substrate_name: Phenylacetic acid; H2O

sequence_variant_note: Resolved canonical sequence from UniProt REST P27169 canonical sequence with direct residue-substitution reconstruction and applied mutation signature H115Q/H134Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant H115Q/H134Q

substrate: Phenylacetic acid; H2O


enzyme_display_name: arylesterase

organism: Homo sapiens

substrate_name: H2O; Phenylacetic acid

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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

km_unit: mM

sequence_source: UniProt REST P27169 canonical sequence

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

assay_conditions_summary: pH 8; 298.15 K; buffer pH 8

proof_lines: isoform PON1, pH and temperature not specified in the publication

source_db: brenda

enzyme: arylesterase

substrate: H2O; Phenylacetic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB P27169 FASTA with H134Q reconstructed after residue check on 2026-06-04 and applied mutation signature H134Q to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 8

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant H134Q


sequence_variant_note: Resolved canonical sequence from UniProtKB P27169 FASTA with H115Q reconstructed after residue check on 2026-06-04 and applied mutation signature H115Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant H115Q


substrate_name: naphthalen-2-yl acetate

source_license: CC BY 4.0

sequence_source: UniProtKB P27169 canonical FASTA checked on 2026-06-04

proof_lines: wild type enzyme, in 50 mM Tris-HCl with 1 mM CaCl2 (pH 8.0), at 25°C

substrate: naphthalen-2-yl acetate

source: brenda


substrate_name: phenyl acetate

kcat_display: Not reported

sequence_variant_note: Resolved canonical sequence from UniProtKB P27169 FASTA with Q192R reconstructed after residue check on 2026-06-04 and applied mutation signature Q192R to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q192R, in 50 mM Tris-HCl with 1 mM CaCl2 (pH 8.0), at 25°C

substrate: phenyl acetate


sequence_source: NCBI GenBank KC456194.1 / protein AGZ62947.1 translation, with UniProtKB P27169 as the human PON1 accession context

sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB P27169 FASTA with H115W reconstructed after residue check on 2026-06-04 and applied mutation signature H115W to reconstruct the assayed variant sequence.


source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

data_origin: experimental

status: unverified

source: oed


sequence_source: UniProtKB P27169 FASTA with H115W reconstructed after residue check on 2026-06-04


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


substrate_name: 4-nitrophenyl propionate

sequence_variant_note: Resolved canonical sequence from uniprot:Q15165 and applied mutation signature S311C to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme S311C, at pH 8.5 and 40Â°C

substrate: 4-nitrophenyl propionate


mutation_type: deletion

proof_lines: mutant enzyme 123-124del, at pH 8.5 and 40Â°C


sequence_variant_note: Resolved canonical sequence from uniprot:Q15165 and applied mutation signature A148G to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme A148G, at pH 8.5 and 40Â°C


organism: Lacticaseibacillus casei

substrate_name: 4-nitrophenyl pentanoate

substrate: 4-nitrophenyl pentanoate


organism: Lactobacillus casei

substrate_name: p-Nitrophenyl acetate; H2O

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

substrate: p-Nitrophenyl acetate; H2O


organism: Lactobacillus helveticus


substrate_name: H2O; Nafamostat

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

assay_conditions_summary: pH 7.4; 303.15 K; buffer 20 mM Tris-HCl

proof_lines: in 20 mM Tris-HCl buffer, pH 7.4, 1 mM CaCl2, temperature not specified in the publication

substrate: H2O; Nafamostat


organism: Unknown


organism: Mus musculus

substrate_name: 2-naphthyl acetate

sequence_source: UniProtKB reviewed FASTA accession Q62087, direct REST check 2026-06-04

substrate: 2-naphthyl acetate


sequence_source: UniProtKB reviewed FASTA accession P52430, direct REST check 2026-06-04

proof_lines: wild type enzyme, in simulated body fluid, at pH 7.34-7.4 and 37°C

proof_lines: wild type enzyme, in 20 mM Tris-HCl and 0.9 mM CaCl2, at pH 8 and 25°C


organism: Oryctolagus cuniculus

sequence_source: UniProtKB reviewed FASTA accession Q9BGN0, direct REST check 2026-06-04


organism: Pseudomonas fluorescens

km_display: Not reported

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant D99E C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant F227I C-terminal His6-tagged


sequence_source: UniProtKB reviewed FASTA accession P22862, direct REST check 2026-06-04

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


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant L29P C-terminal His6-tagged


substrate_name: H2O; p-Nitrophenyl acetate

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant T122P C-terminal His6-tagged

substrate: H2O; p-Nitrophenyl acetate


enzyme_display_name: arsenate reductase (thioredoxin)

organism: Bacillus subtilis (strain 168)

substrate_name: arsenate (in the presence of KCl)

source_db: uniprot

proof_lines: kcat is 96 min(-1) in the presence of KCl (PubMed:16797027). kcat is 80 min(-1) in the presence of NaCl (PubMed:16797027). kcat is 120 min(-1) in the presence of Na(2)SO(4) (PubMed:16797027). kcat is 95 min(-1) in the presence of K(2)SO(4)

enzyme: arsenate reductase (thioredoxin)

substrate: arsenate (in the presence of KCl)

source: uniprot


organism: Staphylococcus aureus

substrate_name: arsenate (below 1 mM arsenate)

proof_lines: kcat is 4.5 min(-1) with arsenate as substrate (at 2 uM arsenate) and kcat is 9.9 min(-1) with arsenate as substrate (at 10 mM arsenate) (PubMed:10606519). kcat is 54 min(-1) in the presence of KCl (PubMed:12682056, PubMed:16797027). kcat i

substrate: arsenate (below 1 mM arsenate)


enzyme_display_name: lactaldehyde dehydrogenase

organism: Escherichia coli (strain K12)

substrate_name: L-lactaldehyde

proof_lines: kcat is 761 sec(-1) with L-lactaldehyde as substrate (PubMed:27671251). kcat is 52 sec(-1) with glycolaldehyde as substrate (PubMed:31850327). kcat is 1100 min(-1) with glycolaldehyde as substrate. kcat is 37 min(-1) with acetaldehyde as su

enzyme: lactaldehyde dehydrogenase

substrate: L-lactaldehyde


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

substrate_name: propionaldehyde (at pH 7.5)

proof_lines: As the lactaldehyde used was a mixture of D and L isomers, the kinetic parameters do not reflect the possible stereospecificity of the enzyme.

substrate: propionaldehyde (at pH 7.5)


enzyme_display_name: acetyl-CoA C-acyltransferase

substrate_name: acetoacetyl-CoA

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 14.8 sec(-1) for the degradation of acetoacetyl-CoA (3-oxoacyl-CoA thiolase) (PubMed:25478839). kcat is 1.4 sec(-1) for the synthesis of acetoacetyl-CoA (PubMed:25478839). kcat is 0.02 sec(-1) for octanoyl-CoA hydrolysis (PubMed:254

enzyme: acetyl-CoA C-acyltransferase

substrate: acetoacetyl-CoA


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: CoA

proof_lines: kcat is 0.725 sec(-1) for 3,22-dioxochol-4-en-24-oyl-CoA substrate (PubMed:25482540). kcat is 0.076 sec(-1) for AcAcCoA substrate (PubMed:19822655). kcat is 0.018 sec(-1) for CoA substrate (PubMed:19822655).

substrate: CoA


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant Y69M C-terminal His6-tagged


