sequence_variant_note: Resolved canonical sequence from UniProtKB G2LET6 canonical sequence; RCSB 6O6M/PMID 32257583 links EgtB Cth to G2LET6 and applied mutation signature A420Y to reconstruct the assayed variant sequence.

proof_lines: mutant A420Y, pH not specified in the publication, temperature not specified in the publication


enzyme_display_name: hercynylcysteine S-oxide synthase

organism: Chloracidobacterium thermophilum

substrate_name: hercynine

source_db: brenda

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_source: UniProtKB G2LET6 canonical sequence; RCSB 6O6M/PMID 32257583 links EgtB Cth to G2LET6

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

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

enzyme: hercynylcysteine S-oxide synthase

substrate: hercynine

source: brenda


organism: Methylobacterium brachiatum

substrate_name: L-cysteine

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

substrate: L-cysteine


enzyme_display_name: gamma-glutamyltransferase

organism: Allium cepa

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

enzyme: gamma-glutamyltransferase


organism: Ascaris suum


organism: Aspergillus nidulans

proof_lines: pH 8.0, 37°C, native extracellular enzyme


organism: Bacillus amyloliquefaciens

proof_lines: recombinant extracellular enzyme, pH 9.0, 40°C


organism: Bacillus licheniformis

mutation_type: substitution


enzyme_display_name: amine N-methyltransferase

organism: Homo sapiens

substrate_name: S-Adenosyl-L-methionine; Tryptamine

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

sequence_source: UniProtKB reviewed entry O95050/INMT_HUMAN; EC 2.1.1.49; canonical sequence length 263. Direct UniProtKB REST lookup on 2026-06-18.

enzyme: amine N-methyltransferase

substrate: S-Adenosyl-L-methionine; Tryptamine


organism: Oryctolagus cuniculus

substrate_name: Aniline

source_db: oed

verification_status: unverified

kcat_over_km_origin: calculated

sequence_source: UniProtKB reviewed entry O97972/INMT_RABIT; EC 2.1.1.49; canonical sequence length 263. Direct UniProtKB REST lookup on 2026-06-18.

data_origin: experimental

substrate: Aniline

status: unverified

source: oed


substrate_name: S-Adenosyl-L-methionine

substrate: S-Adenosyl-L-methionine


substrate_name: Desipramine

substrate: Desipramine


substrate_name: Tryptamine

substrate: Tryptamine


substrate_name: pyrazole

substrate: pyrazole


substrate_name: Tryptamine; S-Adenosyl-L-methionine

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

substrate: Tryptamine; S-Adenosyl-L-methionine


substrate_name: Imidazole

substrate: Imidazole


enzyme_display_name: phosphoserine phosphatase

organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed entry O82796/SERC_ARATH; EC 3.1.3.3; canonical sequence length 295. Direct UniProtKB REST lookup on 2026-06-18.

enzyme: phosphoserine phosphatase


organism: Entamoeba histolytica

substrate_name: O-phospho-L-serine

sequence_source: UniProtKB unreviewed entry C4M5P9/C4M5P9_ENTH1 direct lookup on 2026-06-18; EC annotation absent, so sequence is not accepted as an EC-resolved enzyme record.

substrate: O-phospho-L-serine


organism: Escherichia coli

substrate_name: H2O; O-Phospho-L-serine

km_display: Not reported

sequence_source: UniProtKB reviewed entry P0AGB0/SERB_ECOLI; EC 3.1.3.3; canonical sequence length 322. Direct UniProtKB REST lookup on 2026-06-18.

substrate: H2O; O-Phospho-L-serine


organism: Hydrogenobacter thermophilus

substrate_name: L-phosphoserine

sequence_source: UniProtKB reviewed entry D3DFP8/PSPB_HYDTT; EC 3.1.3.3; canonical sequence length 203. Direct UniProtKB REST lookup on 2026-06-18.

substrate: L-phosphoserine


sequence_source: UniProtKB reviewed entry D3DFG8/PSPA_HYDTT; EC 3.1.3.3; canonical sequence length 211. Direct UniProtKB REST lookup on 2026-06-18.


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

proof_lines:
pH 8.0, 22°C, mutant delI211
pH 8.0, 22°C, mutant delVal2-I211


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB reviewed entry D3DFG8/PSPA_HYDTT after direct lookup on 2026-06-18 confirmed canonical residue 85 is H. and applied mutation signature H85A to reconstruct the assayed variant sequence.


enzyme_display_name: butyrate--acetoacetate CoA-transferase

organism: Clostridium acetobutylicum (strain ATCC 824 / DSM 792 / JCM 1419 / IAM 19013 / LMG 5710 / NBRC 13948 / NRRL B-527 / VKM B-1787 / 2291 / W)

substrate_name: acetate

source_db: uniprot

assay_conditions_summary: cofactor CoA

enzyme: butyrate--acetoacetate CoA-transferase

substrate: acetate

source: uniprot


substrate_name: 3-phosphoserine (at 30 degrees Celsius and pH 7.5)


organism: Bacillus subtilis (strain 168)

substrate_name: D-xylulose 5-phosphate (at pH 7 and 37 degrees Celsius)

assay_conditions_summary: pH 7


organism: Escherichia coli (strain K12)

substrate_name: P-Ser (with magnesium ions as cofactor and at pH 9)

assay_conditions_summary: pH 9


organism: Hydrogenobacter thermophilus (strain DSM 6534 / IAM 12695 / TK-6)


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

substrate_name: O-phospho-L-serine (at 70 degrees Celsius and at pH 7.5)


organism: Wolinella succinogenes (strain ATCC 29543 / DSM 1740 / CCUG 13145 / JCM 31913 / LMG 7466 / NCTC 11488 / FDC 602W)

substrate_name: phosphoserine

substrate: phosphoserine


substrate_name: Unknown

proof_lines: Measured in a reaction mixture containing 1 mM EDTA and no magnesium.

substrate: Unknown


proof_lines: The stereochemistry of phosphoserine and phosphothreonine is not specified in the article. kcat is 6.9 sec(-1) with phosphoserine as substrate. kcat is 9.5 sec(-1) with phosphothreonine as substrate. kcat is 7.9 sec(-1) with phosphoethanola


proof_lines: Values are given for the homodimeric form of the protein.


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)


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

proof_lines: kcat is 13.4 min(-1) with O-phospho-L-serine as substrate.


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

substrate_name: O-phospho-L-serine (at pH 7.0 and 70 degrees Celsius)

proof_lines: kcat is 1506 sec(-1) (at pH 7.0 and 70 degrees Celsius) for the dephosphorylation of O-phospho-L-serine.


organism: Staphylococcus aureus (strain NCTC 8325 / PS 47)

proof_lines: kcat is 107 sec(-1) with Ap4A as substrate. kcat is 32 sec(-1) with Ap5A as substrate. kcat is 210 sec(-1) with Ap4G as substrate. kcat is 324 sec(-1) with Ap4U as substrate. kcat is 1002 sec(-1) with Gp4G as substrate.


sequence_source: UniProtKB:D3DFG8 REST lookup


organism: Mycobacterium marinum

sequence_source: UniProtKB:B2HHH0 REST lookup


organism: Mycobacterium tuberculosis

sequence_source: UniProtKB:O53289 REST lookup


proof_lines: at pH 7.0, temperature not specified in the publication


enzyme_display_name: calcidiol 1-monooxygenase

organism: Unknown

enzyme: calcidiol 1-monooxygenase


enzyme_display_name: cholesterol-5,6-oxide hydrolase

organism: Homo sapiens

substrate_name: 5,6alpha-epoxy-5alpha-cholestan-3beta-ol (in the AEBS complex assay)

enzyme: cholesterol-5,6-oxide hydrolase


substrate: 5,6alpha-epoxy-5alpha-cholestan-3beta-ol (in the AEBS complex assay)


enzyme_display_name: AMP deaminase

organism: Arabidopsis thaliana

substrate_name: AMP (in the absence of ATP)

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

assay_conditions_summary: cofactor ATP

enzyme: AMP deaminase

substrate: AMP (in the absence of ATP)


organism: Dictyostelium discoideum

substrate_name: AMP

substrate: AMP


enzyme_display_name: L-threonine kinase

organism: Salmonella enterica

substrate_name: ATP

sequence_variant_note: Resolved canonical sequence from exact_accession_lookup_uniprot and applied mutation signature D103N to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; cofactor ATP

proof_lines: mutant D103N, pH 7.4, temperature not specified in the publication

enzyme: L-threonine kinase

substrate: ATP


enzyme_display_name: butyrate kinase

organism: Desulfovibrio vulgaris

substrate_name: valerate

smiles: CCCCC(=O)O

enzyme: butyrate kinase

substrate: valerate


assay_conditions_summary: pH 7.5; 355.15 K; cofactor ATP


substrate_name: propionate

substrate: propionate


substrate_name: Isovalerate

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

substrate: Isovalerate


substrate_name: Butanoate

smiles: CCCC(=O)O

substrate: Butanoate


substrate_name: Isobutyrate

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

substrate: Isobutyrate


organism: Nitratidesulfovibrio vulgaris

assay_conditions_summary: pH 7.5; cofactor ATP

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


enzyme_display_name: bile-salt sulfotransferase

substrate_name: lithocholic acid

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

assay_conditions_summary: pH 7.4; 310.15 K; buffer 50 mM Tris/HCl

proof_lines: isoform SULT2A1, in 50 mM Tris/HCl buffer, pH 7.4, 1 mM dithiothreitol, 5 mM MgCl2, and 1 mg/ml bovine serum albumin, at 37°C

source_databases_merged: brenda skid

enzyme: bile-salt sulfotransferase

substrate: lithocholic acid


organism: Mus musculus

substrate_name: cholic acid

substrate: cholic acid


proof_lines: pH 6.3, 37°C, recombinant wild-type enzyme


source_db: skid

source_license: CC BY-NC-ND 4.0

source: skid


organism: Amycolatopsis orientalis

ki_unit: mM


organism: Aspergillus oryzae

substrate_name: colloidal chitosan

substrate: colloidal chitosan


substrate_name: H2O; AMP

sequence_source: UniProtKB reviewed accession Q01433 (AMPD2_HUMAN), direct exact-accession lookup

substrate: H2O; AMP


sequence_source: Canonical context only: UniProtKB reviewed accession Q01432 (AMPD3_HUMAN), direct exact-accession lookup

mutation_type: deletion

proof_lines: SABIO-RK modifier species: AMP deaminase(Enzyme) mutant AMPD3 deltaM90


substrate_name: AMP; H2O

sequence_source: UniProtKB reviewed accession Q01432 (AMPD3_HUMAN), direct exact-accession lookup

substrate: AMP; H2O


sequence_source: Canonical context only: UniProtKB reviewed accession P23109 (AMPD1_HUMAN), direct exact-accession lookup

proof_lines: SABIO-RK modifier species: AMP deaminase(Enzyme) mutant AMPD1 deltaL96


sequence_source: UniProtKB reviewed accession P23109 (AMPD1_HUMAN), direct exact-accession lookup


substrate_name: O2; Calcidiol; NADPH; H+

assay_conditions_summary: cofactor NADPH

substrate: O2; Calcidiol; NADPH; H+


organism: Rattus norvegicus

substrate_name: Calcidiol; H+; NADPH; O2

substrate: Calcidiol; H+; NADPH; O2


substrate_name: ATP; L-Threonine

proof_lines: Michaelis-Menten kinetics, pH 7.4, temperature not specified in the publication

proof_lines: calculated from double-reciprocal plots, pH 7.4, temperature not specified in the publication

substrate: ATP; L-Threonine


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_check and applied mutation signature S253A to reconstruct the assayed variant sequence.

