enzyme_display_name: monodehydroascorbate reductase (NADH)

organism: Solanum lycopersicum

substrate_name: NADH

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

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

proof_lines: mutant enzyme C117A, in 50 mM Tris-HCl (pH 7.5), at 25°C

enzyme: monodehydroascorbate reductase (NADH)

substrate: NADH


source_db: brenda

verification_status: unverified

ki_display: Not reported

kcat_over_km_display: Not reported

source_license: CC BY 4.0

km_unit: mM

mutation_type: substitution

proof_lines: mutant enzyme C117S, in 50 mM Tris-HCl (pH 7.5), at 25°C

status: unverified

source: brenda


mutation_signature: Unknown

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

proof_lines: recombinant wild type enzyme, in 50 mM Tris-HCl (pH 7.5), at 25°C

proof_lines: native wild type enzyme, in 50 mM Tris-HCl (pH 7.5), at 25°C


substrate_name: monodehydroascorbate

kcat_display: Not reported

substrate: monodehydroascorbate


enzyme_display_name: nitroalkane oxidase

organism: Fusarium oxysporum

protein_accession_database: UniProt

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

smiles: O=O

data_origin: experimental

enzyme: nitroalkane oxidase


enzyme_display_name: NADPH dehydrogenase

organism: Bacillus subtilis

proof_lines:
pH 7.5, 25°C, GST-fusion protein
pH 7.5, 25°C, native protein
pH 7.5, 25°C

enzyme: NADPH dehydrogenase


substrate_name: N-ethylmaleimide

substrate: N-ethylmaleimide


substrate_name: nitroglycerin

substrate: nitroglycerin


smiles: CCCC=CC=O


enzyme_display_name: nitrite reductase (NADH)

organism: Escherichia coli

substrate_name: cytochrome c

assay_conditions_summary: pH 8; 303.15 K; cofactor NADH

enzyme: nitrite reductase (NADH)

substrate: cytochrome c


substrate_name: nitrite

substrate: nitrite


proof_lines: with cytochrome c as cosubstrate, apparent value, at pH 8.0 and 30°C


substrate_name: hydroxylamine

smiles: NO

substrate: hydroxylamine


enzyme_display_name: cytochrome-b5 reductase

organism: Homo sapiens

enzyme: cytochrome-b5 reductase


substrate_name: Nitrofurantoin

substrate: Nitrofurantoin


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

organism: Pseudomonas putida

substrate_name: chromate(IV)

enzyme: NAD(P)H dehydrogenase (quinone)

substrate: chromate(IV)


substrate_name: coenzyme Q1

substrate: coenzyme Q1


substrate_name: duroquinone

substrate: duroquinone


substrate_name: menadione

substrate: menadione


substrate_name: benzoquinone

substrate: benzoquinone


enzyme_display_name: dihydrolipoyl dehydrogenase

organism: Thermoplasma acidophilum

substrate_name: NAD+

enzyme: dihydrolipoyl dehydrogenase

substrate: NAD+


substrate_name: dihydrolipoamide

smiles: C(CCC(=O)N)CC(CCS)S

substrate: dihydrolipoamide


source_db: oed

kcat_over_km_origin: calculated

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L99A with inferred residue-numbering offset +35 to reconstruct the assayed variant sequence.

smiles: N=C(O)CCCCC(S)CCS

source: oed


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P156A with inferred residue-numbering offset +35 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P303A with inferred residue-numbering offset +35 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P355A with inferred residue-numbering offset +35 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C50A with inferred residue-numbering offset +35 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -5, so it is treated as a source-provided variant sequence.


enzyme_display_name: UniProt Q56839

organism: Xanthobacter autotrophicus

source_db: skid

source_license: CC BY-NC-ND 4.0

smiles: CC(=O)CSCCS(=O)(=O)O

enzyme: UniProt Q56839

source: skid


enzyme_display_name: glutathione-disulfide reductase

organism: Phycomyces blakesleeanus

substrate_name: NADPH

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

enzyme: glutathione-disulfide reductase

substrate: NADPH


organism: Acidithiobacillus ferrooxidans


substrate_name: GSSG

substrate: GSSG


enzyme_display_name: UniProt P00390

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.5
Raw SKiD Env: Temp=25°C, pH=7.4

enzyme: UniProt P00390


substrate_name: trypanothione

substrate: trypanothione


enzyme_display_name: UniProt P41921

organism: Saccharomyces cerevisiae

enzyme: UniProt P41921


enzyme_display_name: azobenzene reductase

organism: Pseudomonas sp.

assay_conditions_summary: cofactor NADPH

enzyme: azobenzene reductase


substrate_name: NADH

substrate: NADH


organism: Cucumis sativus


assay_conditions_summary: cofactor NADH


substrate_name: ferricyanide

substrate: ferricyanide


assay_conditions_summary: pH 7; 298.15 K; cofactor NADH


organism: Bos taurus

proof_lines:
cofactor NADH
cofactor NADPH


substrate_name: methylene blue

substrate: methylene blue


substrate_name: vitamin K1

proof_lines:
cofactor NADPH
cofactor NADH

substrate: vitamin K1


substrate_name: potassium ferricyanide

substrate: potassium ferricyanide


organism: Lathyrus oleraceus

proof_lines: maltose-binding protein-monodehydroascorbate reductase fusion protein


substrate_name: monodehydroascorbate

substrate: monodehydroascorbate


substrate_name: oxidized 2,6-dichlorophenolindophenol

substrate: oxidized 2,6-dichlorophenolindophenol


proof_lines: wild-type, cosubstrate ferricyanide, 25°C, pH 7.0


proof_lines: mutant P275L, cosubstrate ferricyanide, 25°C, pH 7.0


substrate_name: ferricytochrome b5

substrate: ferricytochrome b5


enzyme_display_name: nitrite reductase (NO-forming)

organism: Alcaligenes faecalis

substrate_name: NO

km_display: Not reported

smiles: [No]

enzyme: nitrite reductase (NO-forming)

substrate: NO


substrate_name: nitrite

substrate: nitrite


substrate_name: reduced pseudoazurin

substrate: reduced pseudoazurin


enzyme_display_name: UniProt Q9JLT4

organism: Mus musculus

substrate_name: hydrogen peroxide

smiles: OO

enzyme: UniProt Q9JLT4

substrate: hydrogen peroxide


enzyme_display_name: UniProt P39051

organism: Trypanosoma brucei

substrate_name: trypanothione disulfide

enzyme: UniProt P39051

substrate: trypanothione disulfide


enzyme_display_name: Trypanothione reductase

organism: Trypanosoma congolense

source_db: uniprot

enzyme: Trypanothione reductase

source: uniprot


enzyme_display_name: UniProt Q72HK3

organism: Thermus thermophilus

enzyme: UniProt Q72HK3


substrate_name: CoA-disulfide

substrate: CoA-disulfide


enzyme_display_name: Coenzyme A disulfide reductase

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

substrate_name: NADPH

enzyme: Coenzyme A disulfide reductase

substrate: NADPH


substrate_name: CoA disulfide

substrate: CoA disulfide


organism: Rattus norvegicus

substrate_name: ferricytochome b5

substrate: ferricytochome b5


enzyme_display_name: NADPH-hemoprotein reductase

organism: Arabidopsis thaliana

substrate_name: ferricytochrome c

enzyme: NADPH-hemoprotein reductase

substrate: ferricytochrome c


substrate_name: ferricyanide

substrate: ferricyanide


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH


organism: Trypanosoma cruzi

substrate_name: menadione

substrate: menadione


assay_conditions_summary: pH 7.7; 303.15 K; cofactor NADPH


enzyme_display_name: sulfite dehydrogenase (cytochrome)

organism: Ancylobacter novellus

assay_conditions_summary: pH 8

enzyme: sulfite dehydrogenase (cytochrome)


enzyme_display_name: monodehydroascorbate reductase (NADH)

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

enzyme: monodehydroascorbate reductase (NADH)


enzyme_display_name: cytochrome-b5 reductase

organism: Brassica napus

substrate_name: NADH

enzyme: cytochrome-b5 reductase

substrate: NADH


enzyme_display_name: GMP reductase

substrate_name: GMP

enzyme: GMP reductase

substrate: GMP


substrate_name: Unknown

ki_unit: mM

substrate: Unknown


organism: Canis lupus familiaris

substrate_name: ferrocytochrome b5

substrate: ferrocytochrome b5


enzyme_display_name: UniProt D3RVD4

organism: Allochromatium vinosum

substrate_name: tetrathionate

enzyme: UniProt D3RVD4

substrate: tetrathionate


enzyme_display_name: sulfite oxidase

substrate_name: sulfite

enzyme: sulfite oxidase

substrate: sulfite


enzyme_display_name: UniProt P07850

organism: Gallus gallus

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.5
Raw SKiD Env: Temp=25°C, pH=7

enzyme: UniProt P07850


enzyme_display_name: Sulfite oxidase

substrate_name: sulfite (at pH 8.0 and 25 degrees Celsius)

enzyme: Sulfite oxidase


enzyme_display_name: nitrite reductase (cytochrome; ammonia-forming)

organism: Escherichia coli

substrate_name: nitrite

proof_lines:
pH 7.0, 20°C, reduction
at pH 7.0

substrate: nitrite


substrate_name: NO radical

enzyme: nitrite reductase (cytochrome; ammonia-forming)

substrate: NO radical


substrate_name: hydroxylamine

substrate: hydroxylamine


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

proof_lines: pH 7.0, 25°C, wild-type enzyme with methyl viologen as reductant


assay_conditions_summary: pH 7

proof_lines: mutant H264N, pH 7.0, temperature not specified in the publication


enzyme_display_name: nitrite reductase [NAD(P)H]

enzyme: nitrite reductase [NAD(P)H]


assay_conditions_summary: cofactor NAD+


enzyme_display_name: methanethiol oxidase

organism: Hyphomicrobium sp.