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant M95T C-terminal His6-tagged


organism: Rattus norvegicus

proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant S74A


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant S74T


proof_lines: SABIO-RK modifier species: arylesterase(Enzyme) mutant S74C


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


proof_lines: wild type enzyme, in simulated body fluid, at pH 7.34-7.4 and 37°C


organism: Saccharolobus islandicus

substrate_name: 4-nitrophenyl acetate

substrate: 4-nitrophenyl acetate


organism: Saccharolobus solfataricus

sequence_source: UniProtKB B5BLW5 direct lookup on 2026-06-04; local identity cache preserved the same source_record sequence.

assay_conditions_summary: pH 7; 333.15 K; buffer 100 mM sodium phosphate

proof_lines: recombinant wild type enzyme, in 100 mM sodium phosphate buffer (pH 7.0), at 60°C


organism: Sulfolobus acidocaldarius

sequence_source: UniProtKB Q4J6Z8 direct lookup on 2026-06-04.


organism: Sulfolobus islandicus

verification_status: corrected

sequence_source: UniProtKB C4KKZ9 direct lookup on 2026-06-04.

assay_conditions_summary: pH 8; 298.15 K; buffer activity

column_label: Retained PLOS PDF page 8, Table 4, pNP-acetate (VIII), SisLac columns: kcat 0.20 +/- 0.01; Km 124 +/- 36 uM; kcat/Km 1.6 (+/- 0.5) x 10^3 M^-1 s^-1.

normalized_value_unit_evidence: Table 4: kcat 0.20 s^-1; Km 124 uM = 0.124 mM; independently printed kcat/Km 1.6 x 10^3 M^-1 s^-1 = 1.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 4 cells: kcat 0.20 +/- 0.01 s^-1; Km 124 +/- 36 uM; independently printed kcat/Km central value 1.6 x 10^3 M^-1 s^-1 with reported uncertainty +/- 0.5 x 10^3 M^-1 s^-1.

row_label: pNP-acetate (VIII) / SisLac

table_label: Table 4. Esterase activity of SisLac.

status: corrected


organism: uncultured organism

substrate_name: 1-naphthyl acetate

sequence_source: UniProtKB G0YFD9 direct lookup on 2026-06-04.

substrate: 1-naphthyl acetate


organism: Vulcanisaeta moutnovskia

sequence_source: UniProtKB F0QXN6 direct lookup on 2026-06-04.


enzyme_display_name: cyclomaltodextrin glucanotransferase

organism: Bacillus circulans

ki_unit: mM

sequence_variant_note: Resolved canonical sequence from UniProtKB:P43379 FASTA plus PubMed:11555657 mutation context and applied mutation signature F183N with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant F183N

enzyme: cyclomaltodextrin glucanotransferase


sequence_source: UniProtKB:P43379 FASTA plus PubMed:11555657 mutation context

sequence_variant_note: Mutation signature E264A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant E264A


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +15, so it is treated as a source-provided variant sequence.

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant F259N


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43379 FASTA plus PubMed:11555657 mutation context and applied mutation signature F183S with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant F183S


sequence_variant_note: Resolved canonical sequence from UniProtKB:P43379 FASTA plus PubMed:11555657 mutation context and applied mutation signature F183S/F259N with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant F183S/F259N


sequence_source: UniProtKB:P43379 FASTA

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


sequence_variant_note: Mutation signature K232L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant K232L


sequence_variant_note: Mutation signature K232Q could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant K232Q


organism: Paenibacillus macerans

substrate_name: sophoricoside

proof_lines: mutant enzyme A156V/L174P/A166Y, at pH 6.0 and 50°C

substrate: sophoricoside


organism: Shouchella lehensis

substrate_name: soluble starch

sequence_source: UniProtKB:A0A060M208 direct REST lookup on 2026-06-04

proof_lines:
free enzyme, pH 6, 60°C
crosslinked enzyme, pH 6, 60°C

substrate: soluble starch


substrate_name: alpha-Cyclodextrin

sequence_source: UniProtKB:P26827 direct REST lookup on 2026-06-04

substrate: alpha-Cyclodextrin


substrate_name: beta-Cyclodextrin

substrate: beta-Cyclodextrin


substrate_name: alpha-Methyl-D-glucopyranoside

substrate: alpha-Methyl-D-glucopyranoside


substrate_name: Glucose

substrate: Glucose


substrate_name: Maltose

substrate: Maltose


substrate_name: Starch

substrate: Starch


organism: Niallia circulans

substrate_name: maltodextrin

sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 direct REST lookup 2026-06-04 plus residue substitution reconstruction and applied mutation signature A599V/Y633A with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

substrate: maltodextrin


source_db: skid

source_license: CC BY-NC-ND 4.0

sequence_source: UniProtKB:P43379 direct REST lookup 2026-06-04

source: skid


sequence_variant_note: Resolved canonical sequence from UniProtKB:O52766 direct REST lookup 2026-06-04 plus residue substitution reconstruction and applied mutation signature K47W with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant K47W, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin


sequence_source: UniProtKB:O52766 direct REST lookup 2026-06-04

proof_lines: wild-type, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin


sequence_variant_note: Resolved canonical sequence from UniProtKB:O52766 direct REST lookup 2026-06-04 plus residue substitution reconstruction and applied mutation signature K47V with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant K47V, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin


sequence_variant_note: Resolved canonical sequence from UniProtKB:O52766 direct REST lookup 2026-06-04 plus residue substitution reconstruction and applied mutation signature K47F with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant K47F, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin


sequence_variant_note: Resolved canonical sequence from UniProtKB:O52766 direct REST lookup 2026-06-04 plus residue substitution reconstruction and applied mutation signature K47L with inferred residue-numbering offset -11 to reconstruct the assayed variant sequence.

proof_lines: mutant K47L, pH 5.5, 37°C, average molecular weight of 2150.68 Da for maltodextrin


sequence_source: UniProtKB:P04830 direct REST lookup 2026-06-04


sequence_source: UniProtKB:A0A097CPM3 plus mature-chain L600E reconstruction

sequence_variant_note: Mutation signature L600E matches the mutant residue at offset +7 and the reference residue at offset +9; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 plus mature-chain L600Y reconstruction and applied mutation signature L600Y with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 plus mature-chain L600R reconstruction and applied mutation signature L600R with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:A0A097CPM3 REST sequence

proof_lines:
wild-type, pH 6.5, 50°C
wild type enzyme, at pH 6.5 and 50°C


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 plus mature-chain A599N/Y633A reconstruction and applied mutation signature A599N/Y633A with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 plus mature-chain A599N reconstruction and applied mutation signature A599N to reconstruct the assayed variant sequence.