proof_lines: mutant S253A, pH 7.4, temperature not specified in the publication


substrate_name: L-threonine

sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_check and applied mutation signature S255A to reconstruct the assayed variant sequence.

proof_lines: mutant S255A, pH 7.4, temperature not specified in the publication

substrate: L-threonine


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_check and applied mutation signature D135N to reconstruct the assayed variant sequence.

proof_lines: mutant D135N, pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_check and applied mutation signature S99A to reconstruct the assayed variant sequence.

proof_lines: mutant S99A, pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_check and applied mutation signature T134A to reconstruct the assayed variant sequence.

proof_lines: mutant T134A, pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_check and applied mutation signature E132Q to reconstruct the assayed variant sequence.

proof_lines: mutant E132Q, pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_check and applied mutation signature E132A to reconstruct the assayed variant sequence.

proof_lines: mutant E132A, pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_check and applied mutation signature D103A to reconstruct the assayed variant sequence.

proof_lines: mutant D103A, pH 7.4, temperature not specified in the publication


proof_lines: wild-type, pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_check and applied mutation signature E24Q to reconstruct the assayed variant sequence.

proof_lines: mutant E24Q, pH 7.4, temperature not specified in the publication


sequence_variant_note: Resolved canonical sequence from direct_uniprot_accession_check and applied mutation signature T101A to reconstruct the assayed variant sequence.

proof_lines: mutant T101A, pH 7.4, temperature not specified in the publication


substrate_name: taurolithocholate

substrate: taurolithocholate


organism: Photobacterium profundum

substrate_name: alpha-D-glucosaminyl fluoride

sequence_variant_note: Resolved canonical sequence from UniProt Q6LUT2 canonical sequence with D139E reconstruction and applied mutation signature D139E to reconstruct the assayed variant sequence.

substrate: alpha-D-glucosaminyl fluoride


substrate_name: chitobiose

sequence_source: UniProt Q6LUT2 canonical sequence

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

substrate: chitobiose


sequence_source: UniProt Q6LUT2 canonical sequence with D139E reconstruction


sequence_variant_note: Resolved canonical sequence from UniProt Q6LUT2 canonical sequence with D139S reconstruction and applied mutation signature D139S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt Q6LUT2 canonical sequence with D139A reconstruction and applied mutation signature D139A to reconstruct the assayed variant sequence.


sequence_source: UniProt Q6LUT2 canonical sequence with D139S reconstruction


sequence_source: UniProt Q6LUT2 canonical sequence with D139A reconstruction


organism: Thermococcus kodakarensis

substrate_name: chitotriose

sequence_source: UniProt Q76HN4 canonical sequence

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

proof_lines:
pH 6.0, 80°C
Raw SKiD Env: Temp=80°C, pH=6

substrate: chitotriose


substrate_name: H2O; Cholesterol-5alpha,6alpha-epoxide

sequence_source: UniProt O33283 canonical sequence

substrate: H2O; Cholesterol-5alpha,6alpha-epoxide


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

proof_lines: SABIO-RK modifier species: AMP deaminase(Enzyme) mutant deltaL31M


proof_lines: SABIO-RK modifier species: AMP deaminase(Enzyme) mutant deltaI139M


sequence_source: UniProt Q54DD0 canonical sequence


organism: Cavia porcellus

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


organism: Gallus gallus

substrate_name: Calcidiol; O2; NADPH; H+

substrate: Calcidiol; O2; NADPH; H+


sequence_source: Direct UniProt lookup found reviewed O15528 for EC 1.14.15.18 and Homo sapiens; sequence not installed because accepted status is blocked by missing kinetic evidence.


substrate_name: 25-hydroxyvitamin D

sequence_source: Direct UniProt lookup found reviewed O35084 for EC 1.14.15.18 and Mus musculus; residue check showed canonical S at position 408, but variant sequence was not installed because accepted status is blocked by missing kinetic evidence.

substrate: 25-hydroxyvitamin D


substrate_name: 1alpha-hydroxyvitamin D

sequence_source: Direct UniProt lookup found reviewed O35084 for EC 1.14.15.18 and Mus musculus; sequence not installed because accepted status is blocked by missing kinetic evidence.

proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme

substrate: 1alpha-hydroxyvitamin D


substrate_name: 25-hydroxyvitamin D2

sequence_source: Direct UniProt lookup found reviewed O35084 for EC 1.14.15.18 and Mus musculus; sequence not installed because accepted status is blocked by missing top-level kinetic evidence in the selected payload.

proof_lines: pH 7.4, 37°C, Michaelis-Menten kinetic parameters

proof_lines: pH 7.4, 37°C, parameters using a kinetic model with substrate binding at two inhibitory sites

substrate: 25-hydroxyvitamin D2


organism: Sus scrofa


organism: Oryctolagus cuniculus

substrate_name: pyrazole

sequence_source: Direct UniProt lookup found reviewed O97972 for EC 2.1.1.49 and Oryctolagus cuniculus, but it was not promoted because the selected PMID/source context separates transferase A/B and lacks a source accession.

proof_lines:
transferase B, pH 7.6
transferase A, pH 8.5
transferase B, pH 8.5

substrate: pyrazole


enzyme_display_name: L-ornithine N(5)-monooxygenase (NADPH)

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

substrate_name: L-ornithine

enzyme: L-ornithine N(5)-monooxygenase (NADPH)

substrate: L-ornithine


enzyme_display_name: fructan beta-fructosidase

organism: Aspergillus awamori

substrate_name: inulin (from Merck)

enzyme: fructan beta-fructosidase

substrate: inulin (from Merck)


organism: Aspergillus ficuum

substrate_name: inulin

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

substrate: inulin


organism: Bacillus subtilis (strain 168)

substrate_name: levan (at pH 5.5 and 55 degrees Celsius)


organism: Homo sapiens

assay_conditions_summary: pH 6.8; 310.15 K; buffer 50 mM Mops


organism: Clostridium sp.

substrate_name: Acetoacetate; Butanoyl-CoA

assay_conditions_summary: pH 8.1; 298.15 K; cofactor CoA

proof_lines: pH 8.1, 25°C, cosubstrate acetoacetate 3.0 mM, 20 mM MgCl2

substrate: Acetoacetate; Butanoyl-CoA


organism: Escherichia coli

substrate_name: acetyl-CoA

substrate: acetyl-CoA


organism: Bos taurus

substrate_name: DL-phosphoserine

proof_lines:
unassociated enzyme form
associated enzyme form

substrate: DL-phosphoserine


substrate_name: D-phosphoserine

substrate: D-phosphoserine


organism: Mus musculus

substrate_name: L-phosphoserine

substrate: L-phosphoserine


organism: Porphyromonas gingivalis

proof_lines: at 30°C, in 50 mM Tris (pH 7.5), with 5 mM MgCl2


organism: Pseudomonas aeruginosa


organism: Rattus norvegicus

proof_lines:
liver enzyme
tumor cell enzyme


organism: Thermus thermophilus

substrate_name: O-phospho-L-serine

substrate: O-phospho-L-serine


substrate_name: NADPH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

proof_lines: pH 8.0, 25°C, recombinant detagged enzyme

substrate: NADPH


organism: Saccharopolyspora erythraea


substrate_name: beta-phenylethylamine

proof_lines: 5-methyltetrahydrofolate as methyl donor

proof_lines: mitochondrial enzyme, control liver, S-adenosyl-L-methionine

proof_lines: mitochondrial enzyme, cholestatic liver, S-adenosyl-L-methionine

substrate: beta-phenylethylamine


proof_lines: SABIO-RK modifier species: gamma-glutamyltransferase(Enzyme) mutant cystinosis cells


proof_lines: isoform GGT5, in 100 mM Na2HPO4, 3.2 mM KCl, 1.8 mM KH2PO4, and 27.5 mM NaCl, pH 7.4, at 37°C


mutation_signature: Δ1

proof_lines: SABIO-RK modifier species: gamma-glutamyltransferase(Enzyme) mutant delta 1-27


proof_lines:
recombinant wild-type, transpeptidation
recombinant wild-type
recombinant wild-type enzyme


organism: Lentinula edodes


substrate_name: glutathione

substrate: glutathione


organism: Oncornavirus

substrate_name: Unknown

substrate: Unknown


organism: Ovis aries


organism: Penicillium roqueforti


organism: Aspergillus fumigatus

assay_conditions_summary: pH 7.5; 288.15 K; cofactor NADPH


substrate_name: NADH

substrate: NADH


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH


proof_lines: mutant S257A, hydroxylamine detection assay, pH 7.5, 25°C

proof_lines: mutant S257A, O2 consumption assay, pH 7.5, 25°C


proof_lines: wild-type, O2 consumption assay, pH 7.5, 25°C

proof_lines: wild-type, hydroxylamine detection assay, pH 7.5, 25°C


proof_lines: pH 7.5, 25°C, recombinant wild-type enzyme, O2 consumption assay

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


proof_lines: pH 7.5, 25°C, recombinant mutant S469A, O2 consumption assay

proof_lines: pH 7.5, 25°C, recombinant mutant S469A, ornithine hydroxylation assay


proof_lines: pH 7.5, 25°C, recombinant mutant N293A, ornithine hydroxylation assay

proof_lines: pH 7.5, 25°C, recombinant mutant N293A, O2 consumption assay


proof_lines: pH 7.5, 25°C, recombinant mutant N323A, ornithine hydroxylation assay

proof_lines: pH 7.5, 25°C, recombinant mutant N323A, O2 consumption assay


organism: Arabidopsis thaliana

sequence_source: UniProtKB reviewed accession Q67XZ3 (INV3_ARATH), retrieved 2026-06-18

assay_conditions_summary: pH 5; 303.15 K; buffer this verdict. Source note: in 50 mM sodium acetate

proof_lines: in 50 mM sodium acetate buffer, pH 5.0, at 30°C


organism: Aspergillus awamori

sequence_source: UniProt REST direct accession lookup for Q96TU3 on 2026-06-18

proof_lines:
at 37ºC, pH 4.5
Raw SKiD Env: Temp=-----, pH=4.5


organism: Aspergillus niger


organism: Cichorium intybus

sequence_source: UniProt REST direct accession lookup for Q93X60 on 2026-06-18


organism: Kluyveromyces marxianus

proof_lines:
at pH 4.5 and 50°C
at pH 5.5 and 50°C
at pH 4.5 and 60°C


organism: Penicillium sp.