substrate_name: ethyl mercaptan

smiles: CCS

enzyme: methanethiol oxidase

substrate: ethyl mercaptan


substrate_name: Sulfide

substrate: Sulfide


organism: Bos taurus

substrate_name: Insulin

substrate: Insulin


enzyme_display_name: NADPH---hemoprotein reductase

substrate_name: Cytochrome c; NADPH; H+

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

proof_lines:
mitochondrial reductase
microsomal reductase

enzyme: NADPH---hemoprotein reductase

substrate: Cytochrome c; NADPH; H+


substrate_name: NADPH

substrate: NADPH


proof_lines:
microsomal reductase
mitochondrial reductase


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

organism: Hevea brasiliensis

assay_conditions_summary: pH 8; cofactor NADH

proof_lines:
pH 8.0, reaction with plumbagin
pH 8.0, reaction with menadione
pH 8.0, reaction with juglone

enzyme: NAD(P)H dehydrogenase (quinone)


assay_conditions_summary: pH 8; cofactor NADPH

proof_lines:
pH 8.0, reaction with plumbagin
pH 8.0, reaction with juglone
pH 8.0, reaction with menadione


substrate_name: duroquinone

substrate: duroquinone


organism: Homo sapiens

substrate_name: sulfamethoxazole hydroxylamine

substrate: sulfamethoxazole hydroxylamine


substrate_name: dapsone hydroxylamine

substrate: dapsone hydroxylamine


substrate_name: benzamidoxime

substrate: benzamidoxime


assay_conditions_summary: pH 7; cofactor NADPH


substrate_name: NADH

assay_conditions_summary: pH 7; cofactor NADH

substrate: NADH


substrate_name: ferricytochrome c

proof_lines:
at pH 7.5 and 25°C
pH 7.0, 25°C

substrate: ferricytochrome c


substrate_name: ferricyanide

substrate: ferricyanide


enzyme_display_name: UniProt A8MI53

organism: Alkaliphilus oremlandii

substrate_name: dithiothreitol

smiles: C(C(C(CS)O)O)S

enzyme: UniProt A8MI53

substrate: dithiothreitol


enzyme_display_name: NADPH dehydrogenase (quinone)

organism: Pseudomonas aeruginosa

assay_conditions_summary: pH 6; 298.15 K; cofactor NADPH

enzyme: NADPH dehydrogenase (quinone)


substrate_name: ferricytochrome b5

assay_conditions_summary: cofactor FAD

proof_lines: cytochrome b5/cytochrome b5 reductase FAD-domain fusion protein

substrate: ferricytochrome b5


enzyme_display_name: nitrite reductase (NO-forming)

organism: Ralstonia pickettii

substrate_name: nitrite

enzyme: nitrite reductase (NO-forming)

substrate: nitrite


proof_lines: core protein carrying mutation Y327F, pH 6.5, 25°C


enzyme_display_name: UniProt Q9HJW5

organism: Thermoplasma acidophilum

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

smiles: CS(=O)CCC(C(=O)O)N

enzyme: UniProt Q9HJW5

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


enzyme_display_name: UniProt P76270

enzyme: UniProt P76270


enzyme_display_name: UniProt P78417

substrate_name: glutathione

smiles: C(CC(=O)NC(CS)C(=O)NCC(=O)O)C(C(=O)O)N

enzyme: UniProt P78417

substrate: glutathione


enzyme_display_name: UniProt Q65XA0

organism: Oryza sativa Japonica Group

enzyme: UniProt Q65XA0


enzyme_display_name: UniProt Q9H4Y5

substrate_name: dehydroascorbate

enzyme: UniProt Q9H4Y5

substrate: dehydroascorbate


enzyme_display_name: UniProt Q57366

organism: Cereibacter sphaeroides

substrate_name: Dimethylsulfoxide

smiles: CS(=O)C

assay_conditions_summary: pH 6

enzyme: UniProt Q57366

substrate: Dimethylsulfoxide


enzyme_display_name: cytochrome-b5 reductase

organism: Rattus norvegicus

enzyme: cytochrome-b5 reductase


proof_lines: pH 7.0, S127P mutant enzyme with cytochrome b5 as substrate

proof_lines: pH 7.0, S127P mutant enzyme with ferricyanide as substrate


organism: Saccharomyces cerevisiae

assay_conditions_summary: pH 6; buffer 50 mM sodium phosphate

proof_lines: in 50 mM sodium phosphate buffer (pH 6.0) and 1 mM EDTA, temperature not specified in the publication


assay_conditions_summary: pH 6; 298.15 K; buffer 50 mM sodium phosphate; cofactor NADH

proof_lines: hyperbolic uncompetitive inhibition of NADH, pH 7.0, 25°C

proof_lines: hyperbolic noncompetitive inhibition of 2,6-dichlorophenolindophenol, pH 7.0, 25°C


enzyme_display_name: UniProt B7JBP8

organism: Acidithiobacillus ferrooxidans

substrate_name: Sulfide

proof_lines:
Raw SKiD Env: Temp=23°C, pH=7
Raw SKiD Env: Temp=-----, pH=6.5

enzyme: UniProt B7JBP8

substrate: Sulfide


enzyme_display_name: UniProt Q9Y6N5

proof_lines:
Raw SKiD Env: Temp=25°C, pH=6.8
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=25°C, pH=8.5

enzyme: UniProt Q9Y6N5


proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.5
Raw SKiD Env: Temp=25°C, pH=7.5


substrate_name: sulfite

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=25°C, pH=8

substrate: sulfite


substrate_name: cyanide

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8.5
Raw SKiD Env: Temp=25°C, pH=8

substrate: cyanide


enzyme_display_name: UniProt O67931

organism: Aquifex aeolicus

proof_lines:
Raw SKiD Env: Temp=-----, pH=7.4
Raw SKiD Env: Temp=40°C, pH=7.4

enzyme: UniProt O67931


substrate_name: decylubiquinone

substrate: decylubiquinone


enzyme_display_name: glutathionyl-hydroquinone reductase

organism: Sphingobium chlorophenolicum

enzyme: glutathionyl-hydroquinone reductase


enzyme_display_name: UniProt P42620

proof_lines:
Raw SKiD Env: Temp=23°C, pH=8
Raw SKiD Env: Temp=-----, pH=7.5

enzyme: UniProt P42620


enzyme_display_name: assimilatory sulfite reductase (ferredoxin)

organism: Spinacia oleracea

substrate_name: reduced methyl viologen

substrate: reduced methyl viologen


organism: Limnospira platensis

enzyme: assimilatory sulfite reductase (ferredoxin)


substrate_name: S-Sulfoglutathione

substrate: S-Sulfoglutathione


enzyme_display_name: adenylyl-sulfate reductase

organism: Megalodesulfovibrio gigas

enzyme: adenylyl-sulfate reductase


organism: Prosthecochloris vibrioformis

substrate_name: AMP

substrate: AMP


substrate_name: adenylyl sulfate

substrate: adenylyl sulfate


enzyme_display_name: bacterial sulfide:quinone reductase

organism: Unknown

substrate_name: Unknown

source_db: unknown

source_license: see source

enzyme: bacterial sulfide:quinone reductase

substrate: Unknown

source: unknown


organism: Thiocapsa roseopersicina

substrate_name: cytochrome c

substrate: cytochrome c


proof_lines:
reaction with ferricyanide
reaction with cytochrome c


substrate_name: ferricyanide

substrate: ferricyanide


organism: Thiobacillus thioparus

proof_lines:
reaction with cytochrome c
reaction with ferricyanide


substrate_name: GMP

substrate: GMP


organism: Allochromatium vinosum


enzyme_display_name: thioredoxin-disulfide reductase (factor 420-dependent)

organism: Methanococcus aeolicus

substrate_name: NADPH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: a reduced factor 420

enzyme: thioredoxin-disulfide reductase (factor 420-dependent)

substrate: a reduced factor 420


organism: archaebacterium


organism: Bacillus subtilis

substrate_name: reduced glutaredoxin 1

substrate: reduced glutaredoxin 1


proof_lines:
pH 8 and saturating thioredoxin 1
pH 8 and saturating glutaredoxin 1


organism: Maridesulfovibrio salexigens


organism: Ulva intestinalis


substrate_name: GSH

substrate: GSH


organism: Methanocaldococcus jannaschii

substrate_name: thioredoxin 1

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

substrate: thioredoxin 1


substrate_name: reduced coenzyme F420

substrate: reduced coenzyme F420


organism: Pseudomonas aeruginosa

substrate_name: thioredoxin

proof_lines: thioredoxin originating from Clamydomonas reinhardtii

proof_lines: thioredoxin originating from Escherichia coli

substrate: thioredoxin


organism: Desulfovibrio gigas

substrate_name: AMP; Hexacyanoferrate(III); Sulfite

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

substrate: AMP; Hexacyanoferrate(III); Sulfite


substrate_name: sulfite

sequence_source: multiple

proof_lines:
adenylylsulfate reductase
Desulfovibrio gigas
redox centers

source_databases_merged: brenda uniprot

substrate: sulfite


substrate_name: dithiothreitol

substrate: dithiothreitol


organism: Nitratidesulfovibrio vulgaris


substrate_name: guanylyl sulfate

substrate: guanylyl sulfate


substrate_name: IMP

substrate: IMP


substrate_name: CMP

substrate: CMP


substrate_name: UMP

substrate: UMP


organism: Bos taurus

assay_conditions_summary: cofactor NADH


substrate_name: ferricytochrome b5

assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADH

substrate: ferricytochrome b5


organism: Methanococcus voltae

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


enzyme_display_name: nitrite reductase (cytochrome; ammonia-forming)

organism: Desulfovibrio desulfuricans

substrate_name: reduced phenosafranine

proof_lines: apparent value, in 0.2 M phosphate buffer pH 7.6, at 37°C

substrate: reduced phenosafranine


substrate_name: reduced methyl viologen

enzyme: nitrite reductase (cytochrome; ammonia-forming)

substrate: reduced methyl viologen


enzyme_display_name: FMN-dependent NADH-azoreductase

organism: Escherichia coli

assay_conditions_summary: pH 7.4; 303.15 K; cofactor FMN

proof_lines: cofactor roseoflavin mononucleotide, pH 7.4, 30°C

enzyme: FMN-dependent NADH-azoreductase


substrate_name: NADH

assay_conditions_summary: pH 7.4; 303.15 K; cofactor NADH

proof_lines:
recombinant enzyme, pH 7.4, 30°C
pH 7.4, 30°C
cofactor FMN, pH 7.4, 30°C

substrate: NADH


enzyme_display_name: GMP reductase

substrate_name: guanosine 5'-phosphate

enzyme: GMP reductase

substrate: guanosine 5'-phosphate


substrate_name: NADPH

assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: Adenylylsulfate reductase subunit alpha

organism: Megalodesulfovibrio gigas (strain ATCC 19364 / DSM 1382 / NCIMB 9332 / VKM B-1759)

substrate_name: AMP

enzyme: Adenylylsulfate reductase subunit alpha

substrate: AMP


enzyme_display_name: preQ1 synthase

proof_lines:
pH 7.5, 25°C
pH 7.0, 37°C
below 1 microM, pH 7.5, 25°C

enzyme: preQ1 synthase


enzyme_display_name: NADPH dehydrogenase (quinone)

substrate_name: menadione

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

enzyme: NADPH dehydrogenase (quinone)

substrate: menadione


organism: Escherichia coli K-12

substrate_name: nitrite

substrate: nitrite


substrate_name: hydroxylamine

substrate: hydroxylamine


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH


enzyme_display_name: nitrate reductase (NADH)

organism: Glycine max

enzyme: nitrate reductase (NADH)


assay_conditions_summary: cofactor NADPH


enzyme_display_name: NADPH:quinone reductase

organism: Homo sapiens

enzyme: NADPH:quinone reductase


assay_conditions_summary: pH 7.5; cofactor NADPH


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

enzyme: NAD(P)H dehydrogenase (quinone)


enzyme_display_name: monodehydroascorbate reductase (NADH)

organism: Hordeum vulgare

enzyme: monodehydroascorbate reductase (NADH)