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


sequence_variant_note: Resolved canonical sequence from UniProtKB:A0A097CPM3 plus mature-chain A599V reconstruction and applied mutation signature A599V to reconstruct the assayed variant sequence.


substrate_name: starch

proof_lines: pH 6.0, 60°C, beta-cyclization activity, mutant A230V/H140Q

substrate: starch


sequence_source: UniProt:P43379 FASTA direct exact-accession lookup on 2026-06-04


organism: Geobacillus stearothermophilus

substrate_name: maltose, soluble starch

sequence_source: UniProtKB P31797 direct lookup; variant mapping from selected BRENDA note and UniProt mature-chain offset

sequence_variant_note: Mutation signature L277A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

substrate: maltose, soluble starch


substrate_name: soluble starch, maltose

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -4, so it is treated as a source-provided variant sequence.

substrate: soluble starch, maltose


sequence_variant_note: Resolved canonical sequence from UniProtKB P31797 direct lookup; variant mapping from selected BRENDA note and UniProt mature-chain offset and applied mutation signature L277M/G282A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_source: UniProtKB P30920 direct lookup; variant mapping from selected BRENDA note and UniProt mature-chain offset

sequence_variant_note: Mutation signature A230V could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 6.0, 60°C, beta-cyclization activity, mutant A230V


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -11, so it is treated as a source-provided variant sequence.

proof_lines: pH 6.0, 60°C, beta-cyclization activity, mutant K232E


sequence_variant_note: Mutation signature F283L could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 6.0, 60°C, beta-cyclization activity, mutant F283L


sequence_source: UniProtKB P30920 direct lookup

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

proof_lines: pH 6.0, 60°C, beta-cyclization activity, wild-type enzyme


sequence_variant_note: Mutation signature H140Q matches the mutant residue at offset +13 and the reference residue at offset -8; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

proof_lines: pH 6.0, 60°C, beta-cyclization activity, mutant H140Q


enzyme_display_name: succinyl-CoA:acetate CoA-transferase

organism: Acetobacter aceti

substrate_name: acetate

proof_lines: kcat is 280 sec(-1) with acetate. kcat is 201 sec(-1) with succinyl-CoA. kcat is 75 sec(-1) with acetyl-CoA. kcat is 36.5 sec(-1) with acetoacetate. kcat is 70.9 sec(-1) with succinate.

enzyme: succinyl-CoA:acetate CoA-transferase

substrate: acetate


proof_lines: kcat is 88.99 sec(-1) for N-benzyloxycarbonyl-L-tyrosine-p-nitrophenyl ester as substrate (PubMed:16515533). kcat is 62.4 sec(-1) for p-nitrophenyl butyrate as substrate (PubMed:9070299). kcat is 15.29 sec(-1) for p-nitrophenyl butyrate as


organism: Pseudomonas fluorescens

proof_lines: kcat is 9 sec(-1) with ethyl acetate as substrate. kcat is 25 sec(-1) with methyl acetate as substrate. kcat is 100 sec(-1) with peracetic acid as substrate. kcat is 0.12 sec(-1) with acetic acid as substrate. kcat is 0.094 sec(-1) with hyd


substrate_name: phenyl acetate (PA)

proof_lines: kcat is 521 sec(-1) with PA as substrate. kcat is 450 sec(-1) with alpha-NA as substrate. kcat is 285 sec(-1) with p-nitrophenyl butyrate (C4) as substrate. kcat is 467 sec(-1) with p-nitrophenyl caproate (C6) as substrate. kcat is 410 sec(

substrate: phenyl acetate (PA)


enzyme_display_name: trehalose-phosphatase

organism: Brugia malayi

substrate_name: trehalose 6-phosphate

proof_lines: kcat is 24 sec(-1) for trehalose 6-phosphate.

enzyme: trehalose-phosphatase

substrate: trehalose 6-phosphate


organism: Thermoplasma acidophilum (strain ATCC 25905 / DSM 1728 / JCM 9062 / NBRC 15155 / AMRC-C165)

substrate_name: Tre6P (at pH 8 and 50 degrees Celsius)

proof_lines: kcat is 10 sec(-1) and 0.8 sec(-1) for Tre6P and pNPP, respectively (at pH 8 and 50 degrees Celsius).

substrate: Tre6P (at pH 8 and 50 degrees Celsius)


enzyme_display_name: pyridoxal phosphatase

organism: Escherichia coli (strain K12)

substrate_name: PLP (in the presence of Mg(2+) and at pH 9)

assay_conditions_summary: pH 9

proof_lines: kcat is 1.0 sec(-1) with PLP as substrate (PubMed:16990279). kcat is 1.7 sec(-1) with PLP as substrate (PubMed:39133002). kcat is 0.1 sec(-1) with PNP as substrate (PubMed:39133002). kcat is 5.3 sec(-1) with Fru1,6bisP as substrate (PubMed:

enzyme: pyridoxal phosphatase


substrate_name: PNP

proof_lines: kcat is 1.9 sec(-1) with PNP as substrate (PubMed:39133002). kcat is 2.4 sec(-1) with PLP as substrate (PubMed:39133002). kcat is 12 sec(-1) with PLP as substrate (PubMed:16990279). kcat is 14 sec(-1) with beta-glucose 6-phosphate as substr

substrate: PNP


organism: Homo sapiens

proof_lines: kcat is 1.52 sec(-1) for the dephosphorylation of pyridoxal 5'-phosphate (at pH 7.4 and 37 degrees Celsius). kcat is 1.25 sec(-1) for the dephosphorylation of pyridoxine 5'-phosphate (at pH 7.4 and 37 degrees Celsius). kcat is 0.45 sec(-1)


organism: Mus musculus

substrate_name: pyridoxal 5'-phosphate

proof_lines: kcat varies between 1.5 and 2.0 sec(-1) for the dephosphorylation of pyridoxal 5'-phosphate (at pH 7.4 and 22 degrees Celsius).

substrate: pyridoxal 5'-phosphate


enzyme_display_name: lacto-N-biosidase

organism: Aquimarina sp. (strain TRL1)

substrate_name: pNP-LNB

proof_lines: kcat is 2.16 sec(-1) with pNP-LNB as substrate (PubMed:39239753). kcat is 3.9 sec(-1) with pNP-LacNAc as substrate (PubMed:39239753).

enzyme: lacto-N-biosidase

substrate: pNP-LNB


organism: Bifidobacterium bifidum (strain DSM 20082 / JCM 1254 / BCRC 11844 / KCTC 3440 / E319f (Variant a))

substrate_name: lacto-N-tetraose

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

proof_lines: kcat is 41.1 sec(-1) with lacto-N-tetraose as substrate (PubMed:23479733). kcat is 89 sec(-1) with chromogenic LNB-beta-pNP (beta-D-Gal-(1->3)-beta-D-GlcNAc-pNP) as substrate (PubMed:18469123).

substrate: lacto-N-tetraose


organism: Bifidobacterium longum subsp. longum (strain ATCC 15707 / DSM 20219 / JCM 1217 / NCTC 11818 / E194b)

proof_lines: kcat is 113 sec(-1) with lacto-N-tetraose (beta-D-Gal-(1->3)-beta-D-GlcNAc-(1->3)-beta-D-Gal-(1->4)-D-Glc) as substrate. kcat is 96.1 sec(-1) with LNB-beta-pNP (beta-D-Gal-(1->3)-beta-D-GlcNAc-pNP) as chromogenic substrate. kcat is 39.4 sec


organism: Paludibaculum fermentans

substrate_name: pNP-LacNAc

verification_status: verified

assay_conditions_summary: pH 6; 318.15 K; buffer pH 6

column_label: Table 6 (Kinetic parameters k cat, K M, K i and k cat/K M of AquiGH20, PadiGH20, PafeGH20, PlbaGH20 and TrdeGH20, determined at their respective optimal conditions of pH and temperature using pNP-LNB and pNP-LacNAc as substrates), enzyme row 'PafeGH20'. pNP-LacNAc column group: column 'k cat' = 17.1, column 'K M' = 1408, column 'K i' = 736, column 'k cat/K M' = 1.30 x 10^4. pNP-LNB column group of the same row: column 'k cat' = en dash, column 'K M' = en dash, column 'k cat/K M' = 6.66 x 10^2.