assay_conditions_summary: pH 5


organism: Proteus mirabilis

proof_lines:
transpeptidation
hydrolase reaction
with GSH


organism: Raphanus sativus

proof_lines: 37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT A

proof_lines: 37°C, pH 8.0, cosubstrate: Gly-Gly, enzyme form GGT II


proof_lines:
kidney enzyme
D-Glu-4-nitroanilide
rat kidney enzyme


organism: Saccharomyces cerevisiae


organism: Setaria cervi

proof_lines: in presence of borate, microsomal enzyme


organism: Solanum lycopersicum

proof_lines:
isoform I, hydrolase reaction
isoform II
isoform I


organism: Sus scrofa


organism: Toona sinensis


enzyme_display_name: shikimate kinase

organism: Colwellia psychrerythraea

substrate_name: shikimate

assay_conditions_summary: pH 7.5; 298.15 K; cofactor ATP

enzyme: shikimate kinase

substrate: shikimate


organism: Dickeya chrysanthemi

substrate_name: ATP

assay_conditions_summary: pH 7; 298.15 K; cofactor ATP

substrate: ATP


organism: Helicobacter pylori

assay_conditions_summary: pH 7.7; 298.15 K; cofactor NADH

proof_lines: in 100 mM Tris–HCl (pH 8.0), 50 mM KCl, 5 mM MgCl2, 2 mM ATP, 2 mM phosphoenolpyruvate, 0.7 mM NADH, 3 U/ml proteinase K, 2.5 U/ml lactate dehydrogenase, and 2 mM shikimate, at 25°C


organism: Methanocaldococcus jannaschii


organism: Mycobacterium tuberculosis

assay_conditions_summary: pH 7.6; 298.15 K; cofactor ATP

proof_lines: estimated Ki-value determined with varied ATP concentrations and a fixed shikimate concentration, at pH 7.6 and 25°C


organism: Sorghum bicolor

assay_conditions_summary: pH 9; cofactor ATP


organism: Vigna mungo

assay_conditions_summary: pH 8.6; cofactor ATP


organism: Clostridium acetobutylicum

substrate_name: Butanoate

substrate: Butanoate


organism: Clostridium butyricum

substrate_name: ATP; Butanoate

assay_conditions_summary: pH 7.2; 303.15 K; cofactor ATP

substrate: ATP; Butanoate


organism: Clostridium tetanomorphum

substrate_name: Isobutanoate

assay_conditions_summary: pH 7.5; 303.15 K; cofactor ATP

proof_lines: pH 7.5, 30°C, activation with 10 mM MgSO4

proof_lines: pH 7.5, 30°C, activation with 6 mM MnSO4

proof_lines: pH 7.5, 30°C, reaction with butanoate, activation with 6 mM MgSO4

substrate: Isobutanoate


organism: Listeria monocytogenes

substrate_name: Isobutyrate

substrate: Isobutyrate


organism: Cavia porcellus


organism: Heterodontus portusjacksoni


organism: Mycolicibacterium smegmatis

substrate_name: N-acetyl-D-glucosamine

sequence_source: UniProt REST FASTA A0R2I7, reviewed MSHB_MYCS2, EC 3.5.1.103, Mycolicibacterium smegmatis strain ATCC 700084 / mc(2)155

proof_lines:
Co2+-enzyme, pH 7.5, 30°C
Fe2+-enzyme, pH 7.5, 30°C
Fe3+-enzyme, pH 7.5, 30°C

substrate: N-acetyl-D-glucosamine


sequence_source: UniProt REST FASTA A0R2I7 used only as canonical context; variant sequence not reconstructed

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


proof_lines: above 400 mM, mutant D146A, pH 7.5, 30°C


organism: Arabidopsis thaliana

sequence_source: UniProt REST FASTA O80452, reviewed AMPD_ARATH, EC 3.5.4.6, Arabidopsis thaliana

proof_lines: in 25 mM imidazole, pH 6.5, 150 mM potassium chloride, 2.4 mM AMP, and 0.2 mg/ml bovine serum albumin


organism: Aspergillus oryzae

substrate_name: AMP

proof_lines: pH 6.0, temperature not specified in the publication

substrate: AMP


organism: Catharanthus roseus


organism: Salmonella enterica subsp. enterica serovar Typhimurium

substrate_name: P1,P4-bis(5'-adenosyl) tetraphosphate

substrate: P1,P4-bis(5'-adenosyl) tetraphosphate


organism: Amycolatopsis orientalis

substrate_name: chitohexaose

proof_lines: 2-amino-2-deoxy-D-glucopyranose split off, pH 5.2, 20°C

substrate: chitohexaose


organism: Aspergillus fumigatus

substrate_name: chitosan

substrate: chitosan


organism: Photobacterium profundum

substrate_name: 4-nitrophenyl beta-D-glucoside

substrate: 4-nitrophenyl beta-D-glucoside


organism: Talaromyces funiculosus

substrate_name: chitobiose

substrate: chitobiose


organism: Alternaria alternata

substrate_name: inulin

substrate: inulin


organism: Aspergillus ficuum


organism: Kluyveromyces marxianus

proof_lines:
purified enzyme, at pH 5.0 and 55°C
purified enzyme, at pH 5.0 and 50°C
pH 5.5, 50°C


organism: Penicillium sp.

proof_lines:
InuE
InuE:D hybrid


organism: Triticum aestivum


organism: Homo sapiens

proof_lines: pH and temperature not specified in the publication


organism: Rattus norvegicus

proof_lines: pH 7.4, 37°C, versus 5,6beta-epoxy-5alpha-cholestan-3beta-ol

proof_lines: pH 7.4, 37°C, versus 5,6alpha-epoxy-5alpha-cholestan-3beta-ol


organism: Helix pomatia


assay_conditions_summary: cofactor ATP

proof_lines:
recombinant AMPD2, with 12.5 mM ATP
recombinant AMPD2, without ATP
recombinant AMPD1, without ATP


organism: Lathyrus oleraceus


organism: Oncorhynchus mykiss


organism: Oryctolagus cuniculus


proof_lines: EDTA-eluted purified enzyme, pH 6.5, 20°C

proof_lines: pH 6.5, 20°C, trinitrobenzene sulfonic acid-treated enzyme


organism: Pisum sativum

substrate_name: H2O; AMP

substrate: H2O; AMP


proof_lines:
myosin-bound enzyme
free enzyme


organism: Sus scrofa


organism: Badhamia polycephala

proof_lines:
and 0.037, biphasic kinetics
and 0.0026, biphasic kinetics


organism: Escherichia coli

proof_lines:
with Mn2+
with Co2+
pH 7.6, 30°C


organism: Salmonella enterica


enzyme_display_name: steroid 11beta-monooxygenase

organism: Bos taurus

enzyme: steroid 11beta-monooxygenase


substrate_name: cortisol

substrate: cortisol


enzyme_display_name: NADH peroxidase

organism: Enterococcus faecalis

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

enzyme: NADH peroxidase


substrate_name: menadione

substrate: menadione


substrate_name: Duroquinone

substrate: Duroquinone


substrate_name: Naphthazarin

substrate: Naphthazarin


substrate_name: H+; H2O2; NADH reaction-component bundle

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

assay_conditions_summary: cofactor NADH


substrate_name: NADH/H+/H2O2 H10Q mutant bundle

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H10Q to reconstruct the assayed variant sequence.

proof_lines: SABIO-RK modifier species: NADH peroxidase(Enzyme) mutant H10Q

substrate: NADH/H+/H2O2 H10Q mutant bundle


substrate_name: H+/NADH/H2O2 H10A mutant bundle

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

proof_lines: SABIO-RK modifier species: NADH peroxidase(Enzyme) mutant H10A

substrate: H+/NADH/H2O2 H10A mutant bundle


substrate_name: NADH, H10Q mutant

assay_conditions_summary: pH 7; 278.15 K; cofactor NADH

substrate: NADH, H10Q mutant


substrate_name: H2O2, H10A mutant

smiles: OO

substrate: H2O2, H10A mutant


substrate_name: competitive inhibition context, substrate not resolved in selected snapshot


proof_lines:
pH 7.4, 37°C
competitive inhibition, pH 7.4


substrate_name: 11-deoxycortisol / 11-deoxycorticosterone variant-unspecified bundle

proof_lines: mutant enzyme, 11beta-hydroxylation, pH 7.5, 37°C


substrate_name: 11-deoxycortisol / 11-deoxycorticosterone wild-type bundle

proof_lines: wild-type enzyme, 11beta,18beta-dihydroxylation, pH 7.5, 37°C

proof_lines: wild-type enzyme, 18beta-hydroxylation, pH 7.5, 37°C

proof_lines: wild-type enzyme, 11beta-hydroxylation, pH 7.5, 37°C


substrate_name: O2; 11-Deoxycorticosterone; Reduced ferredoxin


assay_conditions_summary: pH 5.5; cofactor NADH

proof_lines:
calculated per flavin
under standard assay conditions
at pH 5.5


substrate_name: NADH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADH

substrate: NADH


proof_lines: dipalmitoyl phosphatidylcholine vesicles + diphosphatidyl glycerol


organism: Curvularia lunata


substrate_name: adrenal ferredoxin

proof_lines: pH 7.4, recombinant enzyme, with 11-deoxycorticosterone as substrate

proof_lines: pH 7.4, recombinant enzyme, with 11-deoxycortisol as substrate

substrate: adrenal ferredoxin


sequence_source: UniProtKB:P37062 direct REST lookup on 2026-06-18


substrate_name: H+; NADH; H2O2

sequence_variant_note: Resolved canonical sequence from UniProtKB:P37062 direct REST lookup on 2026-06-18 and applied mutation signature R303M to reconstruct the assayed variant sequence.

assay_conditions_summary: cofactor NAD+

proof_lines: SABIO-RK modifier species: NADH peroxidase(Enzyme) mutant R303M

substrate: H+; NADH; H2O2


assay_conditions_summary: pH 5.4; 298.15 K; cofactor NADH


substrate_name: Hexacyanoferrate(III)

assay_conditions_summary: pH 5.65; 299.15 K; cofactor NADH

substrate: Hexacyanoferrate(III)


substrate_name: Adriamycin

substrate: Adriamycin


substrate_name: PQQ

substrate: PQQ


proof_lines: kcat is 1.67 sec(-1) with 11-deoxycortisol as substrate. kcat is 0.85 sec(-1) with 21-hydroxyprogesterone as substrate.


enzyme_display_name: F-actin monooxygenase

substrate_name: F-actin (at saturating NADPH concentration)

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 0.28 sec(-1) for NADPH for the NADPH oxidase reaction.

enzyme: F-actin monooxygenase


organism: Mus musculus

substrate_name: actin (for a monooxygenase domain construct)


substrate_name: [F-actin]-L-methionine; O2; H+; NADPH

proof_lines: SABIO-RK modifier species: F-actin monooxygenase(Enzyme) mutant residues 1-496 C-terminal His6-tag

substrate: [F-actin]-L-methionine; O2; H+; NADPH


substrate_name: H+; O2; NADPH

proof_lines: SABIO-RK modifier species: F-actin monooxygenase(Enzyme) mutant residues 1-510 N-terminal His6-tag

proof_lines: SABIO-RK modifier species: F-actin monooxygenase(Enzyme) mutant residues 1-490

substrate: H+; O2; NADPH


substrate_name: MICAL-MO; NADPH

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

proof_lines: isolated monooxygenase-like domain, pH 7.0, 25°C

substrate: MICAL-MO; NADPH


substrate_name: [F-actin]-L-methionine; O2; NADPH; H+

substrate: [F-actin]-L-methionine; O2; NADPH; H+


substrate_name: NADPH

sequence_source: UniProtKB:Q8TDZ2 direct REST check

substrate: NADPH


mutation_type: truncation

proof_lines: truncated form comprising the MO and CH domains, pH 7.0, 25°C


mutation_signature: truncated form comprising the MO

proof_lines: truncated form comprising the MO, CH and LIM domains, pH 7.0, 25°C


substrate_name: [F-actin]-L-methionine

substrate: [F-actin]-L-methionine


proof_lines: recombinant MICAL3 lacking the CH domain, pH 7.5, 25°C


proof_lines: pH 8.0, 25°C, recombinant hMICAL3FMOCHDELTA213,530


sequence_source: UniProtKB:Q7RTP6 direct REST check


sequence_source: reconstructed from UniProtKB:Q8VDP3 residues 1-484 plus selected SABIO K141A/K142A note