substrate_name: monodehydroascorbate

substrate: monodehydroascorbate


enzyme_display_name: cytochrome-b5 reductase

organism: Lathyrus oleraceus

substrate_name: ferricyanide

enzyme: cytochrome-b5 reductase

substrate: ferricyanide


organism: Lysinibacillus sphaericus

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADH


substrate_name: Amaranth

substrate: Amaranth


substrate_name: sulfite

substrate: sulfite


enzyme_display_name: nitrite reductase (NO-forming)

enzyme: nitrite reductase (NO-forming)


organism: Physcomitrium patens


substrate_name: ferricytochrome c

assay_conditions_summary: pH 7

proof_lines:
succinylated monomeric enzyme
at pH 7.0
also known as cytochrome c8

substrate: ferricytochrome c


enzyme_display_name: azobenzene reductase

organism: Pseudomonas sp. B1

substrate_name: naphthol blue black

enzyme: azobenzene reductase

substrate: naphthol blue black


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


organism: Rattus norvegicus

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


substrate_name: dichlorophenolindophenol

substrate: dichlorophenolindophenol


enzyme_display_name: NADPH-hemoprotein reductase

organism: Saccharomyces cerevisiae

substrate_name: cytochrome c

enzyme: NADPH-hemoprotein reductase

substrate: cytochrome c


substrate_name: ferricytochrome b5

proof_lines:
yeast cytochrome b5
calf cytochrome b5

substrate: ferricytochrome b5


enzyme_display_name: UniProt Q9ZP19

organism: Ipomoea batatas

substrate_name: catechol

enzyme: UniProt Q9ZP19

substrate: catechol


substrate_name: 2,3,4-trihydroxybenzoic acid

substrate: 2,3,4-trihydroxybenzoic acid


substrate_name: 3,4-dihydroxyphenylacetic acid

substrate: 3,4-dihydroxyphenylacetic acid


enzyme_display_name: laccase

organism: Shiraia sp. SUPER-H168

substrate_name: guaiacol

enzyme: laccase

substrate: guaiacol


substrate_name: syringaldazine

substrate: syringaldazine


enzyme_display_name: UniProt Q96UT7

organism: Trametes versicolor

enzyme: UniProt Q96UT7


organism: Thermobaculum terrenum


organism: Ganoderma fornicatum


organism: Bacillus sp. (in: Bacteria)

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E188A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E188I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E188K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E188L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E188R to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E188V to reconstruct the assayed variant sequence.


organism: Coriolopsis trogii


organism: Bacillus amyloliquefaciens

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D501G to reconstruct the assayed variant sequence.


organism: Bacillus licheniformis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D500G to reconstruct the assayed variant sequence.


organism: Escherichia coli

sequence_variant_note: Mutation signature G276K could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature G276N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


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


sequence_variant_note: Mutation signature G276Y could not be applied safely because the resolved sequence does not match the expected reference residue(s).


organism: Galerina sp. DSM 22662

sequence: GPSTDLVIGNKGFDGGIDSAILR

wild_type_sequence: GPSTDLVIGNKGFDGGIDSAILR

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


organism: Meiothermus ruber


organism: Ochrobactrum sp. 531


organism: Stenotrophomonas maltophilia


organism: Streptomyces sp. C1


organism: Klebsiella pneumoniae


substrate_name: Guaiacol

substrate: Guaiacol


substrate_name: L-Dopa

substrate: L-Dopa


substrate_name: Syringaldazine

substrate: Syringaldazine


enzyme_display_name: Laccase

organism: Lepiota magnispora

substrate_name: ABTS (at pH 4)

sequence: VTIGKEGTLT

wild_type_sequence: VTIGKEGTLT

enzyme: Laccase

substrate: ABTS (at pH 4)


substrate_name: catechol (at pH 4)

substrate: catechol (at pH 4)


substrate_name: hydroquinone (at pH 4)

substrate: hydroquinone (at pH 4)


organism: Galerina sp

substrate_name: ABTS

substrate: ABTS


organism: Cerrena unicolor

sequence: AIGPVADLHI

wild_type_sequence: AIGPVADLHI


sequence: AIGPVADLH

wild_type_sequence: AIGPVADLH


organism: Solanum tuberosum

substrate_name: NADH

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

substrate: NADH


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: nitrous-oxide reductase

organism: Pseudomonas aeruginosa

enzyme: nitrous-oxide reductase


substrate_name: benzyl viologen cation radical

substrate: benzyl viologen cation radical


organism: Spinacia oleracea


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: UniProt Q26710

organism: Trypanosoma brucei brucei

proof_lines:
Raw SKiD Env: Temp=25°C, pH=7.5
Raw SKiD Env: Temp=-----, pH=7.4

enzyme: UniProt Q26710


proof_lines:
Raw SKiD Env: Temp=-----, pH=7.4
Raw SKiD Env: Temp=25°C, pH=7.5


organism: Triticum aestivum


substrate_name: nitrate

substrate: nitrate


enzyme_display_name: UniProt P37062

organism: Enterococcus faecalis

enzyme: UniProt P37062


organism: Sus scrofa

substrate_name: ferricytochrome c

proof_lines: spleen kidney

substrate: ferricytochrome c


proof_lines: kidney spleen


organism: Zea mays


substrate_name: ferricyanide

substrate: ferricyanide


organism: Achromobacter xylosoxidans

substrate_name: nitrite

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

substrate: nitrite


enzyme_display_name: nitric oxide reductase (cytochrome c)

organism: Stutzerimonas stutzeri

substrate_name: phenazine methosulfate

enzyme: nitric oxide reductase (cytochrome c)

substrate: phenazine methosulfate


substrate_name: NO

substrate: NO


organism: Alcaligenes faecalis


enzyme_display_name: adenylyl-sulfate reductase

organism: Archaeoglobus fulgidus

substrate_name: adenylyl sulfate

enzyme: adenylyl-sulfate reductase

substrate: adenylyl sulfate


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.8; cofactor NADPH

proof_lines: pH 7.8, temperature not specified in the publication


substrate_name: sulfite

substrate: sulfite


organism: Bos taurus


enzyme_display_name: nitrite reductase (cytochrome; ammonia-forming)

organism: Desulfovibrio desulfuricans

assay_conditions_summary: pH 7.6; 293.15 K; buffer phosphate


organism: Equus caballus

substrate_name: cytochrome c

substrate: cytochrome c


enzyme_display_name: trimethylamine-N-oxide reductase

organism: Escherichia coli

substrate_name: biotin sulfoxide

enzyme: trimethylamine-N-oxide reductase

substrate: biotin sulfoxide


proof_lines: pH 7.0, 25°C, mutant Q263E with methyl viologen as reductant

enzyme: nitrite reductase (cytochrome; ammonia-forming)


enzyme_display_name: UniProt P00431

organism: Saccharomyces cerevisiae

substrate_name: guaiacol

enzyme: UniProt P00431

substrate: guaiacol


substrate_name: ascorbate

substrate: ascorbate


enzyme_display_name: UniProt P00433

organism: Armoracia rusticana

proof_lines:
Raw SKiD Env: Temp=-----, pH=6
Raw SKiD Env: Temp=30°C, pH=6.5

enzyme: UniProt P00433


enzyme_display_name: UniProt Q9NAV8

organism: Amphitrite ornata

enzyme: UniProt Q9NAV8


enzyme_display_name: glutathione peroxidase

organism: Thunnus maccoyii

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

enzyme: glutathione peroxidase


substrate_name: cumene peroxide

substrate: cumene peroxide


substrate_name: tert-butyl hydroperoxide

smiles: CC(C)(C)OO

substrate: tert-butyl hydroperoxide


substrate_name: GSH

substrate: GSH


organism: Homo sapiens

substrate_name: glutathione

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C2S/C78S/C115S/C156S/C202S to reconstruct the assayed variant sequence.

substrate: glutathione


enzyme_display_name: UniProt P04963

organism: Leptoxyphium fumago

substrate_name: equiline

assay_conditions_summary: pH 3

enzyme: UniProt P04963

substrate: equiline


substrate_name: estrone

substrate: estrone


substrate_name: beta-estradiol

substrate: beta-estradiol


substrate_name: nitric oxide

substrate: nitric oxide


enzyme_display_name: preQ1 synthase

substrate_name: NADPH

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

proof_lines:
pH 7.0, 37°C
or below, pH 7.0, 37°C
pH 7.5, 25°C

enzyme: preQ1 synthase

substrate: NADPH


enzyme_display_name: FMN-dependent NADH-azoreductase

enzyme: FMN-dependent NADH-azoreductase


enzyme_display_name: NADPH-hemoprotein reductase

organism: Fusarium graminearum

substrate_name: ferricytochrome c

proof_lines:
at pH 8.5 and 23°C
at pH 7.5 and 23°C
at pH 9.5 and 23°C

enzyme: NADPH-hemoprotein reductase

substrate: ferricytochrome c


enzyme_display_name: nitrite reductase (NO-forming)

organism: Cupriavidus necator

enzyme: nitrite reductase (NO-forming)


enzyme_display_name: NAD(P)H dehydrogenase (quinone)

substrate_name: mitomycin C

enzyme: NAD(P)H dehydrogenase (quinone)

substrate: mitomycin C


enzyme_display_name: nitrate reductase (NADH)

organism: Glycine max

substrate_name: nitrate

enzyme: nitrate reductase (NADH)

substrate: nitrate


enzyme_display_name: cytochrome-b5 reductase

assay_conditions_summary: pH 7.4; cofactor NADH

enzyme: cytochrome-b5 reductase


enzyme_display_name: GMP reductase

substrate_name: Unknown

enzyme: GMP reductase

substrate: Unknown


enzyme_display_name: L-ascorbate peroxidase

organism: Crocus sativus

assay_conditions_summary: pH 8

enzyme: L-ascorbate peroxidase


substrate_name: L-ascorbate

substrate: L-ascorbate


organism: Citrus limon


enzyme_display_name: UniProt P36969

enzyme: UniProt P36969


enzyme_display_name: UniProt P11542

organism: Phanerodontia chrysosporium

proof_lines:
Raw SKiD Env: Temp=25°C, pH=4.5
Raw SKiD Env: Temp=25°C, pH=2.5
Raw SKiD Env: Temp=25°C, pH=3.5

enzyme: UniProt P11542


enzyme_display_name: UniProt O94753

organism: Pleurotus eryngii

proof_lines:
Raw SKiD Env: Temp=-----, pH=-----
Raw SKiD Env: Temp=-----, pH=3.5
Raw SKiD Env: Temp=25°C, pH=5

enzyme: UniProt O94753


substrate_name: methoxyhydroquinone

substrate: methoxyhydroquinone


substrate_name: guaiacol

substrate: guaiacol


substrate_name: catechol

substrate: catechol


proof_lines:
Raw SKiD Env: Temp=-----, pH=3.5
Raw SKiD Env: Temp=25°C, pH=3
Raw SKiD Env: Temp=25°C, pH=3.5