normalized_value_unit_evidence: kcat: printed Table 6 cell 17.1 s-1; the printed unit is already s^-1, so no conversion is applied and the exported value is 17.1 s^(-1). Km: printed Table 6 cell 1408 uM; 1408 / 1000 = 1.408, so the exported value is 1.408 mM. kcat/Km: printed Table 6 cell 1.30 x 10^4 s-1 M-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 1.30 x 10^4 x 0.001 = 13.0 s^-1 mM^-1; the export row stores no kcat_over_km value, so this converted figure is kept as typed provenance only and no ratio metric is written.

raw_value_unit_evidence: Table 6, enzyme row 'PafeGH20', pNP-LacNAc column group: k cat = 17.1 s-1; K M = 1408 uM; K i = 736 uM; printed k cat/K M = 1.30 x 10^4 s-1 M-1. The pNP-LNB column group of the same row prints an en dash for k cat and for K M and 6.66 x 10^2 s-1 M-1 for k cat/K M.

row_label: Table 6, enzyme row 'PafeGH20', pNP-LacNAc column group (k cat, K M, K i, k cat/K M)

table_label: Table 6: Kinetic parameters k cat (s-1), K M (uM), K i (uM), and k cat/K M (s-1 M-1) of AquiGH20, PadiGH20, PafeGH20, PlbaGH20, and TrdeGH20 (Chembiochem 2025, 26(2), e202400710)

substrate: pNP-LacNAc

status: verified


organism: Parabacteroides distasonis

proof_lines: kcat is 14.6 sec(-1) with pNP-LNB as substrate (PubMed:39239753). kcat is 23.6 sec(-1) with pNP-LacNAc as substrate (PubMed:39239753).


organism: Planctomycetales bacterium (strain ZRK34)

proof_lines: kcat is 4.6 sec(-1) with pNP-LNB as substrate (PubMed:39239753). kcat is 8.9 sec(-1) with pNP-LacNAc as substrate (PubMed:39239753).


organism: Treponema denticola (strain ATCC 35405 / DSM 14222 / CIP 103919 / JCM 8153 / KCTC 15104)

proof_lines: kcat is 0.45 sec(-1) with pNP-LNB as substrate (PubMed:39239753). kcat is 3.3 sec(-1) with pNP-LacNAc as substrate (PubMed:39239753).


enzyme_display_name: glucan 1,3-beta-glucosidase

organism: Streptomyces sp. (strain SirexAA-E / ActE)

substrate_name: L.digitata soluble laminarin (at pH 6 and 40 degrees Celsius)

assay_conditions_summary: pH 6

proof_lines: kcat is 138 sec(-1) with L.digitata soluble laminarin as substrate (at pH 6 and 40 degrees Celsius).

enzyme: glucan 1,3-beta-glucosidase


organism: Bacillus circulans

sequence_variant_note: Resolved canonical sequence from UniProtKB:P43379 and applied mutation signature F259S with inferred residue-numbering offset +27 to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: cyclomaltodextrin glucanotransferase(Enzyme) mutant F259S


organism: Bacillus sp. 1011

substrate_name: rutin

proof_lines:
pH 6, 60°C
ring opening reaction, pH 6, 60°C

substrate: rutin


organism: Bacillus sp. (in: firmicutes)

substrate_name: soluble starch

proof_lines: mutant NS182G, pH 6.0, 60°C, calculated as production of beta-cyclodextrin

substrate: soluble starch


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5U9V9 and applied mutation signature S182E with inferred residue-numbering offset +29 to reconstruct the assayed variant sequence.

proof_lines: mutant S182E, pH 6.0, 60°C, calculated as production of beta-cyclodextrin


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5U9V9 and applied mutation signature N28R with inferred residue-numbering offset +29 to reconstruct the assayed variant sequence.

proof_lines: mutant N28R, pH 6.0, 60°C, calculated as production of beta-cyclodextrin


proof_lines: wild-type, pH 6.0, 60°C, calculated as production of beta-cyclodextrin


organism: Bacillus sp. N-227

substrate_name: soluble corn starch

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q197W1 and applied mutation signature Y127F to reconstruct the assayed variant sequence.

substrate: soluble corn starch


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q197W1 and applied mutation signature D355R to reconstruct the assayed variant sequence.


sequence_source: UniProtKB:Q197W1 direct accession sequence

assay_conditions_summary: pH 6; 333.15 K; buffer pH 6


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q197W1 direct accession sequence plus PMID 28597161 mutation reconstruction and applied mutation signature R254F to reconstruct the assayed variant sequence.


organism: Geobacillus stearothermophilus

km_unit: g liter^-1

kcat_over_km_unit: liters s^-1 g^-1

sequence_source: UniProtKB:P31797 direct accession sequence

assay_conditions_summary: pH 5.5; 323.15 K; buffer 50 mM sodium phosphate


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31797 direct accession sequence plus PMID 33837009 mutation reconstruction using mature-sequence offset +31 and applied mutation signature L277M with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


substrate_name: maltose

sequence_variant_note: Resolved canonical sequence from UniProtKB:P31797 direct accession sequence plus PMID 33837009 mutation reconstruction using mature-sequence offset +31 and applied mutation signature G282A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.

substrate: maltose


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31797 direct accession sequence plus PMID 33837009 mutation reconstruction using mature-sequence offset +31 and applied mutation signature L277F with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31797 direct accession sequence plus PMID 33837009 mutation reconstruction using mature-sequence offset +31 and applied mutation signature L277T with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:P31797 direct accession sequence plus PMID 33837009 mutation reconstruction using mature-sequence offset +31 and applied mutation signature L277F/G282A with inferred residue-numbering offset +31 to reconstruct the assayed variant sequence.


enzyme_display_name: angiotensin-converting enzyme 2

substrate_name: angiotensin I

proof_lines: kcat is 0.034 sec(-1) with angiotensin I as substrate. kcat is 3.5 sec(-1) with angiotensin II as substrate. kcat is 13 sec(-1) with apelin-13 as substrate. kcat is 62 sec(-1) with [des-Arg(9)]-bradykinin as substrate. kcat is 26 sec(-1) wi

enzyme: angiotensin-converting enzyme 2

substrate: angiotensin I


enzyme_display_name: beta-ureidopropionase

substrate_name: N-carbamoyl-beta-alanine

proof_lines: kcat is 0.47 sec(-1) with N-carbamoyl-beta-alanine as substrate.

enzyme: beta-ureidopropionase

substrate: N-carbamoyl-beta-alanine


enzyme_display_name: biuret amidohydrolase

organism: Rhizobium johnstonii (strain DSM 114642 / LMG 32736 / 3841)

substrate_name: biuret

enzyme: biuret amidohydrolase

substrate: biuret


enzyme_display_name: 8-oxo-dGTP diphosphatase

organism: Escherichia coli (strain K12)

proof_lines: kcat is 6.9 sec(-1) with 8-oxo-dGTP as substrate measured by the Fiske-SubbaRow assay. kcat is 5.5 sec(-1) with 8-oxo-dGTP as substrate measured by the Pi sensor assay. kcat is 11.2 sec(-1) with 8-oxo-GTP as substrate.