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

proof_lines: SABIO-RK modifier species: F-actin monooxygenase(Enzyme) mutant residues 1-484 (FAD-binding domain), K141A, K142A


enzyme_display_name: violaxanthin de-epoxidase

organism: Lactuca sativa

substrate_name: violaxanthin

proof_lines: reaction significantly slower in the absence of monogalactosyldiacylglyceride.

enzyme: violaxanthin de-epoxidase

substrate: violaxanthin


organism: Spinacia oleracea

substrate_name: ascorbate at pH 6.0

assay_conditions_summary: pH 6

proof_lines: KM for ascorbate increased when H-245, H-248, H-291 or H-297 are mutated.

substrate: ascorbate at pH 6.0


substrate_name: L-Ascorbate; Violaxanthin

sequence_source: UniProtKB Q40251 REST lookup, direct check on 2026-06-18

substrate: L-Ascorbate; Violaxanthin


sequence_source: UniProtKB Q9SM43 REST lookup, direct check on 2026-06-18


organism: Triticum aestivum

substrate_name: Violaxanthin; L-Ascorbate

sequence_source: UniProtKB Q9AU61 REST lookup, direct check on 2026-06-18

substrate: Violaxanthin; L-Ascorbate


substrate_name: ascorbate

sequence_source: UniProtKB reviewed Q40251 (VDE_LACSA), direct EC+organism lookup

proof_lines: pH 5.1, 26°C, at an ratio of monogalactosyldiacylglyceride to the substrate violaxanthin is 45:1

proof_lines: pH 5.1, 26°C, at the optimal ratio of monogalactosyldiglyceride to the substrate violaxanthin is 28:1

substrate: ascorbate


organism: Mantoniella squamata


sequence_source: UniProtKB reviewed Q9SM43 (VDE_SPIOL), direct EC+organism lookup

proof_lines: at pH 5.0, with 0.0004 mM violaxanthin and 0.0116 mM monogalactosyldiacylglycerol in reaction medium containing 10 mM KCl, 5 mM MgCl2 and 40 mM morpholinoethanesulfonic acid


substrate_name: Coenzyme A; 2-Oxopentanoate; NAD+

substrate: Coenzyme A; 2-Oxopentanoate; NAD+


organism: Syntrophotalea carbinolica

substrate_name: dihydrolipoamide

substrate: dihydrolipoamide


organism: Thermochaetoides thermophila (strain DSM 1495 / CBS 144.50 / DAOM 24625 / IMI 039719)

substrate_name: coenzyme A

sequence_source: source_record; UniProtKB G0S4X6 FASTA direct check

assay_conditions_summary: cofactor CoA

substrate: coenzyme A


substrate_name: Pyruvate; NAD+; Coenzyme A

substrate: Pyruvate; NAD+; Coenzyme A


organism: Corynebacterium glutamicum

substrate_name: Pyruvate; Coenzyme A; NAD+

proof_lines: SABIO-RK modifier species: Enzyme mutant AceF K43Q-K162Q

substrate: Pyruvate; Coenzyme A; NAD+


substrate_name: Coenzyme A; NAD+; Pyruvate

substrate: Coenzyme A; NAD+; Pyruvate


proof_lines: SABIO-RK modifier species: Enzyme mutant AceF K162Q-K278Q


substrate_name: NAD+; Coenzyme A; Pyruvate

substrate: NAD+; Coenzyme A; Pyruvate


substrate_name: Dihydrolipoamide; Acetyl-CoA

substrate: Dihydrolipoamide; Acetyl-CoA


proof_lines: SABIO-RK modifier species: Enzyme mutant E1 Y177F


proof_lines: SABIO-RK modifier species: Enzyme mutant E1 Y177A


proof_lines: SABIO-RK modifier species: Enzyme mutant 1-lip PDHc (single lipoyl domain per E2 chain) G231A


proof_lines: SABIO-RK modifier species: Enzyme mutant 1-lip PDHc (single lipoyl domain per E2 chain) C259N


organism: Homo sapiens


organism: Mycobacterium tuberculosis


organism: Pelobacter carbinolicus


organism: Solanum tuberosum

substrate_name: Coenzyme A; Pyruvate; NAD+

substrate: Coenzyme A; Pyruvate; NAD+


organism: Azotobacter vinelandii

substrate_name: acetyl-CoA

proof_lines:
with dihydrolipoamide, S558A mutant
S558A mutant

substrate: acetyl-CoA


proof_lines:
with dihydrolipoamide, N614D mutant
N614D mutant


proof_lines:
with dihydrolipoamide, wild-type enzyme
wild-type enzyme


proof_lines:
with dihydrolipoamide, H610C mutant
H610C mutant


organism: Escherichia coli


organism: Geobacillus stearothermophilus

proof_lines: catalytic domain after expression in Escherichia coli


proof_lines: SABIO-RK modifier species: Enzyme mutant S264A S271A His-tagged


proof_lines: SABIO-RK modifier species: Enzyme mutant S264A His-tagged


proof_lines: SABIO-RK modifier species: Enzyme mutant S271A His-tagged


organism: Lactococcus lactis subsp. lactis


enzyme_display_name: beta-lactamase

organism: Aeromonas hydrophila

sequence_source: UniProtKB direct lookup for P26918 on 2026-06-18

enzyme: beta-lactamase


organism: Bacillus licheniformis

substrate_name: Penicillin V; H2O

sequence_source: UniProtKB:P00808 FASTA direct lookup on 2026-06-18.

substrate: Penicillin V; H2O


substrate_name: Nitrocefin; H2O

sequence_source: UniProtKB:P13661 direct lookup on 2026-06-18

proof_lines: pH 7.2, temperature not specified in the publication, recombinant enzyme

substrate: Nitrocefin; H2O


organism: Serratia marcescens

substrate_name: Ampicillin; H2O

sequence_source: UniProtKB:P52699 REST direct accession lookup on 2026-06-18

proof_lines:
pH 7.5, 25°C
at 30°C

substrate: Ampicillin; H2O


organism: Pseudomonas aeruginosa

substrate_name: Penicillin G; H2O

substrate: Penicillin G; H2O


organism: Kluyvera ascorbata

substrate_name: cefotaxime

assay_conditions_summary: pH 7; 298.15 K; buffer pH 7

proof_lines: Km above 1.0 mM, in 0.01 M phosphate buffer (pH 7.0), at 25°C

substrate: cefotaxime


substrate_name: cefazolin

assay_conditions_summary: pH 7; 303.15 K; buffer sodium phosphate

proof_lines: at 30°C in 50 mM sodium phosphate buffer (pH 7.0)

substrate: cefazolin


enzyme_display_name: carbonic anhydrase

proof_lines: pH 8.88, TAPS buffer, carbonic anhydrase I mutant H200T

proof_lines: pH 7.21, 1-methylimidazole buffer, carbonic anhydrase I mutant H200T

proof_lines: pH 8.95, 1,2-dimethylimidazole buffer, carbonic anhydrase I mutant H200T

enzyme: carbonic anhydrase


proof_lines: pH 6.3, MES buffer, wild-type carbonic anhydrase I

proof_lines: pH 8.8, TAPS buffer, wild-type carbonic anhydrase I

proof_lines: pH 8.77, 1,2-dimethylimidazole buffer, wild-type carbonic anhydrase I


organism: Methanosarcina thermophila

assay_conditions_summary: pH 7.5; 298.15 K; buffer MOPS

proof_lines: pH 7.5, 25°C, variant E62D, 50 mM MOPS buffer


organism: Methanothermobacter thermautotrophicus

assay_conditions_summary: pH 8.5; 298.15 K; buffer variants

proof_lines: pH 8.5, 25°C, wild-type, imidazole buffer


organism: Populus tremula

assay_conditions_summary: pH 6.6; buffer | pH 8

proof_lines:
pH 6.6, MES buffer
pH 8.8, TAPS buffer


enzyme_display_name: beta-glucosidase

organism: Fusarium proliferatum

substrate_name: ginsenoside Rg3

assay_conditions_summary: pH 5; 323.15 K; buffer pH 5

proof_lines: in NaAc/HAc buffer (0.2 M, pH 5.0), at 50°C

enzyme: beta-glucosidase

substrate: ginsenoside Rg3


organism: Levilactobacillus brevis

assay_conditions_summary: pH 5.5; 310.15 K; buffer citrate-phosphate

proof_lines: in 0.2 mM citrate-phosphate buffer, pH 5.5, at 37°C


organism: Rhynchophorus palmarum

assay_conditions_summary: pH 5; 310.15 K; buffer pH 5

proof_lines: in 100 mM acetate buffer, pH 5.0, at 37°C


enzyme_display_name: carboxylesterase

organism: Oryctolagus cuniculus

substrate_name: D-luciferin methyl ester

sequence_source: UniProtKB:P12337 direct REST lookup

assay_conditions_summary: pH 6.5; cofactor CoA

proof_lines:
isoform CES1, at pH 6.5 and 37Â°C
ratio kcat/Km is 180 per min and mM
at pH 7.4 and 37Â°C

enzyme: carboxylesterase

substrate: D-luciferin methyl ester


organism: Rattus norvegicus

substrate_name: retinyl palmitate

sequence_source: UniProtKB:Q64573 direct REST lookup

assay_conditions_summary: pH 8; 310.15 K; cofactor CoA

substrate: retinyl palmitate


enzyme_display_name: glutathione transferase

organism: Homo sapiens

substrate_name: glutathione

sequence_source: UniProtKB REST/FASTA accession P09211

assay_conditions_summary: pH 7.4; 298.15 K; buffer 0.1 M potassium phosphate

proof_lines: His-tagged recombinant wild type enzyme, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5

proof_lines: wild type enzyme, in the presence of cosubstrate 1-chloro-2,4-dinitrobenzene, in 0.1 M phosphate buffer at pH 6.5

enzyme: glutathione transferase

substrate: glutathione


sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA accession P09211 and applied mutation signature I104V/A113V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; buffer 0.1 M phosphate

proof_lines: mutant enzyme I104V/A113V, at pH 7.4 and 25°C

proof_lines: mutant enzyme I104V/A113V, in the presence of cosubstrate 7-chloro-4-nitrobenz-2-oxa-1,3-diazole, in 0.1 M phosphate buffer at pH 6.5

proof_lines: mutant enzyme I104V/A113V, in 0.1 M phosphate buffer at pH 6.5


organism: Hordeum vulgare

sequence_source: UniProtKB REST/FASTA accession Q3MUP2


organism: Hyphantria cunea

sequence_source: UniProtKB REST/FASTA accession Q4ACU7


organism: Musca domestica

sequence_source: UniProtKB REST/FASTA accession Q9U795

sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA accession Q9U795 and applied mutation signature F108G to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant F108G, pH and temperature not specified in the publication


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

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


sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA accession Q9U795 and applied mutation signature R113A to reconstruct the assayed variant sequence.

proof_lines: recombinant His-tagged mutant R113A, pH and temperature not specified in the publication


organism: Nilaparvata lugens

sequence_source: UniProtKB REST/FASTA accession Q8N0B3


sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA accession Q8N0B3 and applied mutation signature V54A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA accession Q8N0B3 and applied mutation signature H52A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA accession Q8N0B3 and applied mutation signature S11A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA accession Q8N0B3 and applied mutation signature R68A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA accession Q8N0B3 and applied mutation signature E66A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA accession Q8N0B3 and applied mutation signature S67A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA accession Q8N0B3 and applied mutation signature F119A to reconstruct the assayed variant sequence.


organism: Novosphingobium aromaticivorans

sequence_source: UniProtKB REST/FASTA accession Q2G4B4

sequence_variant_note: Resolved canonical sequence from UniProtKB REST/FASTA accession Q2G4B4 and applied mutation signature N14A to reconstruct the assayed variant sequence.