enzyme_display_name: NADPH:quinone reductase

enzyme: NADPH:quinone reductase


substrate_name: GMP

proof_lines:
pH 8.0, 35°C
data from the low concentration range

substrate: GMP


proof_lines:
membrane-bound isoform, pH 7, 37°C
soluble isoform, pH 7, 37°C


assay_conditions_summary: pH 8; 308.15 K; cofactor NADPH


substrate_name: NADH

assay_conditions_summary: cofactor NADH

proof_lines:
enzyme from erythrocyte
enzyme from erythrocyte membrane
enzyme from erythrocyte and liver

substrate: NADH


substrate_name: ferricyanide

proof_lines: enzyme from liver microsomes, protease solubilized

substrate: ferricyanide


substrate_name: Hexacyanoferrate(III); H+; NADH

proof_lines:
soluble isoform, pH 7, 37°C
membrane-bound isoform, pH 7, 37°C
enzyme from eythrocyte membrane

substrate: Hexacyanoferrate(III); H+; NADH


substrate_name: ferricytochrome b5

substrate: ferricytochrome b5


organism: Hordeum vulgare

proof_lines:
in the presence of 5 mM Mg2+
in the presence of 5 mM Ca2+


proof_lines:
in presence of 25 mM phosphate
without phosphate


organism: Microcystis aeruginosa

proof_lines: vs. 1,4-naphthoquinone, value derived from from intercept

proof_lines: vs. NADPH, value derived from from slope

proof_lines: vs. NADPH, value derived from from intercept


enzyme_display_name: UniProt A0A2P1C6N4

organism: Irpex lacteus

enzyme: UniProt A0A2P1C6N4


substrate_name: Reactive Blue 19

substrate: Reactive Blue 19


enzyme_display_name: UniProt Q556V8

organism: Dictyostelium discoideum

substrate_name: pyrogallol

enzyme: UniProt Q556V8

substrate: pyrogallol


substrate_name: Reactive Blue 4

substrate: Reactive Blue 4


substrate_name: veratryl alcohol

substrate: veratryl alcohol


enzyme_display_name: UniProt Q8WZK8

organism: Bjerkandera adusta

enzyme: UniProt Q8WZK8


enzyme_display_name: UniProt Q939D2

organism: Burkholderia pseudomallei

proof_lines:
Raw SKiD Env: Temp=25°C, pH=4.5
Raw SKiD Env: Temp=37°C, pH=7

enzyme: UniProt Q939D2


enzyme_display_name: UniProt Q31MN3

organism: Synechococcus elongatus

substrate_name: isoniazid

enzyme: UniProt Q31MN3

substrate: isoniazid


enzyme_display_name: UniProt P9WIE5

organism: Mycobacterium tuberculosis

enzyme: UniProt P9WIE5


enzyme_display_name: catalase peroxidase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N238S to reconstruct the assayed variant sequence.

enzyme: catalase peroxidase


substrate_name: o-Dianisidine

substrate: o-Dianisidine


enzyme_display_name: UniProt Q9Y9L0

organism: Aeropyrum pernix

enzyme: UniProt Q9Y9L0


organism: Mucor racemosus


enzyme_display_name: adenylyl-sulfate reductase

organism: Nitratidesulfovibrio vulgaris

substrate_name: reduced riboflavin

enzyme: adenylyl-sulfate reductase

substrate: reduced riboflavin


enzyme_display_name: nitrite reductase (NO-forming)

organism: Nitrososphaera viennensis

substrate_name: nitrite

proof_lines:
pH 6.5, 25°C
at pH 8.0 and 25°C

enzyme: nitrite reductase (NO-forming)

substrate: nitrite


enzyme_display_name: cytochrome-b5 reductase

organism: Oryctolagus cuniculus

substrate_name: methemoglobin-ferrocyanide complex

enzyme: cytochrome-b5 reductase

substrate: methemoglobin-ferrocyanide complex


enzyme_display_name: UniProt P30041

organism: Homo sapiens

enzyme: UniProt P30041


substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


substrate_name: tert-butyl hydroperoxide

substrate: tert-butyl hydroperoxide


enzyme_display_name: UniProt Q9PCF4

organism: Xylella fastidiosa

enzyme: UniProt Q9PCF4


substrate_name: Lipoamide

substrate: Lipoamide


enzyme_display_name: unspecific peroxygenase

organism: Marasmius rotula

substrate_name: trans-stilbene

enzyme: unspecific peroxygenase

substrate: trans-stilbene


substrate_name: Cyclohexanol

substrate: Cyclohexanol


substrate_name: Cyclohexane

substrate: Cyclohexane


enzyme_display_name: UniProt B9W4V6

organism: Cyclocybe aegerita

substrate_name: Benzene

enzyme: UniProt B9W4V6

substrate: Benzene


substrate_name: isophorone

substrate: isophorone


proof_lines:
Raw SKiD Env: Temp=20°C, pH=6.5
Raw SKiD Env: Temp=30°C, pH=4.4


enzyme_display_name: UniProt O31440

organism: Bacillus subtilis

proof_lines:
Raw SKiD Env: Temp=25°C, pH=6.7
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt O31440


substrate_name: myristic acid

smiles: CCCCCCCCCCCCCC(=O)O

substrate: myristic acid


substrate_name: NADH

substrate: NADH


organism: Ovis aries

substrate_name: ferricytochrome b5

substrate: ferricytochrome b5


enzyme_display_name: NADPH-hemoprotein reductase

organism: Priestia megaterium

substrate_name: ferricytochrome c

proof_lines: in the presence of laurate and carbon monoxide

enzyme: NADPH-hemoprotein reductase

substrate: ferricytochrome c


organism: Pseudomonas aeruginosa

substrate_name: reduced ascorbate

substrate: reduced ascorbate


enzyme_display_name: hydrogen dehydrogenase

organism: Gloeocapsa alpicola

substrate_name: NADPH

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

enzyme: hydrogen dehydrogenase

substrate: NADPH


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 303.15 K; cofactor NAD+

substrate: NAD+


substrate_name: reduced methyl viologen

substrate: reduced methyl viologen


substrate_name: oxidized methyl viologen

substrate: oxidized methyl viologen


enzyme_display_name: L-tyrosine peroxygenase

organism: Streptomyces refuineus

substrate_name: L-tyrosine

enzyme: L-tyrosine peroxygenase

substrate: L-tyrosine


proof_lines: with L-tyrosine as cosubstrate, at pH 8.0 and 37°C


organism: Caldanaerobacter subterraneus subsp. tengcongensis

assay_conditions_summary: 343.15 K; cofactor NADH


assay_conditions_summary: 343.15 K; cofactor NAD+


organism: Hydrogenomonas sp.

assay_conditions_summary: cofactor NAD+


smiles: [HH]


enzyme_display_name: hydrogen dehydrogenase (NADP+)

organism: Tetradesmus obliquus

enzyme: hydrogen dehydrogenase (NADP+)


substrate_name: oxidized ferredoxin

substrate: oxidized ferredoxin


enzyme_display_name: ferredoxin hydrogenase

organism: Enterobacter cloacae

enzyme: ferredoxin hydrogenase


substrate_name: reduced ferredoxin

substrate: reduced ferredoxin


organism: Synechocystis sp.


enzyme_display_name: hydrogenase (NAD+, ferredoxin)

organism: Neomoorella thermoacetica

assay_conditions_summary: pH 7.5; 318.15 K; cofactor NAD+

enzyme: hydrogenase (NAD+, ferredoxin)


organism: Methanosarcina barkeri

substrate_name: Ferredoxin

substrate: Ferredoxin


enzyme_display_name: cytochrome-c3 hydrogenase

organism: Bacteria

substrate_name: methyl viologen

enzyme: cytochrome-c3 hydrogenase

substrate: methyl viologen


organism: Desulfomicrobium norvegicum

substrate_name: ferricytochrome c3

substrate: ferricytochrome c3


enzyme_display_name: UniProt P95607

organism: Rhodococcus opacus

substrate_name: protocatechuate

enzyme: UniProt P95607

substrate: protocatechuate


substrate_name: Hydroxyquinol

substrate: Hydroxyquinol


substrate_name: 2,3-Dihydroxybenzoic acid

substrate: 2,3-Dihydroxybenzoic acid


substrate_name: pyrogallol

substrate: pyrogallol


substrate_name: catechol

substrate: catechol


enzyme_display_name: UniProt Q9F103

organism: Acinetobacter radioresistens

proof_lines:
Raw SKiD Env: Temp=-----, pH=8.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt Q9F103


enzyme_display_name: UniProt Q67FT0

organism: Pseudaminobacter salicylatoxidans

enzyme: UniProt Q67FT0


substrate_name: salicylate

substrate: salicylate


substrate_name: gentisate

substrate: gentisate


enzyme_display_name: UniProt Q5LLB1

organism: Ruegeria pomeroyi

enzyme: UniProt Q5LLB1


enzyme_display_name: UniProt Q8X655

organism: Escherichia coli

enzyme: UniProt Q8X655


organism: Alvikia littoralis


organism: Chlamydomonas reinhardtii


organism: Thermotoga maritima

proof_lines: pH and temperature not specified in the publication


organism: Caldanaerobacter subterraneus subsp. tengcongensis


enzyme_display_name: lipoyl-dependent peroxiredoxin

organism: Mycobacterium tuberculosis

substrate_name: tert-butyl hydroperoxide

enzyme: lipoyl-dependent peroxiredoxin

substrate: tert-butyl hydroperoxide


substrate_name: trans-pinocarveylhydroperoxide

substrate: trans-pinocarveylhydroperoxide


substrate_name: cumene hydroperoxide

substrate: cumene hydroperoxide


organism: Hypoxylon sp. EC38


substrate_name: indole

substrate: indole


enzyme_display_name: gentisate 1,2-dioxygenase

proof_lines: pH 8.0, temperature not specified in the publication

enzyme: gentisate 1,2-dioxygenase


enzyme_display_name: catechol 2,3-dioxygenase

organism: Pseudomonas stutzeri

verification_status: corrected

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H199N to reconstruct the assayed variant sequence.

column_label: PMID 15347689 Table III row (H199N)-C2,3O / 3-formylcatechol; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Normalized evidence: kcat 0.03 s^-1; Km 1.17 mM; kcat/Km 0.026 s^-1 mM^-1.

raw_value_unit_evidence: Table evidence: kcat 0.03 s^-1; Km 1170 uM; kcat/Km 2.6e-05 s^-1 uM^-1.

row_label: (H199N)-C2,3O / 3-formylcatechol

table_label: Table III. Kinetic parameters at pH 7.5 of wild-type and mutant C2,3O

enzyme: catechol 2,3-dioxygenase

status: corrected


verification_status: verified

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y255F to reconstruct the assayed variant sequence.

column_label: PMID 15347689 Table III row (Y255F)-C2,3O / catechol; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Normalized evidence: kcat 8.8 s^-1; Km 0.005 mM; kcat/Km 1760 s^-1 mM^-1.

raw_value_unit_evidence: Table evidence: kcat 8.8 s^-1; Km 5 uM; kcat/Km 1.76 s^-1 uM^-1.