enzyme: 8-oxo-dGTP diphosphatase


enzyme_display_name: 2-hydroxy-dATP diphosphatase

organism: Danio rerio

substrate_name: 8-oxo-dGTP (at pH 7.5)

proof_lines: kcat is 5.4 sec(-1) with 8-oxo-dGTP as substrate (at pH 7.5) (PubMed:26862114). kcat is 12.0 sec(-1) with 2-oxo-dATP as substrate (at pH 7.5) (PubMed:26862114). kcat is 7.6 sec(-1) with dGTP as substrate (at pH 7.5) (PubMed:26862114). Shows

enzyme: 2-hydroxy-dATP diphosphatase

substrate: 8-oxo-dGTP (at pH 7.5)


organism: Homo sapiens

substrate_name: 2-oxo-dATP (at 30 degrees Celsius and pH 8.0)

assay_conditions_summary: pH 8; cofactor ATP

proof_lines: kcat is 13.9 sec(-1) with 2-oxo-dATP as substrate (at 30 degrees Celsius and pH 8.0) (PubMed:10373420). kcat is 4.7 sec(-1) with 2-oxo-dATP as substrate (at 30 degrees Celsius and pH 7.2) (PubMed:10373420). kcat is 4.7 sec(-1) with 2-oxo-AT


enzyme_display_name: soluble epoxide hydrolase

substrate_name: trans-1,3-diphenylpropene oxide

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature R287Q to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block [3H]t-DPPO, enzyme column R287Q; printed row 'KM (uM)' = 10.1; printed row 'kcat (s^-1)' = 0.076; printed row 'kcat/KM (s^-1 uM^-1)' = 0.008. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.076 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.076 s^(-1). Km: printed Table 1 cell 10.1 in a row headed KM (uM); 1 uM is 1/1000 mM, so 10.1 / 1000 = 0.0101 mM. kcat/Km: printed Table 1 cell 0.008 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.008 x 1000 = 8.0 s^(-1)*mM^(-1). The exported values are kcat 0.076 s^(-1), Km 0.0101 mM and kcat_over_km 7.524752475247525 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block [3H]t-DPPO, enzyme column R287Q: KM = 10.1 uM; kcat = 0.076 s-1; printed kcat/KM = 0.008 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.

table_label: Table 1: Kinetic parameters for WT and four sEH polymorphs (Journal of Lipid Research, Volume 55, 2014). The table prints one substrate block per assayed substrate, each block printing the rows KM, kcat and kcat/KM, and one value column per assayed enzyme form.

enzyme: soluble epoxide hydrolase

substrate: trans-1,3-diphenylpropene oxide


substrate_name: AttoPhos

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature R103C to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block Attophos, enzyme column R103C; printed row 'KM (uM)' = 14; printed row 'kcat (10^-3 s^-1)' = 5.0; printed row 'kcat/KM (10^-3 s^-1 uM^-1)' = 0.36. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.0 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 5.0 x 10^-3 = 0.005 s^(-1). Km: printed Table 1 cell 14 in a row headed KM (uM); 1 uM is 1/1000 mM, so 14 / 1000 = 0.014 mM. kcat/Km: printed Table 1 cell 0.36 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.36 x 10^-3 x 1000 = 0.36 s^(-1)*mM^(-1). The exported values are kcat 0.005 s^(-1), Km 0.014 mM and kcat_over_km 0.35714285714285715 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block Attophos, enzyme column R103C: KM = 14 uM; kcat = 5.0 x 10^-3 s-1; printed kcat/KM = 0.36 x 10^-3 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.

substrate: AttoPhos


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature C154Y to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block Attophos, enzyme column C154Y; printed row 'KM (uM)' = 7.4; printed row 'kcat (10^-3 s^-1)' = 27.0; printed row 'kcat/KM (10^-3 s^-1 uM^-1)' = 3.63. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 27.0 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 27.0 x 10^-3 = 0.027 s^(-1). Km: printed Table 1 cell 7.4 in a row headed KM (uM); 1 uM is 1/1000 mM, so 7.4 / 1000 = 0.0074 mM. kcat/Km: printed Table 1 cell 3.63 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 3.63 x 10^-3 x 1000 = 3.63 s^(-1)*mM^(-1). The exported values are kcat 0.027 s^(-1), Km 0.0074 mM and kcat_over_km 3.6486486486486482 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block Attophos, enzyme column C154Y: KM = 7.4 uM; kcat = 27.0 x 10^-3 s-1; printed kcat/KM = 3.63 x 10^-3 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


substrate_name: 1-myristoyl-sn-glycerol 3-phosphate

sequence_variant_note: Resolved canonical sequence from UniProtKB:P34913 and applied mutation signature R287Q to reconstruct the assayed variant sequence.

proof_lines:
mutant enzyme R287Q, at pH 7.4 and 30°C
mutant enzyme R287Q, at pH 7.4 and 37°C

substrate: 1-myristoyl-sn-glycerol 3-phosphate


column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block [3H]t-DPPO, enzyme column C154Y; printed row 'KM (uM)' = 4.0; printed row 'kcat (s^-1)' = 2.55; printed row 'kcat/KM (s^-1 uM^-1)' = 0.64. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 2.55 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 2.55 s^(-1). Km: printed Table 1 cell 4.0 in a row headed KM (uM); 1 uM is 1/1000 mM, so 4.0 / 1000 = 0.004 mM. kcat/Km: printed Table 1 cell 0.64 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.64 x 1000 = 640.0 s^(-1)*mM^(-1). The exported values are kcat 2.55 s^(-1), Km 0.004 mM and kcat_over_km 637.4999999999999 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block [3H]t-DPPO, enzyme column C154Y: KM = 4.0 uM; kcat = 2.55 s-1; printed kcat/KM = 0.64 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


substrate_name: 14,15-epoxyeicosatrienoic acid

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block 14,15-EET, enzyme column C154Y; printed row 'KM (uM)' = 9.2; printed row 'kcat (s^-1)' = 15.0; printed row 'kcat/KM (s^-1 uM^-1)' = 1.6. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 15.0 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 15.0 s^(-1). Km: printed Table 1 cell 9.2 in a row headed KM (uM); 1 uM is 1/1000 mM, so 9.2 / 1000 = 0.0092 mM. kcat/Km: printed Table 1 cell 1.6 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.6 x 1000 = 1600.0 s^(-1)*mM^(-1). The exported values are kcat 15.0 s^(-1), Km 0.0092 mM and kcat_over_km 1630.4347826086957 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block 14,15-EET, enzyme column C154Y: KM = 9.2 uM; kcat = 15.0 s-1; printed kcat/KM = 1.6 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.