organism: Phanerodontia chrysosporium

substrate_name: Unknown

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

proof_lines: pH 6.5, temperature not specified in the publication

substrate: Unknown


substrate_name: 4-nitrophenyl butyrate; glutathione; 1-chloro-2,4-dinitrobenzene

sequence_variant_note: Resolved canonical sequence from UniProtKB:I6ZUH3 plus direct S22A reconstruction and applied mutation signature S22A to reconstruct the assayed variant sequence.

proof_lines: recombinant mutant S22A, pH 6.5, temperature not specified in the publication


organism: Pinus brutia


organism: Pinus tabuliformis

substrate_name: 1-chloro-2,3-dinitrobenzene; GSH

substrate: 1-chloro-2,3-dinitrobenzene; GSH


organism: Plasmodium falciparum


organism: Plasmodium vivax


organism: Plasmodium yoelii


organism: Populus trichocarpa

substrate_name: sulforaphane; 1-chloro-2,4-dinitrobenzene; phenethyl isothiocyanate; allyl-isothiocyanate; cumene hydroperoxide

proof_lines: isoform GSTU45, pH not specified in the publication, at 30°C


substrate_name: allyl-isothiocyanate; phenethyl isothiocyanate; cumene hydroperoxide; sulforaphane; 1-chloro-2,4-dinitrobenzene

proof_lines: isoform GSTU16, pH not specified in the publication, at 30°C


organism: Salix babylonica


organism: Glycine max

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

proof_lines: with tert-butyl peroxide as cosubstrate, at pH 6.5 and 25°C

proof_lines: with fluorodifen as cosubstrate, at pH 6.5 and 25°C

proof_lines: with 1-chloro-2,4-dinitrobenzene as cosubstrate, at pH 6.5 and 25°C


organism: Hippocampus abdominalis


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C14A/C47A/C101A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 303.15 K; buffer 0.1 M potassium phosphate

proof_lines: mutant enzyme C14A/C47A/C101A, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C47A/C101A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C47A/C101A, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C14A/C47A/C101A/C169A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C14A/C47A/C101A/C169A, at 30°C, in 0.1 M potassium phosphate buffer, pH 6.5


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A113V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; buffer 0.1 M phosphate

proof_lines: mutant enzyme A113V, in the presence of cosubstrate 1-chloro-2,4-dinitrobenzene, in 0.1 M phosphate buffer at pH 6.5

proof_lines: mutant enzyme A113V, in the presence of cosubstrate ethacrynic acid, in 0.1 M phosphate buffer at pH 6.5

proof_lines: mutant enzyme A113V, in the presence of cosubstrate 7-chloro-4-nitrobenz-2-oxa-1,3-diazole, in 0.1 M phosphate buffer at pH 6.5


substrate_name: Ethacrynic acid

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 enzyme104V, in 0.1 M phosphate buffer at pH 6.5

substrate: Ethacrynic acid


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T67A with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 298.15 K; buffer phosphate

proof_lines: mutant enzyme T67A, in phosphate buffer (pH 6.5), at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D94N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D94N, in phosphate buffer (pH 6.5), at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D90N with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme D90N, in phosphate buffer (pH 6.5), at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R70Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R70Q, in phosphate buffer (pH 6.5) ,at 25°C

proof_lines: mutant enzyme R70Q, in phosphate buffer (pH 6.5), at 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R74Q with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R74Q, in phosphate buffer (pH 6.5), at 25°C


proof_lines: in phosphate buffered saline, pH 7.4, at 37°C


substrate_name: iodobutane

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

substrate: iodobutane


substrate_name: gamma-Glu-Cys-Sar

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature I104V with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme I104V, in the presence of cosubstrate 1-chloro-2,4-dinitrobenzene, in 0.1 M phosphate buffer at pH 6.5

proof_lines: mutant enzyme I104V, in the presence of cosubstrate 7-chloro-4-nitrobenz-2-oxa-1,3-diazole, in 0.1 M phosphate buffer at pH 6.5

substrate: gamma-Glu-Cys-Sar


sequence_source: UniProtKB:Q2G4B4 canonical sequence


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q2G4B4 canonical sequence by S15A and applied mutation signature S15A to reconstruct the assayed variant sequence.


proof_lines: mutant enzyme S14A/S15A, at pH 8.0 and 30°C


organism: Onchocerca volvulus

sequence_source: UniProtKB:P46427 canonical sequence


organism: Oryza sativa

sequence_source: UniProtKB:Q93WY5 canonical sequence


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q93WY5 canonical sequence by L112A and applied mutation signature L112A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme L112A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q93WY5 canonical sequence by Y113A and applied mutation signature Y113A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y113A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q93WY5 canonical sequence by N109A and applied mutation signature N109A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N109A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q93WY5 canonical sequence by F116A and applied mutation signature F116A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F116A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q93WY5 canonical sequence by W161A and applied mutation signature W161A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme W161A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q93WY5 canonical sequence by M17A and applied mutation signature M17A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme M17A, at 25°C, pH not specified in the publication


sequence_variant_note: Resolved canonical sequence from Reconstructed from UniProtKB:Q93WY5 canonical sequence by F162A and applied mutation signature F162A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F162A, at 25°C, pH not specified in the publication


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

proof_lines: wild type enzyme, at 25°C, pH not specified in the publication


organism: Pagrus major

sequence_source: UniProtKB:Q50LH1 canonical sequence

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


substrate_name: 4-nitrophenyl butyrate

sequence_source: UniProtKB:I6ZUH3 canonical sequence

proof_lines: recombinant wild-type, pH 6.5, temperature not specified in the publication

substrate: 4-nitrophenyl butyrate


organism: Anopheles dirus

sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup for Q9GN60 and applied mutation signature F212E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F212E, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup for Q9GN60 and applied mutation signature F212A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F212A, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup for Q9GN60 and applied mutation signature Q112A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Q112A, in 0.1 M phosphate buffer pH 6.5


organism: Anopheles gambiae

sequence_source: UniProt REST exact accession lookup for Q7PVS6


organism: Arabidopsis thaliana

substrate_name: acrolein

sequence_source: UniProt REST exact accession lookup for Q9ZRW8

substrate: acrolein


organism: Ascaris suum

sequence_source: UniProt REST exact accession lookup for P46436


organism: Bombyx mori

sequence_source: UniProt REST exact accession lookup for A8R5V3


sequence_source: UniProt REST exact accession lookup for Q60GK5


sequence_source: UniProt REST exact accession lookup for Q5CCJ4


organism: Brucella anthropi

sequence_source: UniProt REST exact accession lookup for P81065


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup for P81065 and applied mutation signature C10A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProt REST exact accession lookup for P81065 and applied mutation signature C10A/S11A to reconstruct the assayed variant sequence.


organism: Chlamys islandica

sequence_source: UniProt REST exact accession lookup for Q0P7I5


organism: Clonorchis sinensis

sequence_source: UniProt REST exact accession lookup for Q1L2C7


organism: Danio rerio

sequence_source: UniProt REST exact accession lookup for Q9DDU5


organism: Drosophila melanogaster

substrate_name: dehydroascorbate

sequence_source: UniProt REST exact accession lookup for Q9VSL5

substrate: dehydroascorbate


verification_status: corrected

sequence_source: UniProtKB REST accession lookup for A0A4Y5R0K8

assay_conditions_summary: pH 6.5; 298.15 K; buffer 50 mM potassium phosphate

column_label: Table 2 'Steady-state kinetic parameters of Salix tau GSTs'; row head 'GSTs' = 'SbGSTU3'; column 'KmGSH' (unit row 'mM') = 0.140; column 'kcatGSH' (unit row 's^-1') = 16.714; column '(kcat/Km)GSH' (unit row 'mM^-1 s^-1') = 119.300; the same row's CDNB-varied columns read 'KmCDNB' = 1.003 mM, 'kcatCDNB' = 28.819 s^-1 and '(kcat/Km)CDNB' = 28.733 mM^-1 s^-1 and belong to the other substrate.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.140 mM; the paper already prints millimolar, so no conversion is applied and the normalized value is 0.14 mM. kcat: printed Table 2 cell 16.714 s^-1; the paper already prints reciprocal seconds (this table prints no min^-1 cell), so no conversion is applied and the normalized value is 16.714 s^(-1). kcat/Km: printed Table 2 cell 119.300 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no conversion is applied and the normalized value is 119.3 s^(-1)*mM^(-1). Closure disclosure: 16.714 / 0.140 = 119.386 s^-1 mM^-1, which agrees with the separately printed efficiency cell 119.300 to the paper's three-decimal precision.

raw_value_unit_evidence: Table 2, row SbGSTU3, glutathione-varied columns: KmGSH = 0.140 printed in the unit row 'mM'; kcatGSH = 16.714 printed in the unit row 's^-1'; (kcat/Km)GSH = 119.300 printed in the unit row 'mM^-1 s^-1'.

row_label: Table 2, row SbGSTU3, glutathione-varied columns (KmGSH, kcatGSH, (kcat/Km)GSH)

table_label: Table 2: Steady-state kinetic parameters of Salix tau GSTs (Frontiers in Plant Science 2020, volume 11, article 364)

status: corrected


sequence_source: UniProtKB REST accession lookup for A0A4Y5QZW9

column_label: Table 2 'Steady-state kinetic parameters of Salix tau GSTs'; row head 'GSTs' = 'SbGSTU5'; column 'KmGSH' (unit row 'mM') = 0.240; column 'kcatGSH' (unit row 's^-1') = 3.376; column '(kcat/Km)GSH' (unit row 'mM^-1 s^-1') = 14.073; the same row's CDNB-varied columns read 'KmCDNB' = 2.364 mM, 'kcatCDNB' = 7.782 s^-1 and '(kcat/Km)CDNB' = 3.292 mM^-1 s^-1 and belong to the other substrate.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.240 mM; the paper already prints millimolar, so no conversion is applied and the normalized value is 0.24 mM. kcat: printed Table 2 cell 3.376 s^-1; the paper already prints reciprocal seconds (this table prints no min^-1 cell), so no conversion is applied and the normalized value is 3.376 s^(-1). kcat/Km: printed Table 2 cell 14.073 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no conversion is applied and the normalized value is 14.073 s^(-1)*mM^(-1). Closure disclosure: 3.376 / 0.240 = 14.067 s^-1 mM^-1, which agrees with the separately printed efficiency cell 14.073 to the paper's three-decimal precision.

raw_value_unit_evidence: Table 2, row SbGSTU5, glutathione-varied columns: KmGSH = 0.240 printed in the unit row 'mM'; kcatGSH = 3.376 printed in the unit row 's^-1'; (kcat/Km)GSH = 14.073 printed in the unit row 'mM^-1 s^-1'.

row_label: Table 2, row SbGSTU5, glutathione-varied columns (KmGSH, kcatGSH, (kcat/Km)GSH)


sequence_source: UniProtKB REST accession lookup for A0A4Y5R0L5

column_label: Table 2 'Steady-state kinetic parameters of Salix tau GSTs'; row head 'GSTs' = 'SbGSTU13'; column 'KmGSH' (unit row 'mM') = 0.262; column 'kcatGSH' (unit row 's^-1') = 11.400; column '(kcat/Km)GSH' (unit row 'mM^-1 s^-1') = 43.529; the same row's CDNB-varied columns read 'KmCDNB' = 1.273 mM, 'kcatCDNB' = 14.948 s^-1 and '(kcat/Km)CDNB' = 11.742 mM^-1 s^-1 and belong to the other substrate.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.262 mM; the paper already prints millimolar, so no conversion is applied and the normalized value is 0.262 mM. kcat: printed Table 2 cell 11.400 s^-1; the paper already prints reciprocal seconds (this table prints no min^-1 cell), so no conversion is applied and the normalized value is 11.4 s^(-1). kcat/Km: printed Table 2 cell 43.529 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no conversion is applied and the normalized value is 43.529 s^(-1)*mM^(-1). Closure disclosure: 11.400 / 0.262 = 43.511 s^-1 mM^-1, which agrees with the separately printed efficiency cell 43.529 to the paper's three-decimal precision.