row_label: (Y255F)-C2,3O / catechol

status: verified


column_label: Table III. Kinetic parameters at pH 7.5 of wild-type and mutant C2,3O, Table III / Wt-C2,3O / 4-Formylcatechol: Km=188 uM; kcat=16 s^-1; kcat/Km=0.085 s^-1 uM^-1.

row_label: Table III / Wt-C2,3O / 4-Formylcatechol


column_label: PMID 15347689 Table III row (Y255F)-C2,3O / 3-formylcatechol; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Normalized evidence: kcat 2.6 s^-1; Km 0.0516 mM; kcat/Km 50 s^-1 mM^-1.

raw_value_unit_evidence: Table evidence: kcat 2.6 s^-1; Km 51.6 uM; kcat/Km 0.05 s^-1 uM^-1.

row_label: (Y255F)-C2,3O / 3-formylcatechol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H246N to reconstruct the assayed variant sequence.

column_label: PMID 15347689 Table III row (H246N)-C2,3O / 4-formylcatechol; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Normalized evidence: kcat 0.43 s^-1; Km 0.97 mM; kcat/Km 0.44 s^-1 mM^-1.

raw_value_unit_evidence: Table evidence: kcat 0.43 s^-1; Km 970 uM; kcat/Km 0.00044 s^-1 uM^-1.

row_label: (H246N)-C2,3O / 4-formylcatechol


column_label: PMID 15347689 Table III row (H246N)-C2,3O / 3-formylcatechol; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Normalized evidence: kcat 6.9 s^-1; Km 0.44 mM; kcat/Km 16 s^-1 mM^-1.

raw_value_unit_evidence: Table evidence: kcat 6.9 s^-1; Km 440 uM; kcat/Km 0.016 s^-1 uM^-1.

row_label: (H246N)-C2,3O / 3-formylcatechol


column_label: PMID 15347689 Table III row (H199N)-C2,3O / catechol; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Normalized evidence: kcat 0.46 s^-1; Km 0.434 mM; kcat/Km 1.1 s^-1 mM^-1.

raw_value_unit_evidence: Table evidence: kcat 0.46 s^-1; Km 434 uM; kcat/Km 0.0011 s^-1 uM^-1.

row_label: (H199N)-C2,3O / catechol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H246A to reconstruct the assayed variant sequence.


substrate_name: Catechol; O2

column_label: PMID 15347689 Table III row Wt-C2,3O / catechol; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Normalized evidence: kcat 200 s^-1; Km 0.0015 mM; kcat/Km 120000 s^-1 mM^-1.

raw_value_unit_evidence: Table evidence: kcat 200 s^-1; Km 1.5 uM; kcat/Km 120 s^-1 uM^-1.

row_label: Wt-C2,3O / catechol

substrate: Catechol; O2


organism: Comamonas testosteroni


organism: Delftia acidovorans


enzyme_display_name: catechol 1,2-dioxygenase

organism: Geobacillus sp.

enzyme: catechol 1,2-dioxygenase


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


substrate_name: 1-hydroxynaphthalene-2-carboxylic acid

substrate: 1-hydroxynaphthalene-2-carboxylic acid


enzyme_display_name: protocatechuate 3,4-dioxygenase

organism: Azotobacter vinelandii

enzyme: protocatechuate 3,4-dioxygenase


substrate_name: Unknown

substrate: Unknown


organism: Corynebacterium glutamicum


organism: Brevibacterium fuscum


organism: Cutaneotrichosporon cutaneum


organism: Halalkalibacterium ligniniphilum

protein_accession_database: NCBI Protein

column_label: Table 3A columns Substrate, Km (uM), Kcat (s^-1), Kcat/Km (M^-1 s^-1); row 3-ethyl Catechol.

row_label: 3-ethyl Catechol

table_label: Table 3A: BLC23O catalytic properties towards 3-methyl catechol and 3-ethyl catechol


column_label: Table 3A columns Substrate, Km (uM), Kcat (s^-1), Kcat/Km (M^-1 s^-1); row 3-methyl Catechol.

row_label: 3-methyl Catechol


column_label: PMID 15347689 Table III row (H246N)-C2,3O / catechol; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Normalized evidence: kcat 1.6 s^-1; Km 0.714 mM; kcat/Km 2.2 s^-1 mM^-1.

raw_value_unit_evidence: Table evidence: kcat 1.6 s^-1; Km 714 uM; kcat/Km 0.0022 s^-1 uM^-1.

row_label: (H246N)-C2,3O / catechol


column_label: Table III. Kinetic parameters at pH 7.5 of wild-type and mutant C2,3O, Table III / Wt-C2,3O / 3-Formylcatechol: Km=32 uM; kcat=47 s^-1; kcat/Km=1.5 s^-1 uM^-1.

row_label: Table III / Wt-C2,3O / 3-Formylcatechol


column_label: PMID 15347689 Table III row (Y255F)-C2,3O / 4-formylcatechol; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Normalized evidence: kcat 0.45 s^-1; Km 0.248 mM; kcat/Km 1.8 s^-1 mM^-1.

raw_value_unit_evidence: Table evidence: kcat 0.45 s^-1; Km 248 uM; kcat/Km 0.0018 s^-1 uM^-1.

row_label: (Y255F)-C2,3O / 4-formylcatechol


column_label: Table III. Kinetic parameters at pH 7.5 of wild-type and mutant C2,3O, Table III / Wt-C2,3O / Catechol: Km=1.5 uM; kcat=200 s^-1; kcat/Km=120 s^-1 uM^-1.

row_label: Table III / Wt-C2,3O / Catechol


column_label: PMID 15347689 Table III row (H199N)-C2,3O / 4-formylcatechol; columns kcat (s^-1), Km (uM), and kcat/Km (s^-1 uM^-1).

normalized_value_unit_evidence: Normalized evidence: kcat 0.0047 s^-1; Km 0.6 mM; kcat/Km 0.0078 s^-1 mM^-1.

raw_value_unit_evidence: Table evidence: kcat 0.0047 s^-1; Km 600 uM; kcat/Km 7.8e-06 s^-1 uM^-1.

row_label: (H199N)-C2,3O / 4-formylcatechol


column_label: Table III. Kinetic parameters at pH 7.5 of wild-type and mutant C2,3O, Table III / Wt-C2,3O / 4-Nitrocatechol: Km=35 uM; kcat=1.4 s^-1; kcat/Km=0.04 s^-1 uM^-1.

row_label: Table III / Wt-C2,3O / 4-Nitrocatechol


organism: Tecoma stans


enzyme_display_name: sulfhydrogenase

organism: Thermotoga neapolitana

substrate_name: Polysulfide

enzyme: sulfhydrogenase

substrate: Polysulfide


organism: Megasphaera elsdenii

substrate_name: Oxidized benzyl viologen

substrate: Oxidized benzyl viologen


organism: Candida tropicalis


organism: Acinetobacter radioresistens

proof_lines:
isoenzyme B
isoenzyme A
IsoB


enzyme_display_name: UniProt P14902

organism: Homo sapiens

substrate_name: L-tryptophan

enzyme: UniProt P14902

substrate: L-tryptophan


organism: Sphingobium xenophagum


organism: Pseudomonas putida

substrate_name: oxygen

proof_lines:
isoenzymes 1 and 2
isoenzyme 3

substrate: oxygen


proof_lines:
isoenzyme 3
isoenzyme 2
isoenzyme 1


organism: Nocardia erythropolis

substrate_name: protocatechuate

substrate: protocatechuate


organism: Tetradesmus obliquus

substrate_name: methyl viologen

substrate: methyl viologen


enzyme_display_name: UniProt Q96SZ5

enzyme: UniProt Q96SZ5


enzyme_display_name: UniProt Q9I0N5

organism: Pseudomonas aeruginosa

proof_lines:
Raw SKiD Env: Temp=37°C, pH=7.5
Raw SKiD Env: Temp=37°C, pH=8
Raw SKiD Env: Temp=37°C, pH=7

enzyme: UniProt Q9I0N5


organism: Delftia acidovorans


organism: Faucicola osloensis


enzyme_display_name: Sulfhydrogenase 1 subunit alpha

organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

enzyme: Sulfhydrogenase 1 subunit alpha


substrate_name: methylene blue

substrate: methylene blue


enzyme_display_name: Sulfhydrogenase 1 subunit delta

enzyme: Sulfhydrogenase 1 subunit delta


organism: Brevibacterium fuscum


proof_lines:
mutant H200F
24°C, pH 7.5, mutant enzyme H200F


proof_lines:
wild-type
24°C, pH 7.5, wild-type enzyme


enzyme_display_name: persulfide dioxygenase

organism: Paraburkholderia phytofirmans

substrate_name: S-sulfanylglutathione

smiles: C(CC(=O)NC(CSS)C(=O)NCC(=O)O)C(C(=O)O)N

enzyme: persulfide dioxygenase

substrate: S-sulfanylglutathione


proof_lines: recombinant wild-type enzyme, pH 7.4, 22°C


smiles: O=O


organism: Geobacillus stearothermophilus


substrate_name: 3,4-Dihydroxyphenylpropionic acid

substrate: 3,4-Dihydroxyphenylpropionic acid


substrate_name: DL-3,4-dihydroxymandelic acid

substrate: DL-3,4-dihydroxymandelic acid


substrate_name: 3,4-dihydroxybenzoic acid

substrate: 3,4-dihydroxybenzoic acid


organism: Staphylococcus aureus

substrate_name: S-sulfanyl-L-cysteine

proof_lines: recombinant wild-type enzyme CstB, pH 6.0, 25°C, coupled persulfide dioxygenase-persulfide transferase activity

substrate: S-sulfanyl-L-cysteine


substrate_name: CoASSH

substrate: CoASSH


organism: Arthrobacter synephrinum


organism: Brevibacillus brevis


enzyme_display_name: cysteine dioxygenase

organism: Cupriavidus necator

substrate_name: L-Cysteine

enzyme: cysteine dioxygenase

substrate: L-Cysteine


smiles: O=C([O-])CCS

column_label: Primary article prose immediately before Figure 4 lists both CdoA cysteine and CdoA 3MP kinetic constants; Figure 4 caption gives assay conditions.

normalized_value_unit_evidence: CSV values match the paper cysteine row, not the sheet substrate 3-Mercaptopropanoate/3MP. For 3MP, paper values normalize to kcat 0.82 s^-1, Km 5.7 mM, kcat/Km 0.144 s^-1 mM^-1.

raw_value_unit_evidence: Paper reports for CdoA cysteine: Km 6.7 mM, kcat 0.01 s^-1, kcat/Km 0.002 s^-1 mM^-1; for 3MP: Km 5.7 mM, kcat 0.82 s^-1, kcat/Km 0.144 s^-1 mM^-1.

row_label: CdoA with 3MP; separate CdoA with cysteine prose

table_label: PMC article prose, Results: Characterization of CdoA


smiles: O=C(O)CCS

column_label: Primary article prose immediately before Figure 4 gives the 3MP row; Figure 4 caption gives CdoA 3MP substrate concentration range and assay conditions.

normalized_value_unit_evidence: CSV values match after unit normalization: kcat 0.82 s^-1, Km 5.7 mM, kcat/Km 0.143859649122807 s^-1 mM^-1, matching rounded paper 0.144.