substrate: 14,15-epoxyeicosatrienoic acid


sequence_variant_note: Resolved canonical sequence from UniProtKB:P34913 and applied mutation signature K55R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature K55R to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block [3H]t-DPPO, enzyme column K55R; printed row 'KM (uM)' = 5.8; printed row 'kcat (s^-1)' = 1.72; printed row 'kcat/KM (s^-1 uM^-1)' = 0.30. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.72 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 1.72 s^(-1). Km: printed Table 1 cell 5.8 in a row headed KM (uM); 1 uM is 1/1000 mM, so 5.8 / 1000 = 0.0058 mM. kcat/Km: printed Table 1 cell 0.30 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.30 x 1000 = 300.0 s^(-1)*mM^(-1). The exported values are kcat 1.72 s^(-1), Km 0.0058 mM and kcat_over_km 296.55172413793105 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block [3H]t-DPPO, enzyme column K55R: KM = 5.8 uM; kcat = 1.72 s-1; printed kcat/KM = 0.30 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block 14,15-EET, enzyme column R287Q; printed row 'KM (uM)' = 9; printed row 'kcat (s^-1)' = 0.44; printed row 'kcat/KM (s^-1 uM^-1)' = 0.05. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.44 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.44 s^(-1). Km: printed Table 1 cell 9 in a row headed KM (uM); 1 uM is 1/1000 mM, so 9 / 1000 = 0.009 mM. kcat/Km: printed Table 1 cell 0.05 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.05 x 1000 = 50.0 s^(-1)*mM^(-1). The exported values are kcat 0.44 s^(-1), Km 0.009 mM and kcat_over_km 48.88888888888889 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block 14,15-EET, enzyme column R287Q: KM = 9 uM; kcat = 0.44 s-1; printed kcat/KM = 0.05 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


sequence_source: UniProtKB reviewed accession P34913 direct REST check

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

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block Attophos, enzyme column WT; printed row 'KM (uM)' = 9.7; printed row 'kcat (10^-3 s^-1)' = 13.1; printed row 'kcat/KM (10^-3 s^-1 uM^-1)' = 1.35. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 13.1 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 13.1 x 10^-3 = 0.0131 s^(-1). Km: printed Table 1 cell 9.7 in a row headed KM (uM); 1 uM is 1/1000 mM, so 9.7 / 1000 = 0.0097 mM. kcat/Km: printed Table 1 cell 1.35 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.35 x 10^-3 x 1000 = 1.35 s^(-1)*mM^(-1). The exported values are kcat 0.0131 s^(-1), Km 0.0097 mM and kcat_over_km 1.3505154639175259 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block Attophos, enzyme column WT: KM = 9.7 uM; kcat = 13.1 x 10^-3 s-1; printed kcat/KM = 1.35 x 10^-3 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


proof_lines:
wild type enzyme, at pH 7.4 and 30°C
wild type enzyme, at pH 7.4 and 37°C


organism: Mus musculus

substrate_name: 2-Benzyl-3-phenyloxirane; H2O

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

sequence_source: UniProtKB reviewed accession P34914 direct REST check

source_databases_merged: sabio_rk brenda skid

substrate: 2-Benzyl-3-phenyloxirane; H2O


organism: Mycobacterium tuberculosis

substrate_name: Styrene oxide; H2O

sequence_source: UniProtKB reviewed accession O33283 direct REST check

substrate: Styrene oxide; H2O


organism: Rattus norvegicus

substrate_name: trans-Stilbene oxide

sequence_source: UniProtKB reviewed accession P80299 direct REST check

substrate: trans-Stilbene oxide


substrate_name: H2O; trans-Stilbene oxide

sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P80299 plus direct W540L reconstruction from canonical residue W540 and applied mutation signature W540L to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant fusion protein W540L

substrate: H2O; trans-Stilbene oxide


sequence_variant_note: Resolved canonical sequence from UniProtKB reviewed accession P80299 plus direct H332Q reconstruction from canonical residue H332 and applied mutation signature H332Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant fusion protein H332Q


organism: Arabidopsis thaliana

sequence_source: UniProtKB:Q42566 canonical sequence retrieved 2026-06-04


organism: Aspergillus niger

substrate_name: H2O; p-Nitrostyrene oxide

sequence_source: UniProtKB:Q9UR30 canonical sequence retrieved 2026-06-04

substrate: H2O; p-Nitrostyrene oxide


substrate_name: p-Nitrostyrene oxide; H2O

sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q9UR30 canonical sequence retrieved 2026-06-04 and applied mutation signature D348E to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant D348E

substrate: p-Nitrostyrene oxide; H2O


organism: Caenorhabditis elegans

sequence_source: UniProtKB:G5EBI4 canonical sequence retrieved 2026-06-04

assay_conditions_summary: pH 7.4; 303.15 K; buffer this paper: sodium phosphate

column_label: Table 3: Km and Kcat with t-DPPO and EpOMEs (Arch Biochem Biophys 2008, 472(2):139-149) prints, for each of its three Name blocks (t-DPPO, 9,10-EpOME, 12,13-EpOME), the kinetic-parameter rows Km (uM), kcat (s^-1) and kcat/Km(uM^-1*s^-1) under three construct columns, Recombinant CEEH1, Recombinant CEEH2 and Recombinant human. The cited cell set is the t-DPPO block, Recombinant CEEH1 column: Km (uM) = 160; kcat (s^-1) = 12; kcat/Km(uM^-1*s^-1) = 0.07.

normalized_value_unit_evidence: kcat: printed Table 3 cell 12 under the Recombinant CEEH1 column; the column is already per second, so no conversion applies and the paper value is 12.0 s^(-1). Km: printed Table 3 cell 160 under the Recombinant CEEH1 column; 1 uM is 1/1000 mM, so 160 / 1000 = 0.16 mM. kcat/Km: printed Table 3 cell 0.07 uM^-1 s^-1 under the Recombinant CEEH1 column; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.07 x 1000 = 70.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, t-DPPO block, Recombinant CEEH1 column: Km = 160 uM; kcat = 12 s^-1; printed kcat/Km = 0.07 uM^-1 s^-1.


column_label: Table 3: Km and Kcat with t-DPPO and EpOMEs (Arch Biochem Biophys 2008, 472(2):139-149) prints, for each of its three Name blocks (t-DPPO, 9,10-EpOME, 12,13-EpOME), the kinetic-parameter rows Km (uM), kcat (s^-1) and kcat/Km(uM^-1*s^-1) under three construct columns, Recombinant CEEH1, Recombinant CEEH2 and Recombinant human. The cited cell set is the 12,13-EpOME block, Recombinant CEEH1 column: Km (uM) = 11.4; kcat (s^-1) = 0.11; kcat/Km(uM^-1*s^-1) = 0.0096.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.11 under the Recombinant CEEH1 column; the column is already per second, so no conversion applies and the paper value is 0.11 s^(-1). Km: printed Table 3 cell 11.4 under the Recombinant CEEH1 column; 1 uM is 1/1000 mM, so 11.4 / 1000 = 0.0114 mM. kcat/Km: printed Table 3 cell 0.0096 uM^-1 s^-1 under the Recombinant CEEH1 column; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.0096 x 1000 = 9.6 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, 12,13-EpOME block, Recombinant CEEH1 column: Km = 11.4 uM; kcat = 0.11 s^-1; printed kcat/Km = 0.0096 uM^-1 s^-1.


sequence_source: UniProtKB:G5EDL5 canonical sequence retrieved 2026-06-04


column_label: Table 3: Km and Kcat with t-DPPO and EpOMEs (Arch Biochem Biophys 2008, 472(2):139-149) prints, for each of its three Name blocks (t-DPPO, 9,10-EpOME, 12,13-EpOME), the kinetic-parameter rows Km (uM), kcat (s^-1) and kcat/Km(uM^-1*s^-1) under three construct columns, Recombinant CEEH1, Recombinant CEEH2 and Recombinant human. The cited cell set is the 9,10-EpOME block, Recombinant CEEH2 column: Km (uM) = 8.4; kcat (s^-1) = 0.01; kcat/Km(uM^-1*s^-1) = 0.0012.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.01 under the Recombinant CEEH2 column; the column is already per second, so no conversion applies and the paper value is 0.01 s^(-1). Km: printed Table 3 cell 8.4 under the Recombinant CEEH2 column; 1 uM is 1/1000 mM, so 8.4 / 1000 = 0.0084 mM. kcat/Km: printed Table 3 cell 0.0012 uM^-1 s^-1 under the Recombinant CEEH2 column; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.0012 x 1000 = 1.2 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, 9,10-EpOME block, Recombinant CEEH2 column: Km = 8.4 uM; kcat = 0.01 s^-1; printed kcat/Km = 0.0012 uM^-1 s^-1.