raw_value_unit_evidence: Table 2, row SbGSTU13, glutathione-varied columns: KmGSH = 0.262 printed in the unit row 'mM'; kcatGSH = 11.400 printed in the unit row 's^-1'; (kcat/Km)GSH = 43.529 printed in the unit row 'mM^-1 s^-1'.

row_label: Table 2, row SbGSTU13, glutathione-varied columns (KmGSH, kcatGSH, (kcat/Km)GSH)


sequence_source: UniProtKB REST accession lookup for A0A4Y5QZX9

column_label: Table 2 'Steady-state kinetic parameters of Salix tau GSTs'; row head 'GSTs' = 'SbGSTU14'; column 'KmGSH' (unit row 'mM') = 0.491; column 'kcatGSH' (unit row 's^-1') = 12.281; column '(kcat/Km)GSH' (unit row 'mM^-1 s^-1') = 25.022; the same row's CDNB-varied columns read 'KmCDNB' = 4.269 mM, 'kcatCDNB' = 41.823 s^-1 and '(kcat/Km)CDNB' = 9.797 mM^-1 s^-1 and belong to the other substrate.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.491 mM; the paper already prints millimolar, so no conversion is applied and the normalized value is 0.491 mM. kcat: printed Table 2 cell 12.281 s^-1; the paper already prints reciprocal seconds (this table prints no min^-1 cell), so no conversion is applied and the normalized value is 12.281 s^(-1). kcat/Km: printed Table 2 cell 25.022 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no conversion is applied and the normalized value is 25.022 s^(-1)*mM^(-1). Closure disclosure: 12.281 / 0.491 = 25.012 s^-1 mM^-1, which agrees with the separately printed efficiency cell 25.022 to the paper's three-decimal precision.

raw_value_unit_evidence: Table 2, row SbGSTU14, glutathione-varied columns: KmGSH = 0.491 printed in the unit row 'mM'; kcatGSH = 12.281 printed in the unit row 's^-1'; (kcat/Km)GSH = 25.022 printed in the unit row 'mM^-1 s^-1'.

row_label: Table 2, row SbGSTU14, glutathione-varied columns (KmGSH, kcatGSH, (kcat/Km)GSH)


sequence_source: UniProtKB REST accession lookup for A0A4Y5R087

column_label: Table 2 'Steady-state kinetic parameters of Salix tau GSTs'; row head 'GSTs' = 'SbGSTU7'; column 'KmGSH' (unit row 'mM') = 1.183; column 'kcatGSH' (unit row 's^-1') = 0.804; column '(kcat/Km)GSH' (unit row 'mM^-1 s^-1') = 0.679; the same row's CDNB-varied columns read 'KmCDNB' = 2.074 mM, 'kcatCDNB' = 1.415 s^-1 and '(kcat/Km)CDNB' = 0.682 mM^-1 s^-1 and belong to the other substrate.

normalized_value_unit_evidence: Km: printed Table 2 cell 1.183 mM; the paper already prints millimolar, so no conversion is applied and the normalized value is 1.183 mM. kcat: printed Table 2 cell 0.804 s^-1; the paper already prints reciprocal seconds (this table prints no min^-1 cell), so no conversion is applied and the normalized value is 0.804 s^(-1). kcat/Km: printed Table 2 cell 0.679 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no conversion is applied and the normalized value is 0.679 s^(-1)*mM^(-1). Closure disclosure: 0.804 / 1.183 = 0.68 s^-1 mM^-1, which agrees with the separately printed efficiency cell 0.679 to the paper's three-decimal precision.

raw_value_unit_evidence: Table 2, row SbGSTU7, glutathione-varied columns: KmGSH = 1.183 printed in the unit row 'mM'; kcatGSH = 0.804 printed in the unit row 's^-1'; (kcat/Km)GSH = 0.679 printed in the unit row 'mM^-1 s^-1'.

row_label: Table 2, row SbGSTU7, glutathione-varied columns (KmGSH, kcatGSH, (kcat/Km)GSH)


sequence_source: UniProtKB REST accession lookup for A0A4Y5R2M7

column_label: Table 2 'Steady-state kinetic parameters of Salix tau GSTs'; row head 'GSTs' = 'SbGSTU1'; column 'KmGSH' (unit row 'mM') = 0.473; column 'kcatGSH' (unit row 's^-1') = 6.283; column '(kcat/Km)GSH' (unit row 'mM^-1 s^-1') = 13.277; the same row's CDNB-varied columns read 'KmCDNB' = 0.201 mM, 'kcatCDNB' = 6.056 s^-1 and '(kcat/Km)CDNB' = 30.102 mM^-1 s^-1 and belong to the other substrate.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.473 mM; the paper already prints millimolar, so no conversion is applied and the normalized value is 0.473 mM. kcat: printed Table 2 cell 6.283 s^-1; the paper already prints reciprocal seconds (this table prints no min^-1 cell), so no conversion is applied and the normalized value is 6.283 s^(-1). kcat/Km: printed Table 2 cell 13.277 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no conversion is applied and the normalized value is 13.277 s^(-1)*mM^(-1). Closure disclosure: 6.283 / 0.473 = 13.283 s^-1 mM^-1, which agrees with the separately printed efficiency cell 13.277 to the paper's three-decimal precision.

raw_value_unit_evidence: Table 2, row SbGSTU1, glutathione-varied columns: KmGSH = 0.473 printed in the unit row 'mM'; kcatGSH = 6.283 printed in the unit row 's^-1'; (kcat/Km)GSH = 13.277 printed in the unit row 'mM^-1 s^-1'.

row_label: Table 2, row SbGSTU1, glutathione-varied columns (KmGSH, kcatGSH, (kcat/Km)GSH)


sequence_source: UniProtKB REST accession lookup for A0A4Y5QZX3

column_label: Table 2 'Steady-state kinetic parameters of Salix tau GSTs'; row head 'GSTs' = 'SbGSTU10'; column 'KmGSH' (unit row 'mM') = 0.284; column 'kcatGSH' (unit row 's^-1') = 7.391; column '(kcat/Km)GSH' (unit row 'mM^-1 s^-1') = 26.053; the same row's CDNB-varied columns read 'KmCDNB' = 0.156 mM, 'kcatCDNB' = 16.183 s^-1 and '(kcat/Km)CDNB' = 104.004 mM^-1 s^-1 and belong to the other substrate.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.284 mM; the paper already prints millimolar, so no conversion is applied and the normalized value is 0.284 mM. kcat: printed Table 2 cell 7.391 s^-1; the paper already prints reciprocal seconds (this table prints no min^-1 cell), so no conversion is applied and the normalized value is 7.391 s^(-1). kcat/Km: printed Table 2 cell 26.053 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no conversion is applied and the normalized value is 26.053 s^(-1)*mM^(-1). Closure disclosure: 7.391 / 0.284 = 26.025 s^-1 mM^-1, which agrees with the separately printed efficiency cell 26.053 to the paper's three-decimal precision.

raw_value_unit_evidence: Table 2, row SbGSTU10, glutathione-varied columns: KmGSH = 0.284 printed in the unit row 'mM'; kcatGSH = 7.391 printed in the unit row 's^-1'; (kcat/Km)GSH = 26.053 printed in the unit row 'mM^-1 s^-1'.

row_label: Table 2, row SbGSTU10, glutathione-varied columns (KmGSH, kcatGSH, (kcat/Km)GSH)


sequence_source: UniProtKB REST accession lookup for A0A4Y5R2N2

column_label: Table 2 'Steady-state kinetic parameters of Salix tau GSTs'; row head 'GSTs' = 'SbGSTU11'; column 'KmGSH' (unit row 'mM') = 0.732; column 'kcatGSH' (unit row 's^-1') = 16.302; column '(kcat/Km)GSH' (unit row 'mM^-1 s^-1') = 22.285; the same row's CDNB-varied columns read 'KmCDNB' = 3.372 mM, 'kcatCDNB' = 22.472 s^-1 and '(kcat/Km)CDNB' = 6.664 mM^-1 s^-1 and belong to the other substrate.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.732 mM; the paper already prints millimolar, so no conversion is applied and the normalized value is 0.732 mM. kcat: printed Table 2 cell 16.302 s^-1; the paper already prints reciprocal seconds (this table prints no min^-1 cell), so no conversion is applied and the normalized value is 16.302 s^(-1). kcat/Km: printed Table 2 cell 22.285 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no conversion is applied and the normalized value is 22.285 s^(-1)*mM^(-1). Closure disclosure: 16.302 / 0.732 = 22.27 s^-1 mM^-1, which agrees with the separately printed efficiency cell 22.285 to the paper's three-decimal precision.

raw_value_unit_evidence: Table 2, row SbGSTU11, glutathione-varied columns: KmGSH = 0.732 printed in the unit row 'mM'; kcatGSH = 16.302 printed in the unit row 's^-1'; (kcat/Km)GSH = 22.285 printed in the unit row 'mM^-1 s^-1'.

row_label: Table 2, row SbGSTU11, glutathione-varied columns (KmGSH, kcatGSH, (kcat/Km)GSH)


sequence_source: UniProtKB REST accession lookup for A0A4Y5R0C1

column_label: Table 2 'Steady-state kinetic parameters of Salix tau GSTs'; row head 'GSTs' = 'SbGSTU12'; column 'KmGSH' (unit row 'mM') = 0.333; column 'kcatGSH' (unit row 's^-1') = 1.314; column '(kcat/Km)GSH' (unit row 'mM^-1 s^-1') = 3.947; the same row's CDNB-varied columns read 'KmCDNB' = 2.144 mM, 'kcatCDNB' = 1.934 s^-1 and '(kcat/Km)CDNB' = 0.902 mM^-1 s^-1 and belong to the other substrate.

normalized_value_unit_evidence: Km: printed Table 2 cell 0.333 mM; the paper already prints millimolar, so no conversion is applied and the normalized value is 0.333 mM. kcat: printed Table 2 cell 1.314 s^-1; the paper already prints reciprocal seconds (this table prints no min^-1 cell), so no conversion is applied and the normalized value is 1.314 s^(-1). kcat/Km: printed Table 2 cell 3.947 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^-1 mM^-1, so no conversion is applied and the normalized value is 3.947 s^(-1)*mM^(-1). Closure disclosure: 1.314 / 0.333 = 3.946 s^-1 mM^-1, which agrees with the separately printed efficiency cell 3.947 to the paper's three-decimal precision.

raw_value_unit_evidence: Table 2, row SbGSTU12, glutathione-varied columns: KmGSH = 0.333 printed in the unit row 'mM'; kcatGSH = 1.314 printed in the unit row 's^-1'; (kcat/Km)GSH = 3.947 printed in the unit row 'mM^-1 s^-1'.