raw_value_unit_evidence: Paper reports CdoA with 3MP: maximal specific activity 2.2 umol 3SP/mg protein/min, Km 5.7 mM, kcat 0.82 s^-1, kcat/Km 0.144 s^-1 mM^-1.

row_label: CdoA with 3MP


proof_lines:
pH 7.5, 4°C
pH 7.5, 22°C
recombinant enzyme


organism: Acidithiobacillus caldus

substrate_name: glutathione

substrate: glutathione


proof_lines: sigmoidal curve with Hill coefficient 2.3, pH 7.5, 40°C


proof_lines: wild-type, phosphate buffer pH 8.0, 37°C


enzyme_display_name: indole 2,3-dioxygenase

organism: Tecoma stans

substrate_name: indole

enzyme: indole 2,3-dioxygenase

substrate: indole


organism: Zea mays


proof_lines: Mn-HPCD Fe-HPCD


organism: Acidianus brierleyi

substrate_name: sulfur

smiles: S

substrate: sulfur


organism: Streptomyces coelicolor

substrate_name: L-cysteine

smiles: C(C(C(=O)O)N)S

proof_lines: SCO3035, measurement of cysteine sulfinic acid production is done by high-performance liquid chromatography

substrate: L-cysteine


organism: Thiobacillus thioparus


enzyme_display_name: Gentisate 1,2 dioxygenase 1

organism: Aquipseudomonas alcaligenes

substrate_name: gentisate

proof_lines: kcat is 2433 min(-1) with gentisate as substrate. kcat is 3098 min(-1) with 3-methylgentisate as substrate. kcat is 613 min(-1) with 3-bromogentisate as substrate. kcat is 1573 min(-1) with 3-isopropylgentisate as substrate.

enzyme: Gentisate 1,2 dioxygenase 1

substrate: gentisate


organism: Arthrobacter globiformis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H200A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H200N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H200Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H200E to reconstruct the assayed variant sequence.


organism: Azotobacter vinelandii

substrate_name: cysteamine

smiles: C(CS)N

substrate: cysteamine


enzyme_display_name: Sulfhydrogenase 2 subunit alpha

organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)

substrate_name: H(2) (methyl viologen as cosubstrate)

enzyme: Sulfhydrogenase 2 subunit alpha

substrate: H(2) (methyl viologen as cosubstrate)


enzyme_display_name: Sulfhydrogenase 2 subunit delta

enzyme: Sulfhydrogenase 2 subunit delta


organism: Pseudomonas sp. HB01

proof_lines: pH and temperature not specified in the publication


substrate_name: catechol

substrate: catechol


organism: Hydrogenophaga palleronii


substrate_name: protocatechuate

substrate: protocatechuate


organism: Acinetobacter radioresistens


proof_lines: Mn-MndD Fe-MndD


proof_lines: Fe-MndD Mn-MndD


organism: Bacillus cereus

column_label: Table 1 columns CDO construct, pH optimum, Cysteine Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); row BC2617.

normalized_value_unit_evidence: kcat 2.0 s^-1; Km 5.7 mM; printed kcat/Km 0.4 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row BC2617: Cysteine Km 5.7 mM; kcat 2.0 s^-1; kcat/Km 0.4 mM^-1 s^-1.

row_label: BC2617 (Bacillus cereus ATCC 14579 CDO homolog)

table_label: Table 1, comparison of molecular properties and kinetic parameters of purified eukaryotic and bacterial CDOs


organism: Pseudomonas sp. HA10

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


organism: Homo sapiens

proof_lines: cosubstrate N-terminal Cys of RGS5, pH not specified in the publication, 37°C

proof_lines: cosubstrate N-terminal Cys of RGS4, pH not specified in the publication, 37°C


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

proof_lines: determind under saturating oxygen conditions

proof_lines: under conditions where the second substrate oxygen is saturated

source_databases_merged: brenda skid uniprot


enzyme_display_name: UniProt Q88E47

organism: Pseudomonas putida

substrate_name: homogentisate

proof_lines: kcat is 79.5 sec(-1) for the oxidative ring cleavage of homogentisate.

source_databases_merged: skid uniprot

enzyme: UniProt Q88E47

substrate: homogentisate


proof_lines: pH 6.1, 37°C, recombinnat wild-type enzyme

proof_lines: pH 6.1, 37°C, recombinant wild-type enzyme, under iron saturation


substrate_name: O2; L-Cysteine

substrate: O2; L-Cysteine


enzyme_display_name: Gentisate 1,2 dioxygenase 2

enzyme: Gentisate 1,2 dioxygenase 2


enzyme_display_name: UniProt Q67FT0

organism: Pseudaminobacter salicylatoxidans

enzyme: UniProt Q67FT0


enzyme_display_name: gentisate 1,2-dioxygenase

organism: Rhizorhabdus dicambivorans

enzyme: gentisate 1,2-dioxygenase


enzyme_display_name: homogentisate 1,2-dioxygenase

organism: Mus musculus

substrate_name: O2; Homogentisate

enzyme: homogentisate 1,2-dioxygenase

substrate: O2; Homogentisate


substrate_name: ferredoxin

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

substrate: ferredoxin


enzyme_display_name: NADP-reducing hydrogenase subunit HndC

organism: Solidesulfovibrio fructosivorans

substrate_name: Unknown

enzyme: NADP-reducing hydrogenase subunit HndC

substrate: Unknown


enzyme_display_name: NADP-reducing hydrogenase subunit HndD

enzyme: NADP-reducing hydrogenase subunit HndD


enzyme_display_name: NADP-reducing hydrogenase subunit HndA

enzyme: NADP-reducing hydrogenase subunit HndA


enzyme_display_name: NADP-reducing hydrogenase subunit HndB

enzyme: NADP-reducing hydrogenase subunit HndB


enzyme_display_name: Gentisate 1,2-dioxygenase

organism: Haloferax sp

substrate_name: gentisic acid

proof_lines: Highest activity in the presence of 2 M KCl or NaCl. 60% loss of activity in the presence of 1.5 M KCl.

enzyme: Gentisate 1,2-dioxygenase

substrate: gentisic acid


substrate_name: methyl viologen (sodium dithionate and H(+) as cosubstrates)

assay_conditions_summary: cofactor NADPH


substrate: methyl viologen (sodium dithionate and H(+) as cosubstrates)


enzyme_display_name: cytochrome-c3 hydrogenase

organism: Nitratidesulfovibrio vulgaris

substrate_name: mutant cytochrome c3 K101M

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K101M with inferred residue-numbering offset +5 to reconstruct the assayed variant sequence.

proof_lines: 25°C, pH 7.0, mutant cytochrome c3 K101M

enzyme: cytochrome-c3 hydrogenase

substrate: mutant cytochrome c3 K101M


substrate_name: mutant cytochrome c3 K95M

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K95M with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.

substrate: mutant cytochrome c3 K95M


substrate_name: mutant cytochrome c3 K58M

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K58M with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.

substrate: mutant cytochrome c3 K58M


substrate_name: mutant cytochrome c3 K94M

sequence_variant_note: Resolved canonical sequence from identity matching and applied mutation signature K94M with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.

substrate: mutant cytochrome c3 K94M


enzyme_display_name: catechol 1,2-dioxygenase

organism: Candida albicans

substrate_name: Catechol

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

enzyme: catechol 1,2-dioxygenase

substrate: Catechol


organism: Brevibacterium fuscum


enzyme_display_name: 3-carboxyethylcatechol 2,3-dioxygenase

organism: Cupriavidus necator

enzyme: 3-carboxyethylcatechol 2,3-dioxygenase


organism: Escherichia coli


organism: Rhodococcus sp.

substrate_name: 3-(2,3-dihydroxyphenyl)propionic acid

substrate: 3-(2,3-dihydroxyphenyl)propionic acid


enzyme_display_name: sulfur dioxygenase

substrate_name: S-Sulfanylglutathione

enzyme: sulfur dioxygenase

substrate: S-Sulfanylglutathione


substrate_name: mutant cytochrome c3 K60M

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K60M with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

substrate: mutant cytochrome c3 K60M


substrate_name: mutant cytochrome c3 K15M

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K15M with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

substrate: mutant cytochrome c3 K15M


substrate_name: mutant cytochrome c3 K72M

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K72M with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

substrate: mutant cytochrome c3 K72M


substrate_name: mutant cytochrome c3 K57M

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K57M with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.

substrate: mutant cytochrome c3 K57M


enzyme_display_name: Membrane-bound hydrogenase subunit alpha

organism: Pyrococcus furiosus (strain ATCC 43587 / DSM 3638 / JCM 8422 / Vc1)


enzyme_display_name: Membrane-bound hydrogenase subunit beta

enzyme: Membrane-bound hydrogenase subunit beta


enzyme_display_name: Probable membrane-bound hydrogenase subunit mbhJ


enzyme_display_name: Sulfhydrogenase 2 subunit gamma

substrate_name: sulfur (H(2) as cosubstrate)

enzyme: Sulfhydrogenase 2 subunit gamma

substrate: sulfur (H(2) as cosubstrate)


enzyme_display_name: Sulfhydrogenase 2 subunit beta

enzyme: Sulfhydrogenase 2 subunit beta


enzyme_display_name: Sulfhydrogenase 1 subunit beta

enzyme: Sulfhydrogenase 1 subunit beta


enzyme_display_name: Sulfhydrogenase 1 subunit gamma

enzyme: Sulfhydrogenase 1 subunit gamma


organism: Comamonas testosteroni


enzyme_display_name: Homogentisate 1,2-dioxygenase

organism: Pseudomonas putida (strain ATCC 47054 / DSM 6125 / CFBP 8728 / NCIMB 11950 / KT2440)

enzyme: Homogentisate 1,2-dioxygenase


enzyme_display_name: cysteine dioxygenase

organism: Arabidopsis thaliana

substrate_name: O2; L-Cysteine

proof_lines: kcat is 4.18 sec(-1) with CGGAIISDFIPPPR peptide as substrate.

enzyme: cysteine dioxygenase

substrate: O2; L-Cysteine


proof_lines: kcat is 7.9 sec(-1) with CGGAIISDFIPPPR peptide as substrate.


organism: Homo sapiens

substrate_name: N-terminal Cys of RGS5

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

substrate: N-terminal Cys of RGS5


enzyme_display_name: protocatechuate 3,4-dioxygenase

organism: Hydrogenophaga palleronii

enzyme: protocatechuate 3,4-dioxygenase


enzyme_display_name: Gentisate 1,2 dioxygenase 1

organism: Aquipseudomonas alcaligenes

proof_lines: kcat is 2433 min(-1) with gentisate as substrate. kcat is 3098 min(-1) with 3-methylgentisate as substrate. kcat is 613 min(-1) with 3-bromogentisate as substrate. kcat is 1573 min(-1) with 3-isopropylgentisate as substrate.