sequence_source: UniProtKB direct accession lookup G5EBI4 on 2026-06-04

column_label: Table 3: Km and Kcat with t-DPPO and EpOMEs (Arch Biochem Biophys 2008, 472(2):139-149) prints, for each of its three Name blocks (t-DPPO, 9,10-EpOME, 12,13-EpOME), the kinetic-parameter rows Km (uM), kcat (s^-1) and kcat/Km(uM^-1*s^-1) under three construct columns, Recombinant CEEH1, Recombinant CEEH2 and Recombinant human. The cited cell set is the 9,10-EpOME block, Recombinant CEEH1 column: Km (uM) = 7.5; kcat (s^-1) = 0.22; kcat/Km(uM^-1*s^-1) = 0.029.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.22 under the Recombinant CEEH1 column; the column is already per second, so no conversion applies and the paper value is 0.22 s^(-1). Km: printed Table 3 cell 7.5 under the Recombinant CEEH1 column; 1 uM is 1/1000 mM, so 7.5 / 1000 = 0.0075 mM. kcat/Km: printed Table 3 cell 0.029 uM^-1 s^-1 under the Recombinant CEEH1 column; 1 uM^-1 s^-1 is 1000 s^-1 mM^-1, so 0.029 x 1000 = 29.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, 9,10-EpOME block, Recombinant CEEH1 column: Km = 7.5 uM; kcat = 0.22 s^-1; printed kcat/Km = 0.029 uM^-1 s^-1.


sequence_source: UniProtKB direct accession lookup G5EDL5 on 2026-06-04


substrate_name: (S)-styrene oxide

sequence_source: UniProtKB direct accession lookup Q5PRC6 on 2026-06-04; mutation coordinate check performed against the returned canonical sequence

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

proof_lines: mutant enzyme E88R/T102A/M368I/K398E/G412D, at pH 6.0 and 10°C

substrate: (S)-styrene oxide


substrate_name: (R)-styrene oxide

sequence_source: UniProtKB direct accession lookup Q5PRC6 on 2026-06-04

substrate: (R)-styrene oxide


organism: Gallus gallus

sequence_source: UniProtKB direct accession lookup Q45QT1 on 2026-06-04

proof_lines: pH 7.4, 30°C, purified recombinant enzyme


organism: Glycine max

substrate_name: H2O; 9,10-Epoxystearic acid

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup O49857 on 2026-06-04; Y255F reconstructed from the returned canonical sequence and applied mutation signature Y255F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant Y255F

substrate: H2O; 9,10-Epoxystearic acid


substrate_name: 9,10-Epoxystearic acid; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB direct accession lookup O49857 on 2026-06-04; Y175S reconstructed from the returned canonical sequence and applied mutation signature Y175S to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant Y175S

substrate: 9,10-Epoxystearic acid; H2O


sequence_source: UniProtKB direct accession lookup O49857 on 2026-06-04

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


sequence_source: UniProtKB:P80299 direct accession lookup


substrate_name: trans-Stilbene oxide; H2O

sequence_variant_note: Resolved canonical sequence from UniProtKB:P80299 direct accession lookup plus W334F reconstruction and applied mutation signature W334F to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant fusion protein W334F

substrate: trans-Stilbene oxide; H2O


organism: Solanum tuberosum

sequence_source: UniProtKB:Q41413 direct accession lookup


organism: Strongylocentrotus purpuratus

sequence_source: UniProtKB:B2MWN2 direct accession lookup


organism: Trichoderma reesei

sequence_source: UniProtKB:G0R7E2 direct accession lookup


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

proof_lines:
pH 7.0, 37°C
Raw SKiD Env: Temp=37°C, pH=7

source_databases_merged: brenda skid


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check for O49857 on 2026-06-04; variant reconstructed from selected SABIO-RK Y255H note. and applied mutation signature Y255H to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: soluble epoxide hydrolase(Enzyme) mutant Y255H


sequence_source: UniProt REST direct accession check for P07099 on 2026-06-04.


sequence_source: UniProt REST direct accession check for P34913 on 2026-06-04.

assay_conditions_summary: pH 7.4; 310.15 K; buffer sodium phosphate

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

proof_lines: pH 7, temperature not specified in the publication


sequence_source: UniProt REST direct accession check for Q9H6B9 on 2026-06-04.


substrate_name: Epoxy Fluor 7

sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check for P34913 on 2026-06-04; variant reconstructed from selected BRENDA R287E note. and applied mutation signature R287E to reconstruct the assayed variant sequence.

substrate: Epoxy Fluor 7


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check for P34913 on 2026-06-04; variant reconstructed from selected BRENDA E254R note. and applied mutation signature E254R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check for P34913 on 2026-06-04; variant reconstructed from selected BRENDA E254R/R287E note. and applied mutation signature E254R/R287E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E254R/R287E, at pH 7.4 and 37°C


sequence_variant_note: Resolved canonical sequence from UniProt REST direct accession check for P34913 on 2026-06-04; variant reconstructed from selected OED R103C note. and applied mutation signature R103C to reconstruct the assayed variant sequence.


sequence_source: UniProtKB reviewed accession P34913 FASTA and JSON fetched via UniProt REST on 2026-06-04; PMID 24771868 / PMCID PMC4031944 checked for human soluble epoxide hydrolase SNP and substrate context.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block 14,15-EET, enzyme column WT; printed row 'KM (uM)' = 7; printed row 'kcat (s^-1)' = 5.0; printed row 'kcat/KM (s^-1 uM^-1)' = 0.71. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.0 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 5.0 s^(-1). Km: printed Table 1 cell 7 in a row headed KM (uM); 1 uM is 1/1000 mM, so 7 / 1000 = 0.007 mM. kcat/Km: printed Table 1 cell 0.71 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.71 x 1000 = 710.0 s^(-1)*mM^(-1). The exported values are kcat 5.0 s^(-1), Km 0.007 mM and kcat_over_km 714.2857142857142 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block 14,15-EET, enzyme column WT: KM = 7 uM; kcat = 5.0 s-1; printed kcat/KM = 0.71 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature R103C to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat: printed Table 1 cell 5.0 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 5.0 x 10^-3 = 0.005 s^(-1). Km: printed Table 1 cell 14 in a row headed KM (uM); 1 uM is 1/1000 mM, so 14 / 1000 = 0.014 mM. kcat/Km: printed Table 1 cell 0.36 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.36 x 10^-3 x 1000 = 0.36 s^(-1)*mM^(-1). The exported values are kcat 2.1 s^(-1), Km 0.0059 mM; this export row carries no kcat_over_km field.

row_label: Table 1, substrate block Attophos, enzyme column R103C


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature C154Y to reconstruct the assayed variant sequence.

