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

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


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_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.

assay_conditions_summary: pH 8

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.