enzyme: Gentisate 1,2 dioxygenase 1


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: 2-aminoethanethiol dioxygenase

enzyme: 2-aminoethanethiol dioxygenase


enzyme_display_name: cysteamine dioxygenase

organism: Sus scrofa

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

enzyme: cysteamine dioxygenase


enzyme_display_name: catechol 2,3-dioxygenase

organism: Pseudomonas sp. HB01

proof_lines: pH and temperature not specified in the publication

enzyme: catechol 2,3-dioxygenase


substrate_name: L-Cysteine; O2

proof_lines: kcat is 31 sec(-1) with CGGAIISDFIPPPR peptide as substrate.

substrate: L-Cysteine; O2


proof_lines: kcat is 1.98 sec(-1) with CGGAIISDFIPPPR peptide as substrate.


proof_lines: kcat is 4.7 sec(-1) with CGGAIISDFIPPPR peptide as substrate.


substrate_name: Catechol; O2

substrate: Catechol; O2


organism: Bacillus cereus


organism: Bacillus subtilis

column_label: Table 1 columns CDO construct, pH optimum, Cysteine Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); row YubC.

normalized_value_unit_evidence: kcat 0.39 s^-1; Km 3.0 mM; printed kcat/Km 0.1 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row YubC: Cysteine Km 3.0 mM; kcat 0.39 s^-1; kcat/Km 0.1 mM^-1 s^-1.

row_label: YubC (Bacillus subtilis CDO homolog)


organism: Rattus norvegicus


organism: Streptomyces coelicolor

column_label: Table 1 columns CDO construct, pH optimum, Cysteine Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); row SCO5772.

normalized_value_unit_evidence: kcat 0.30 s^-1; Km 3.8 mM; printed kcat/Km 0.1 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row SCO5772: Cysteine Km 3.8 mM; kcat 0.30 s^-1; kcat/Km 0.1 mM^-1 s^-1.

row_label: SCO5772 (Streptomyces coelicolor A3(2) CDO homolog)


organism: Escherichia coli (strain K12)

substrate_name: 2,3-dihydroxycinnamic acid (at 20 degrees Celsius and pH 8)

proof_lines:
MhpB
MpcI
3-substituted catechols


substrate_name: methyl-2,3-dihydroxyphenylpropionate (at 20 degrees Celsius and pH 8)


substrate_name: 3-propylcatechol (at 20 degrees Celsius and pH 8)


substrate_name: 3-ethylcatechol (at 20 degrees Celsius and pH 8)


substrate_name: catechol (at 20 degrees Celsius and pH 8)

proof_lines: MhpB MpcI catechols


enzyme_display_name: catechol 1,2-dioxygenase

organism: Rhodococcus opacus

substrate_name: 2,3-Dihydroxybenzoic acid

column_label: Table 1 C 1,2-DO row 2,3-Dihydroxybenzoic acid; columns Km uM, kcat min^-1, kcat/Km min^-1*uM^-1; raw cells 700, 17, 0.024; normalized cells 0.7 mM, 0.2833333333333333333333333333 s^-1, 0.4 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.7 normalized_unit=mM; kcat normalized_value=0.2833333333333333333333333333 normalized_unit=s^-1; kcat/Km normalized_value=0.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=700 raw_unit=uM; kcat raw_value=17 raw_unit=min^-1; kcat/Km raw_value=0.024 raw_unit=min^-1*uM^-1

row_label: 2,3-Dihydroxybenzoic acid

table_label: Table 1. Kinetic data of two intradiol dioxygenases from R. opacus 1CP grown on different substrates

substrate: 2,3-Dihydroxybenzoic acid


normalized_value_unit_evidence: Km normalized_value=0.0007 normalized_unit=mM; kcat normalized_value=0.1783333333333333333333333333 normalized_unit=s^-1; kcat/Km normalized_value=255 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=0.7 raw_unit=uM; kcat raw_value=10.7 raw_unit=min^-1; kcat/Km raw_value=15.3 raw_unit=min^-1*uM^-1


normalized_value_unit_evidence: Km normalized_value=0.0065 normalized_unit=mM; kcat normalized_value=10.615 normalized_unit=s^-1; kcat/Km normalized_value=1633.333333333333333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=6.5 raw_unit=uM; kcat raw_value=636.9 raw_unit=min^-1; kcat/Km raw_value=98 raw_unit=min^-1*uM^-1


normalized_value_unit_evidence: Km normalized_value=0.0015 normalized_unit=mM; kcat normalized_value=0.2733333333333333333333333333 normalized_unit=s^-1; kcat/Km normalized_value=181.6666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=1.5 raw_unit=uM; kcat raw_value=16.4 raw_unit=min^-1; kcat/Km raw_value=10.9 raw_unit=min^-1*uM^-1


substrate_name: catechol

column_label: Table 1 C 1,2-DO row Catechol; columns Km uM, kcat min^-1, kcat/Km min^-1*uM^-1; raw cells 3, 613.8, 204.6; normalized cells 0.003 mM, 10.23 s^-1, 3410 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.003 normalized_unit=mM; kcat normalized_value=10.23 normalized_unit=s^-1; kcat/Km normalized_value=3410 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=3 raw_unit=uM; kcat raw_value=613.8 raw_unit=min^-1; kcat/Km raw_value=204.6 raw_unit=min^-1*uM^-1

row_label: Catechol

substrate: catechol


substrate_name: Hydroxyquinol

column_label: Table 1 C 1,2-DO row Hydroxyquinol (1,2,4-trihydroxy benzene); columns Km uM, kcat min^-1, kcat/Km min^-1*uM^-1; raw cells 97, 16.5, 0.17; normalized cells 0.097 mM, 0.275 s^-1, 2.833333333333333333333333333 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.097 normalized_unit=mM; kcat normalized_value=0.275 normalized_unit=s^-1; kcat/Km normalized_value=2.833333333333333333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=97 raw_unit=uM; kcat raw_value=16.5 raw_unit=min^-1; kcat/Km raw_value=0.17 raw_unit=min^-1*uM^-1

substrate: Hydroxyquinol


substrate_name: protocatechuate

column_label: Table 1 C 1,2-DO row Protocatechuic acid (3,4-Dihydroxybenzoic acid); columns Km uM, kcat min^-1, kcat/Km min^-1*uM^-1; raw cells 310, 2.65, 0.009; normalized cells 0.31 mM, 0.04416666666666666666666666667 s^-1, 0.15 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.31 normalized_unit=mM; kcat normalized_value=0.04416666666666666666666666667 normalized_unit=s^-1; kcat/Km normalized_value=0.15 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=310 raw_unit=uM; kcat raw_value=2.65 raw_unit=min^-1; kcat/Km raw_value=0.009 raw_unit=min^-1*uM^-1

substrate: protocatechuate


substrate_name: pyrogallol

column_label: Table 1 C 1,2-DO row Pyrogallol (1,2,3-trihydroxy benzene); columns Km uM, kcat min^-1, kcat/Km min^-1*uM^-1; raw cells 4.5, 144.5, 32.1; normalized cells 0.0045 mM, 2.408333333333333333333333333 s^-1, 535 s^-1*mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0045 normalized_unit=mM; kcat normalized_value=2.408333333333333333333333333 normalized_unit=s^-1; kcat/Km normalized_value=535 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=4.5 raw_unit=uM; kcat raw_value=144.5 raw_unit=min^-1; kcat/Km raw_value=32.1 raw_unit=min^-1*uM^-1

row_label: Pyrogallol (1,2,3-trihydroxy benzene)

substrate: pyrogallol


normalized_value_unit_evidence: Km normalized_value=0.004 normalized_unit=mM; kcat normalized_value=7.315 normalized_unit=s^-1; kcat/Km normalized_value=1828.333333333333333333333333 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=4 raw_unit=uM; kcat raw_value=438.9 raw_unit=min^-1; kcat/Km raw_value=109.7 raw_unit=min^-1*uM^-1


organism: Candida albicans


enzyme_display_name: persulfide dioxygenase

substrate_name: S-sulfanylglutathione

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O95571 and applied mutation signature C161Y to reconstruct the assayed variant sequence.

column_label: Table 1 (Comparison of the kinetic parameters for WT and mutant PDOs), enzyme row 'C161Y'; column 'Km (GSSH)' with unit head 'mM' = 1.2; column 'kcat' with unit head 's^-1' = 2.6; column 'kcat/Km' with unit head 'mM^-1 s^-1' = 2.2; column 'Specific activity' with unit head 'umol min^-1 mg^-1' = 5.8.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.2 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 1.2 mM. kcat: printed Table 1 cell 2.6 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 2.6 s^(-1). kcat/Km: the exported value 2.166666666666667 s^(-1)*mM^(-1) is the exact quotient 2.6 / 1.2 of the two printed component cells, and the paper's own printed efficiency cell 2.2 mM^-1 s^-1 is that same quotient written to the one-decimal precision of the table column.

raw_value_unit_evidence: Table 1, enzyme row 'C161Y': Km (GSSH) = 1.2 mM; kcat = 2.6 s^-1; printed kcat/Km = 2.2 mM^-1 s^-1.

row_label: Table 1, enzyme row 'C161Y'

table_label: Table 1: Comparison of the kinetic parameters for WT and mutant PDOs (J. Biol. Chem. 2018, 293(32):12429-12439)

enzyme: persulfide dioxygenase

substrate: S-sulfanylglutathione


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O95571 and applied mutation signature L55P to reconstruct the assayed variant sequence.

column_label: Table 1 (Comparison of the kinetic parameters for WT and mutant PDOs), enzyme row 'L55P'; column 'Km (GSSH)' with unit head 'mM' = 0.86; column 'kcat' with unit head 's^-1' = 2.8; column 'kcat/Km' with unit head 'mM^-1 s^-1' = 3.3; column 'Specific activity' with unit head 'umol min^-1 mg^-1' = 6.3.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.86 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.86 mM. kcat: printed Table 1 cell 2.8 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 2.8 s^(-1). kcat/Km: the exported value 3.255813953488372 s^(-1)*mM^(-1) is the exact quotient 2.8 / 0.86 of the two printed component cells, and the paper's own printed efficiency cell 3.3 mM^-1 s^-1 is that same quotient written to the one-decimal precision of the table column.

raw_value_unit_evidence: Table 1, enzyme row 'L55P': Km (GSSH) = 0.86 mM; kcat = 2.8 s^-1; printed kcat/Km = 3.3 mM^-1 s^-1.

row_label: Table 1, enzyme row 'L55P'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O95571 and applied mutation signature R163W to reconstruct the assayed variant sequence.

column_label: Table 1 (Comparison of the kinetic parameters for WT and mutant PDOs), enzyme row 'R163W'; column 'Km (GSSH)' with unit head 'mM' = 0.73; column 'kcat' with unit head 's^-1' = 5.6; column 'kcat/Km' with unit head 'mM^-1 s^-1' = 7.6; column 'Specific activity' with unit head 'umol min^-1 mg^-1' = 12.9.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.73 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 0.73 mM. kcat: printed Table 1 cell 5.6 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 5.6 s^(-1). kcat/Km: printed Table 1 cell 7.6 mM^-1 s^-1; 1 mM^-1 s^-1 is 1 s^(-1)*mM^(-1), so the printed cell carries over as 7.6 s^(-1)*mM^(-1); this is the paper's own independently fitted catalytic-efficiency value and it is proposed as the value for kcat_over_km.