normalized_value_unit_evidence: kcat: printed Table 1 cell 15.0 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 15.0 s^(-1). Km: printed Table 1 cell 9.2 in a row headed KM (uM); 1 uM is 1/1000 mM, so 9.2 / 1000 = 0.0092 mM. kcat/Km: printed Table 1 cell 1.6 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.6 x 1000 = 1600.0 s^(-1)*mM^(-1). The exported values are kcat 15.0 s^(-1), Km 0.004 mM; this export row carries no kcat_over_km field.

row_label: Table 1, substrate block 14,15-EET, enzyme column C154Y


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature R287Q to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block Attophos, enzyme column R287Q; printed row 'KM (uM)' = 17; printed row 'kcat (10^-3 s^-1)' = 1.0; printed row 'kcat/KM (10^-3 s^-1 uM^-1)' = 0.06. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.0 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 1.0 x 10^-3 = 0.001 s^(-1). Km: printed Table 1 cell 17 in a row headed KM (uM); 1 uM is 1/1000 mM, so 17 / 1000 = 0.017 mM. kcat/Km: printed Table 1 cell 0.06 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.06 x 10^-3 x 1000 = 0.06 s^(-1)*mM^(-1). The exported values are kcat 0.001 s^(-1), Km 0.017 mM and kcat_over_km 0.058823529411764705 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block Attophos, enzyme column R287Q: KM = 17 uM; kcat = 1.0 x 10^-3 s-1; printed kcat/KM = 0.06 x 10^-3 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block [3H]t-DPPO, enzyme column R103C; printed row 'KM (uM)' = 5.9; printed row 'kcat (s^-1)' = 0.76; printed row 'kcat/KM (s^-1 uM^-1)' = 0.13. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.76 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.76 s^(-1). Km: printed Table 1 cell 5.9 in a row headed KM (uM); 1 uM is 1/1000 mM, so 5.9 / 1000 = 0.0059 mM. kcat/Km: printed Table 1 cell 0.13 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.13 x 1000 = 130.0 s^(-1)*mM^(-1). The exported values are kcat 0.76 s^(-1), Km 0.0059 mM and kcat_over_km 128.8135593220339 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block [3H]t-DPPO, enzyme column R103C: KM = 5.9 uM; kcat = 0.76 s-1; printed kcat/KM = 0.13 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P34913 and applied mutation signature K55R to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block 14,15-EET, enzyme column K55R; printed row 'KM (uM)' = 7.4; printed row 'kcat (s^-1)' = 7.5; printed row 'kcat/KM (s^-1 uM^-1)' = 1.0. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.5 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 7.5 s^(-1). Km: printed Table 1 cell 7.4 in a row headed KM (uM); 1 uM is 1/1000 mM, so 7.4 / 1000 = 0.0074 mM. kcat/Km: printed Table 1 cell 1.0 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 1.0 x 1000 = 1000.0 s^(-1)*mM^(-1). The exported values are kcat 7.5 s^(-1), Km 0.0074 mM and kcat_over_km 1013.5135135135134 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block 14,15-EET, enzyme column K55R: KM = 7.4 uM; kcat = 7.5 s-1; printed kcat/KM = 1.0 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block Attophos, enzyme column K55R; printed row 'KM (uM)' = 7.4; printed row 'kcat (10^-3 s^-1)' = 18.2; printed row 'kcat/KM (10^-3 s^-1 uM^-1)' = 2.5. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 18.2 in a row headed kcat (10^-3 s^-1); the printed row head carries the multiplier 10^-3, so 18.2 x 10^-3 = 0.0182 s^(-1). Km: printed Table 1 cell 7.4 in a row headed KM (uM); 1 uM is 1/1000 mM, so 7.4 / 1000 = 0.0074 mM. kcat/Km: printed Table 1 cell 2.5 in a row headed kcat/KM (10^-3 s^-1 uM^-1); the printed row head carries the multiplier 10^-3 and 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 2.5 x 10^-3 x 1000 = 2.5 s^(-1)*mM^(-1). The exported values are kcat 0.0182 s^(-1), Km 0.0074 mM and kcat_over_km 2.4594594594594597 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block Attophos, enzyme column K55R: KM = 7.4 uM; kcat = 18.2 x 10^-3 s-1; printed kcat/KM = 2.5 x 10^-3 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


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

column_label: Table 1 (Kinetic parameters for WT and four sEH polymorphs), substrate block [3H]t-DPPO, enzyme column WT; printed row 'KM (uM)' = 3.3; printed row 'kcat (s^-1)' = 0.99; printed row 'kcat/KM (s^-1 uM^-1)' = 0.30. Each of these three cells prints its own SD after the value, and Table 1 states that results are the average and SD of three replicates.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.99 in a row headed kcat (s^-1); s^-1 is already the canonical s^(-1), so no unit conversion applies and the value is 0.99 s^(-1). Km: printed Table 1 cell 3.3 in a row headed KM (uM); 1 uM is 1/1000 mM, so 3.3 / 1000 = 0.0033 mM. kcat/Km: printed Table 1 cell 0.30 in a row headed kcat/KM (s^-1 uM^-1); 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.30 x 1000 = 300.0 s^(-1)*mM^(-1). The exported values are kcat 0.99 s^(-1), Km 0.0033 mM and kcat_over_km 300.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate block [3H]t-DPPO, enzyme column WT: KM = 3.3 uM; kcat = 0.99 s-1; printed kcat/KM = 0.30 s-1 uM-1. The number printed beside each of these three cells is that cell's own printed SD and is not a kinetic metric the export schema carries.


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

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


substrate_name: p-nitrophenyl phosphate

substrate: p-nitrophenyl phosphate


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: Leu-p-nitroanilide

substrate: Leu-p-nitroanilide


enzyme_display_name: nitrile hydratase

organism: Rhodococcus erythropolis

substrate_name: methacrylonitrile (at pH 7.5)

smiles: CC(=C)C#N

proof_lines: Measured for the whole complex (PubMed:16636455, PubMed:20221653). kcat is 55000 min(-1) with methacrylonitrile as substrate (at pH 7.5) (PubMed:16636455). kcat is 96000 min(-1) with methacrylonitrile as substrate (at pH 7.5 and 20 degrees

enzyme: nitrile hydratase

substrate: methacrylonitrile (at pH 7.5)


enzyme_display_name: tyrosine 3-monooxygenase

organism: Bombyx mori

substrate_name: L-tyrosine

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

enzyme: tyrosine 3-monooxygenase

substrate: L-tyrosine


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


organism: Bos taurus

substrate_name: tyrosine

proof_lines:
bovine adrenal gland
bovine adrenal
versus tetrahydrobiopterin

substrate: tyrosine


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


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

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

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

enzyme: adenosylmethionine decarboxylase

substrate: S-adenosyl-L-methionine


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


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.


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


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


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.

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


substrate_name: PHOME

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

substrate: PHOME


substrate_name: 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).

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

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


organism: Escherichia coli

substrate_name: dTMP; ATP

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

assay_conditions_summary: cofactor ATP

substrate: dTMP; ATP


substrate_name: Thiamine monophosphate; ATP

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

substrate: Thiamine monophosphate; ATP


substrate_name: dUMP

substrate: dUMP


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)


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


organism: Homo sapiens

substrate_name: AZTMP; dTMP

substrate: AZTMP; dTMP


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

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

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.


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


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.


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.


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


organism: Vaccinia virus


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

assay_conditions_summary: cofactor CoA

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


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

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 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


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: 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