row_label: Table 2, row SbGSTU12, glutathione-varied columns (KmGSH, kcatGSH, (kcat/Km)GSH)


organism: Sarcoptes scabiei

sequence_source: UniProtKB REST accession lookup for Q5ISV1


organism: Schistosoma japonicum

sequence_source: UniProtKB REST accession lookup for P26624


organism: Schistosoma mansoni

sequence_source: UniProtKB REST accession lookup for P15964


organism: Sus scrofa

sequence_source: UniProtKB REST accession lookup for P51781


organism: Taenia solium

sequence_source: UniProtKB REST accession lookup for Q8MWS0


sequence_source: UniProtKB REST accession lookup for Q3ZJN3


organism: Thermosynechococcus vestitus

sequence_source: UniProtKB REST accession lookup for Q8DMB4

assay_conditions_summary: 303.15 K; buffer 0.1 M potassium phosphate

proof_lines: at 30°C in 0.1 M potassium phosphate buffer


organism: Acidovorax sp. KKS102

substrate_name: 4-nitrobenzyl chloride

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

proof_lines: mutant enzyme Y12C, pH and temperature not specified in the publication

substrate: 4-nitrobenzyl chloride


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

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


organism: Alitta succinea

sequence_source: UniProtKB FASTA exact accession A6MN06


organism: Anopheles dirus

sequence_source: UniProtKB FASTA exact accession Q9GN60

sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature Y215F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y215F, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature F212Y to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F212Y, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature F212L to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F212L, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature F212W to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F212W, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature F216A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F216A, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature Y215H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y215H, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature F212H to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F212H, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature Y215S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y215S, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature Y215E to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y215E, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature R214A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme R214A, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature Y215A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y215A, in 0.1 M phosphate buffer pH 6.5


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

proof_lines: wild type enzyme, in 0.1 M phosphate buffer pH 6.5


sequence_variant_note: Resolved canonical sequence from UniProtKB FASTA exact accession Q9GN60 and applied mutation signature T174A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme T174A, in 0.1 M phosphate buffer pH 6.5


organism: Aedes aegypti

proof_lines: recombinant His6-tagged isozyme GSTE8-8, pH and temperature not specified in the publication

proof_lines: recombinant His6-tagged isozyme GSTE7-7, pH and temperature not specified in the publication

proof_lines: recombinant His6-tagged isozyme GSTE1-1, pH and temperature not specified in the publication


organism: Apis mellifera macedonica

substrate_name: GSH

substrate: GSH


organism: Bos taurus

proof_lines:
isozyme I
isozymes I and II
more ionic transferase


organism: Bulinus truncatus

proof_lines:
pH 6.0, 25°C, isozyme GST2
pH 7.0, 25°C, isozyme GST2
pH 8.5, 25°C, isozyme GST2


organism: Homo sapiens

substrate_name: (S,S)-1-phenylpropylene oxide

assay_conditions_summary: pH 7.2; 303.15 K; buffer 250 mM Tris-HCl

proof_lines: wild type enzyme I10C, at 30°C in 250 mM Tris-HCl buffer, pH 7.2

proof_lines: wild type enzyme G112C, at 30°C in 250 mM Tris-HCl buffer, pH 7.2

proof_lines: wild type enzyme, at 30°C in 250 mM Tris-HCl buffer, pH 7.2

substrate: (S,S)-1-phenylpropylene oxide


proof_lines: pH 7.4, 30°C, purified recombinant isozyme P1-1


organism: Mus musculus

proof_lines: pH 7.4, 37°C, recombinant wild-type isozyme GST-T1-1

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


organism: Rattus norvegicus

proof_lines:
isoenzyme 3-?, cofactor: glutathione
isoenzyme 4-4, cofactor: glutathione
isoenzyme 3-4, cofactor: glutathione


organism: Unknown


organism: Drosophila melanogaster

sequence_source: UniProtKB:Q9VSL4 direct REST lookup


organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9D2 canonical sequence plus reconstructed C10A variant and applied mutation signature C10A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 298.15 K; buffer 100 mM phosphate

proof_lines: mutant enzyme C10A, at 25°C, in 100 mM phosphate buffer (pH 6.5)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9D2 canonical sequence plus reconstructed H106F variant and applied mutation signature H106F to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H106F, at 25°C, in 100 mM phosphate buffer (pH 6.5)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9D2 canonical sequence plus reconstructed C10S variant and applied mutation signature C10S to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme C10S, at 25°C, in 100 mM phosphate buffer (pH 6.5)


sequence_variant_note: Resolved canonical sequence from UniProtKB:P0A9D2 canonical sequence plus reconstructed H106A variant and applied mutation signature H106A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme H106A, at 25°C, in 100 mM phosphate buffer (pH 6.5)


sequence_source: UniProtKB:P0A9D2 direct REST lookup

proof_lines: wild type enzyme, at 25°C, in 100 mM phosphate buffer (pH 6.5)


organism: Fasciola gigantica

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q9XYL9 canonical sequence plus reconstructed F136A variant and applied mutation signature F136A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme F136A, at pH 7.5, temperature not specified in the publication


sequence_source: UniProtKB:Q9XYL9 direct REST lookup

proof_lines: wild type enzyme, at pH 7.5, temperature not specified in the publication


organism: Gelatoporia subvermispora

substrate_name: cumene hydroperoxide

sequence_variant_note: Resolved canonical sequence from UniProtKB:M2QJS8 canonical sequence plus reconstructed N24A variant and applied mutation signature N24A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N24A, pH and temperature not specified in the publication

substrate: cumene hydroperoxide


sequence_source: UniProtKB:M2QJS8 direct REST lookup

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


substrate_name: 5-chloromethylfluorescein diacetate

sequence_variant_note: Resolved canonical sequence from UniProtKB:M2QJS8 canonical sequence plus reconstructed Y46A variant and applied mutation signature Y46A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme Y46A, pH and temperature not specified in the publication

substrate: 5-chloromethylfluorescein diacetate


sequence_variant_note: Resolved canonical sequence from UniProtKB:M2QJS8 canonical sequence plus reconstructed N22A variant and applied mutation signature N22A to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme N22A, pH and temperature not specified in the publication


organism: Glycine max

sequence_source: UniProtKB:O49235 direct REST lookup

proof_lines: pH 6.5, 30°C, recombinant wild-type GSTU4-4


sequence_variant_note: Resolved canonical sequence from UniProtKB:O49235 canonical sequence plus reconstructed P49A variant and applied mutation signature P49A to reconstruct the assayed variant sequence.

proof_lines: pH 6.5, 30°C, recombinant GSTU4-4 mutant P49A


sequence_variant_note: Resolved canonical sequence from UniProtKB:O49235 canonical sequence plus reconstructed S13A variant and applied mutation signature S13A to reconstruct the assayed variant sequence.

proof_lines: pH 6.5, 30°C, recombinant GSTU4-4 mutant S13A


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

proof_lines: pH 6.5, 30°C, recombinant GSTU4-4 mutant D48A


organism: Agrobacterium tumefaciens

substrate_name: glutathione

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

proof_lines: pH 6.5, 37°C, recombinant AtuGSTH1-1, with 1-chloro-2,4-dinitrobenzene

proof_lines: pH 6.5, 37°C, recombinant AtuGSTH1-1, with 2-hydroxyethyl disulfide


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

proof_lines: pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant R187A, with 1-chloro-2,4-dinitrobenzene


proof_lines: pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant S25A, with 1-chloro-2,4-dinitrobenzene


proof_lines: pH 6.5, 37°C, recombinant AtuGSTH1-1 mutant F22A, with 1-chloro-2,4-dinitrobenzene


organism: Alburnus tarichi

proof_lines: pH and temperature not specified in the publication


organism: Alternaria brassicicola

proof_lines: isoform GTT1.2, at pH 7.5, temperature not specified in the publication

proof_lines: isoform Ure2pB1, at pH 7.5, temperature not specified in the publication

proof_lines: isoform GSTFuA1, at pH 7.5, temperature not specified in the publication


organism: Anopheles dirus


sequence_variant_note: Resolved canonical sequence from uniprot:Q7KIF2;pdb:1JLV and applied mutation signature V147A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q7KIF2;pdb:1JLV and applied mutation signature D150Y to reconstruct the assayed variant sequence.


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

proof_lines:
25-27°C, pH 6.5, wild-type enzyme
wild-type enzyme


sequence_variant_note: Resolved canonical sequence from uniprot:Q7KIF2;pdb:1JLV and applied mutation signature D150S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q7KIF2;pdb:1JLV and applied mutation signature H144A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q7KIF2;pdb:1JLV and applied mutation signature D150A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q7KIF2;pdb:1JLV and applied mutation signature R96A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q7KIF1;pdb:1JLW and applied mutation signature I52L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q7KIF1;pdb:1JLW and applied mutation signature T31A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q7KIF1;pdb:1JLW and applied mutation signature L33A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q7KIF1;pdb:1JLW and applied mutation signature L33F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot:Q7KIF1;pdb:1JLW and applied mutation signature A35R to reconstruct the assayed variant sequence.


organism: Bombyx mori


proof_lines: pH 6.5, 30°C, recombinant wild-type enzyme


organism: Callithrix jacchus

substrate_name: styrene 7,8-oxide

proof_lines:
isoform GSTM4, at pH 7.4 and 25°C
isoform GSTM2, at pH 7.4 and 25°C
isoform GSTT1, at pH 7.4 and 25°C

substrate: styrene 7,8-oxide


organism: Camelus dromedarius

assay_conditions_summary: pH 7

proof_lines: with phenethyl isothiocyanate as cosubstrate, at pH 7.0, temperature not specified in the publication

proof_lines: with 1-chloro-2,4-dinitrobenzene as cosubstrate, at pH 7.0, temperature not specified in the publication


organism: Caretta caretta


organism: Cavia porcellus

substrate_name: Unknown


organism: Chelonia mydas


organism: Coturnix sp.

proof_lines: at pH 6.5, temperature not specified in the publication


organism: Cydia pomonella


organism: Wuchereria bancrofti

sequence_source: UniProtKB Q86LL8 direct REST lookup


organism: Zea mays

sequence_source: UniProtKB P12653 direct REST lookup

proof_lines: pH 6.5, 37°C, versus 1-chloro-2,4-dinitrobenzene


substrate_name: reduced glutathione

sequence_variant_note: Resolved canonical sequence from GenBank AF273040.1 protein_id AAG38506.1, used by PMID 16153184 for adGSTD4-4 mutagenesis and applied mutation signature L33I to reconstruct the assayed variant sequence.

substrate: reduced glutathione


sequence_variant_note: Resolved canonical sequence from GenBank AF273040.1 protein_id AAG38506.1, used by PMID 16153184 for adGSTD4-4 mutagenesis and applied mutation signature L6A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from GenBank AF273040.1 protein_id AAG38506.1, used by PMID 16153184 for adGSTD4-4 mutagenesis and applied mutation signature I52A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from GenBank AF273040.1 protein_id AAG38506.1, used by PMID 16153184 for adGSTD4-4 mutagenesis and applied mutation signature K40A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from GenBank AF273040.1 protein_id AAG38506.1, used by PMID 16153184 for adGSTD4-4 mutagenesis and applied mutation signature E37Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from GenBank AF273040.1 protein_id AAG38506.1, used by PMID 16153184 for adGSTD4-4 mutagenesis and applied mutation signature L33Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from GenBank AF273040.1 protein_id AAG38506.1, used by PMID 16153184 for adGSTD4-4 mutagenesis and applied mutation signature E37A to reconstruct the assayed variant sequence.


sequence_source: GenBank AF273040.1 protein_id AAG38506.1, used by PMID 16153184 for adGSTD4-4 mutagenesis

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


organism: Aspergillus nidulans

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


organism: Atactodea striata


organism: Bemisia tabaci

substrate_name: monochlorobimane

proof_lines:
strain GER-01
strain SUD-S

substrate: monochlorobimane


organism: Danio rerio

proof_lines:
isoform Gstz1, at pH 6.5 and 25°C
isoform Gstp2, at pH 6.5 and 25°C
isoform Gstta1, at pH 6.5 and 25°C

substrate: glutathione


organism: Drosophila melanogaster

proof_lines: GSTD1, pH and temperature not specified in the publication


organism: Eretmochelys imbricata


organism: Fasciola gigantica


organism: Gallus gallus

proof_lines:
pH 7.5, 28°C, GSH-S transferase rho
with reduced glutathione


organism: Glycine max

proof_lines: with 1-chloro-2,4-dinitrobenzene as cosubstrate, pH and temperature not specified in the publication

proof_lines: with tert-butyl peroxide as cosubstrate, pH and temperature not specified in the publication

proof_lines: with fluorodifen as cosubstrate, pH and temperature not specified in the publication


organism: Haloarcula hispanica

proof_lines: pH and temperature not specified in the publication


organism: Hevea brasiliensis


organism: Homo sapiens

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

proof_lines: pH 7.4, 37°C, mutant enzyme S15A of glutathione transferase Zeta 1c-1c, reaction with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid

proof_lines: pH 7.4, 37°C, mutant enzyme S15A of glutathione transferase Zeta 1c-1c, reaction with maleylacetone


proof_lines: pH 7.4, 37°C, mutant enzyme C16A of glutathione transferase Zeta 1c-1c, reaction with maleylacetone

proof_lines: pH 7.4, 37°C, mutant enzyme C16A of glutathione transferase Zeta 1c-1c, reaction with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid


proof_lines: pH 7.4, 37°C, mutant enzyme R175A of glutathione transferase Zeta 1c-1c, reaction with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid

proof_lines: pH 7.4, 37°C, mutant enzyme R175A of glutathione transferase Zeta 1c-1c, reaction with maleylacetone


proof_lines: pH 7.4, 37°C, enzyme variant glutathione transferase Zeta 1d-1d

proof_lines: pH 7.4, 37°C, enzyme variant glutathione transferase Zeta 1b-1b

proof_lines: pH 7.4, 37°C, enzyme variant glutathione transferase Zeta 1c-1c


proof_lines: pH 7.4, 37°C, mutant enzyme R175K of glutathione transferase Zeta 1c-1c, reaction with maleylacetone

proof_lines: pH 7.4, 37°C, mutant enzyme R175K of glutathione transferase Zeta 1c-1c, reaction with (+)-2-bromo-3-(4-nitrophenyl)propanoic acid


proof_lines: mutant enzyme I10C, at 30°C in 250 mM Tris-HCl buffer, pH 7.2


proof_lines: mutant enzyme G112C, at 30°C in 250 mM Tris-HCl buffer, pH 7.2


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant M91A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant K62E


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant W126A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant Y18F


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant L88A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant F83W


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant L15A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant F83A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant K62A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature S19A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant S19A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature F87A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant F87A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature M91K to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant M91K


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature N53A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant N53A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature R202A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant R202A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature D69A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant D69A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature F87W to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant F87W


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature P56A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant P56A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature I44A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant I44A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature L58A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant L58A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature P17A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant P17A


sequence_variant_note: Resolved canonical sequence from UniProtKB Q9Y2Q3 canonical sequence; RCSB 3RPN/3RPP linked to PMID 21728995; BRENDA row mutation note and applied mutation signature S200A to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, 25°C, recombinant GSTk mutant S200A


organism: Penaeus vannamei


organism: Phanerodontia chrysosporium

substrate_name: S-phenylacetylglutathione

substrate: S-phenylacetylglutathione


organism: Pinus tabuliformis


organism: Plasmodium yoelii


organism: Plutella xylostella

substrate_name: Ethacrynic acid


organism: Proteus mirabilis


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant P55A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant D201A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant D69T


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant S16A


proof_lines: pH 7.4, 25°C, recombinant GSTk mutant L183A


proof_lines: 30°C, mutant enzyme Y108F, reaction with 1,2-dichloro-4-nitrobenzene

proof_lines: 30°C, mutant enzyme Y108F, reaction with 1,2-epoxy-3-(p-nitrophenoxy)propane


proof_lines: 30°C, mutant enzyme Y108A, reaction with 1,2-epoxy-3-(p-nitrophenoxy)propane

proof_lines: 30°C, mutant enzyme Y108A, reaction with 1,2-dichloro-4-nitrobenzene


proof_lines: 30°C, mutant enzyme Y108W, reaction with 1,2-epoxy-3-(p-nitrophenoxy)propane

proof_lines: 30°C, mutant enzyme Y108W, reaction with 1,2-dichloro-4-nitrobenzene


organism: Lathyrus oleraceus

substrate_name: fluorodifen

substrate: fluorodifen


organism: Lepidochelys olivacea


organism: Liposcelis bostrychophila

proof_lines: in phosphate buffer (0.1 M, pH 6.5), at 25°C


organism: Liposcelis entomophila


organism: Rattus norvegicus


organism: Rhodotorula mucilaginosa


organism: Saccharomyces cerevisiae


proof_lines: Ure2p mutant A122C, at 25°C and pH 8.0, in the presence of 1 mM dithiothreitol


organism: Schistocerca gregaria


organism: Schistosoma japonicum


assay_conditions_summary: pH 7; 298.15 K; buffer pH 7

proof_lines: 25°C, 20 mM sodium phosphate buffer, pH 7.0, 0.5 mM glutathione

proof_lines: 4°C, 20 mM sodium phosphate buffer, pH 6.5, 0.5 mM glutathione


organism: Schistosoma mansoni

substrate_name: hydroxyethyldisulfide

substrate: hydroxyethyldisulfide


organism: Setaria cervi


organism: Setaria faberi

substrate_name: metolachlor

substrate: metolachlor


organism: Solenopsis invicta

sequence_source: UniProtKB Q6X4T7 FASTA; entry references PMID 14505691

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


organism: Spinacia oleracea

substrate_name: acrolein


organism: Sus scrofa


organism: Synechococcus elongatus

proof_lines: at 30°C in 0.1 M potassium phosphate buffer


organism: Synechocystis sp.


organism: Syrphus ribesii


organism: Taenia crassiceps

proof_lines:
isoform GST1, at pH 8.5 and 25°C
isoform GST2, at pH 7.5 and 25°C
isoform GST2, at pH 8.5 and 25°C


organism: Taenia solium

substrate: Unknown


organism: Tetranychus urticae

proof_lines:
isoform GSTd14, at pH 6.5 and 25°C
isoform GSTd10, at pH 6.5 and 25°C
isoform GSTm09, at pH 6.5 and 25°C


organism: Trachemys scripta elegans

proof_lines:
heterodimeric enzyme
homodimeric enzyme


organism: Trichinella spiralis


organism: Proteus mirabilis


organism: Pseudomonas putida


organism: Rattus norvegicus


proof_lines: pH 6.5, 25°C, recombinant wild-type enzyme


organism: Triticum aestivum

proof_lines: pH 6.5, 35°C, in presence of cloquintocet-mexyl


organism: Zea mays

proof_lines: mutant enzyme T12I, reaction with 1-chloro-2,3-dinitrobenzoate

proof_lines: mutant enzyme T12I, reaction with ethacrynic acid


proof_lines: mutant enzyme T12P, reaction with ethacrynic acid

proof_lines: mutant enzyme T12P, reaction with 1-chloro-2,3-dinitrobenzoate


substrate_name: alachlor

proof_lines: mutant enzyme F35L, reaction with 1-chloro-2,3-dinitrobenzoate

substrate: alachlor


proof_lines: pH 6.5, 30°C, recombinant wild-type enzyme

proof_lines: wild-type enzyme GST I, reaction with 1-chloro-2,3-dinitrobenzoate


proof_lines: mutant enzyme I118F, reaction with 1-chloro-2,3-dinitrobenzoate


organism: Liposcelis paeta

proof_lines: pH 7.5, 37°C, enzyme of Wuzhou population

proof_lines: pH 7.5, 37°C, enzymes of Hezhou and Nanyang population

proof_lines: pH 7.5, 37°C, enzyme of Nanyang population


organism: Lucilia cuprina

proof_lines: Y113F mutant, cosubstrate: 1-chloro-2,4-dinitrobenzene


proof_lines: S9A mutant, cosubstrate: 1-chloro-2,4-dinitrobenzene


organism: Macaca mulatta


organism: Macrobrachium vollenhovenii


organism: Monopterus albus


organism: Mucor mucedo

assay_conditions_summary: pH 8

proof_lines: pH 8.0, substrate concentration 0.1-0.3 mM

proof_lines: pH 8.0, substrate concentration 0.3-2.0 mM


organism: Mus musculus

proof_lines: pH 6.5, 25°C, recombinant catalytically active monoclonal antibody fragment ScFv2F3


proof_lines: pH 7.4, 37°C, recombinant mutant F2:1215


organism: Myathropa florea


organism: Paraburkholderia xenovorans

proof_lines: pH 6.5, 25°C, recombinant enzyme, with (2E,4Z)-5-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid

proof_lines: pH 6.5, 25°C, recombinant enzyme, with (2Z,4E)-3-chloro-6-(3,5-dichlorophenyl)-2-hydroxy-6-oxohexa-2,4-dienoic acid

proof_lines: pH 6.5, 25°C, recombinant enzyme, with (2Z,4E)-3-chloro-2-hydroxy-6-oxo-6-phenylhexa-2,4-dienoic acid


enzyme_display_name: tyrosinase

organism: Lentinula edodes

substrate_name: L-Dopa

proof_lines:
isoenzyme A2
isozyme A2, at pH 6.0 and 30°C
isoenzyme A3

enzyme: tyrosinase

substrate: L-Dopa


organism: Metroxylon sagu

substrate_name: D-catechin

proof_lines:
isoenzyme III
isoenzyme I

substrate: D-catechin


organism: Pinus densiflora

proof_lines:
isoenzyme 3
isoenzyme 1
isoenzyme 2


organism: Unknown

substrate_name: phenol

substrate: phenol


organism: Vibrio tyrosinaticus

substrate_name: L-tyrosine

proof_lines:
isoenzyme A and B
isoenzyme B
isoenzyme A

substrate: L-tyrosine


organism: Agaricus bisporus

substrate_name: L-ascorbic acid

assay_conditions_summary: pH 7; 298.15 K; buffer phosphate

proof_lines: pH and temperature not specified in the publication

substrate: L-ascorbic acid


organism: Amorphophallus paeoniifolius var. campanulatus

substrate_name: dopamine

proof_lines: using tyrosinase immobilized on eggshell membrane. Km is 0.67 mM and Vmax 0.08 mM min-1. Increase in Km (compared to soluble enzyme for which Km is 0.20 mM) indicate that the affinity of enzyme for substrate has decreased to some extent aft

substrate: dopamine


organism: Anethum graveolens

substrate_name: catechol

proof_lines: PPO of dill has a great affinity towards chlorogenic acid. calculated from the Lineweaver-Burk graphs for substrates

substrate: catechol


organism: Aspergillus nidulans

substrate_name: Hydroquinone monomethylether

proof_lines: range of estimated values for crude or purified extracts

substrate: Hydroquinone monomethylether


organism: Bacillus thuringiensis


organism: Bactris gasipaes

substrate_name: chlorogenic acid

substrate: chlorogenic acid