raw_value_unit_evidence: Table 1, enzyme row 'R163W': Km (GSSH) = 0.73 mM; kcat = 5.6 s^-1; printed kcat/Km = 7.6 mM^-1 s^-1.

row_label: Table 1, enzyme row 'R163W'


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O95571 and applied mutation signature T136A to reconstruct the assayed variant sequence.

column_label: Table 1 (Comparison of the kinetic parameters for WT and mutant PDOs), enzyme row 'T136A'; column 'Km (GSSH)' with unit head 'mM' = 1.1; column 'kcat' with unit head 's^-1' = 0.8; column 'kcat/Km' with unit head 'mM^-1 s^-1' = 0.7; column 'Specific activity' with unit head 'umol min^-1 mg^-1' = 1.7.

normalized_value_unit_evidence: Km: printed Table 1 cell 1.1 mM; the printed unit is already mM, so no unit conversion applies; the exported value is 1.1 mM. kcat: printed Table 1 cell 0.8 s^-1; the printed unit is already s^-1, so no unit conversion applies; the exported value is 0.8 s^(-1). kcat/Km: the exported value 0.7272727272727273 s^(-1)*mM^(-1) is the exact quotient 0.8 / 1.1 of the two printed component cells, and the paper's own printed efficiency cell 0.7 mM^-1 s^-1 is that same quotient written to the one-decimal precision of the table column.

raw_value_unit_evidence: Table 1, enzyme row 'T136A': Km (GSSH) = 1.1 mM; kcat = 0.8 s^-1; printed kcat/Km = 0.7 mM^-1 s^-1.

row_label: Table 1, enzyme row 'T136A'


organism: Equus caballus

substrate_name: cysteamine

column_label: Table 2; Cysteamine row; K_m / Phenazine Omitted column; raw K_m value 5.7 x 10^-4 M.

raw_value_unit_evidence: Table 2 reports Cysteamine K_m = 5.7 x 10^-4 M in the Phenazine Omitted subcolumn.

row_label: Cysteamine row; K_m column; Phenazine Omitted subcolumn

table_label: PMID 1157952, Table 2: Initial oxidation rate and K_m for compounds listed in table 1 under group 3

substrate: cysteamine


substrate_name: N-acetylcysteamine

smiles: CC(=O)NCCS

column_label: Table 2; N-acetylcysteamine row; K_m / Phenazine Added column; raw K_m value 7.1 x 10^-4 M.

raw_value_unit_evidence: Table 2 reports N-acetylcysteamine K_m = 7.1 x 10^-4 M in the Phenazine Added subcolumn.

row_label: N-acetylcysteamine row; K_m column; Phenazine Added subcolumn

substrate: N-acetylcysteamine


substrate_name: homocysteamine

smiles: C(CN)CS

column_label: Table 2; Homocysteamine row; K_m / Phenazine Added column; raw K_m value 8.3 x 10^-4 M.

raw_value_unit_evidence: Table 2 reports Homocysteamine K_m = 8.3 x 10^-4 M in the Phenazine Added subcolumn.

row_label: Homocysteamine row; K_m column; Phenazine Added subcolumn

substrate: homocysteamine


substrate_name: mercaptoethanol

smiles: C(CS)O

column_label: Table 2; Mercaptoethanol row; K_m / Phenazine Added and Omitted columns; raw K_m value 1.2 x 10^-3 M in both.

raw_value_unit_evidence: Table 2 reports Mercaptoethanol K_m = 1.2 x 10^-3 M in both Phenazine Added and Phenazine Omitted subcolumns.

row_label: Mercaptoethanol row; K_m column; Phenazine Added and Omitted subcolumns

substrate: mercaptoethanol


substrate_name: 3-Mercaptopropionic acid

smiles: C(CS)C(=O)O

column_label: Table 2; 3-mercaptopropionic acid row; K_m / Phenazine Added column; raw K_m value 5.0 x 10^-3 M.

raw_value_unit_evidence: Table 2 reports 3-mercaptopropionic acid K_m = 5.0 x 10^-3 M in the Phenazine Added subcolumn.

row_label: 3-mercaptopropionic acid row; K_m column; Phenazine Added subcolumn

substrate: 3-Mercaptopropionic acid


organism: Cupriavidus necator

substrate_name: 2,3-dihydroxyphenylpropionic acid (at 20 degrees Celsius and pH 8)


substrate_name: 2,3-dihydroxycinnamic acid (at 20 degrees Celsius and pH 8)


substrate: 3-ethylcatechol (at 20 degrees Celsius and pH 8)


substrate_name: 3-methylcatechol (at 20 degrees Celsius and pH 8)


enzyme_display_name: NADP-reducing hydrogenase subunit HndA

organism: Solidesulfovibrio fructosivorans

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

enzyme: NADP-reducing hydrogenase subunit HndA


enzyme_display_name: NADP-reducing hydrogenase subunit HndC

enzyme: NADP-reducing hydrogenase subunit HndC

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


enzyme_display_name: NADP-reducing hydrogenase subunit HndD

enzyme: NADP-reducing hydrogenase subunit HndD


enzyme_display_name: NADP-reducing hydrogenase subunit HndB

enzyme: NADP-reducing hydrogenase subunit HndB


substrate_name: L-Cysteine

column_label: Table 1 (Steady-state kinetic parameters of AtPCOs 1–5 toward AtRAP2(2–15) at atmospheric O2), AtPCO row '3'; column 'kcat (s-1)' = 4.70; column 'Km (mM)' = 0.56; column 'Vmax (umol min-1 mg-1)' = 8.43. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4.70 s-1; the printed unit s-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 4.7 s^(-1); the exported value is 4.7 s^(-1). Km: printed Table 1 cell 0.56 mM; the printed unit mM is already the export unit (this table prints no uM kinetic cell), so no unit conversion applies and the paper value is 0.56 mM; the exported value is 0.56 mM. kcat/Km: Table 1 prints no catalytic-efficiency column, so the paper value 8.392857142857142 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 4.70 / 0.56 of this row own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, AtPCO row '3': kcat = 4.70 s-1; Km = 0.56 mM; Table 1 has no kcat/Km column, so it prints no kcat/Km cell for this row.

row_label: Table 1, AtPCO row '3' (AtPCO3)

table_label: Table 1: Steady-state kinetic parameters of AtPCOs 1–5 toward AtRAP2(2–15) at atmospheric O2 (J. Biol. Chem. 2018, 293(30):11786–11795)

substrate: L-Cysteine


column_label: Table 1 (Steady-state kinetic parameters of AtPCOs 1–5 toward AtRAP2(2–15) at atmospheric O2), AtPCO row '2'; column 'kcat (s-1)' = 1.98; column 'Km (mM)' = 0.09; column 'Vmax (umol min-1 mg-1)' = 3.45. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 1.98 s-1; the printed unit s-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 1.98 s^(-1); the exported value is 1.98 s^(-1). Km: printed Table 1 cell 0.09 mM; the printed unit mM is already the export unit (this table prints no uM kinetic cell), so no unit conversion applies and the paper value is 0.09 mM; the exported value is 0.09 mM. kcat/Km: Table 1 prints no catalytic-efficiency column, so the paper value 22.0 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 1.98 / 0.09 of this row own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, AtPCO row '2': kcat = 1.98 s-1; Km = 0.09 mM; Table 1 has no kcat/Km column, so it prints no kcat/Km cell for this row.

row_label: Table 1, AtPCO row '2' (AtPCO2)


column_label: Table 1 (Steady-state kinetic parameters of AtPCOs 1–5 toward AtRAP2(2–15) at atmospheric O2), AtPCO row '1'; column 'kcat (s-1)' = 4.18; column 'Km (mM)' = 0.24; column 'Vmax (umol min-1 mg-1)' = 7.14. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 4.18 s-1; the printed unit s-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 4.18 s^(-1); the exported value is 4.18 s^(-1). Km: printed Table 1 cell 0.24 mM; the printed unit mM is already the export unit (this table prints no uM kinetic cell), so no unit conversion applies and the paper value is 0.24 mM; the exported value is 0.24 mM. kcat/Km: Table 1 prints no catalytic-efficiency column, so the paper value 17.416666666666668 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 4.18 / 0.24 of this row own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, AtPCO row '1': kcat = 4.18 s-1; Km = 0.24 mM; Table 1 has no kcat/Km column, so it prints no kcat/Km cell for this row.

row_label: Table 1, AtPCO row '1' (AtPCO1)


column_label: Table 1 (Steady-state kinetic parameters of AtPCOs 1–5 toward AtRAP2(2–15) at atmospheric O2), AtPCO row '5'; column 'kcat (s-1)' = 7.90; column 'Km (mM)' = 0.16; column 'Vmax (umol min-1 mg-1)' = 16.1. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 7.90 s-1; the printed unit s-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 7.9 s^(-1); the exported value is 7.9 s^(-1). Km: printed Table 1 cell 0.16 mM; the printed unit mM is already the export unit (this table prints no uM kinetic cell), so no unit conversion applies and the paper value is 0.16 mM; the exported value is 0.16 mM. kcat/Km: Table 1 prints no catalytic-efficiency column, so the paper value 49.375 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 7.90 / 0.16 of this row own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, AtPCO row '5': kcat = 7.90 s-1; Km = 0.16 mM; Table 1 has no kcat/Km column, so it prints no kcat/Km cell for this row.

row_label: Table 1, AtPCO row '5' (AtPCO5)


column_label: Table 1 (Steady-state kinetic parameters of AtPCOs 1–5 toward AtRAP2(2–15) at atmospheric O2), AtPCO row '4'; column 'kcat (s-1)' = 31.0; column 'Km (mM)' = 0.69; column 'Vmax (umol min-1 mg-1)' = 63.4. Table 1 carries no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 1 cell 31.0 s-1; the printed unit s-1 is already the export unit (this table prints no min^-1 kinetic cell), so no unit conversion applies and the paper value is 31.0 s^(-1); the exported value is 31.0 s^(-1). Km: printed Table 1 cell 0.69 mM; the printed unit mM is already the export unit (this table prints no uM kinetic cell), so no unit conversion applies and the paper value is 0.69 mM; the exported value is 0.69 mM. kcat/Km: Table 1 prints no catalytic-efficiency column, so the paper value 44.92753623188406 s^(-1)*mM^(-1) is not a printed cell; it is the quotient 31.0 / 0.69 of this row own two printed cells, typed derived_same_measurement.

raw_value_unit_evidence: Table 1, AtPCO row '4': kcat = 31.0 s-1; Km = 0.69 mM; Table 1 has no kcat/Km column, so it prints no kcat/Km cell for this row.

row_label: Table 1, AtPCO row '4' (AtPCO4)


enzyme_display_name: UniProt A2VA43

organism: Streptomyces sp.

substrate_name: quercetin

enzyme: UniProt A2VA43

substrate: quercetin


enzyme_display_name: UniProt P32754

enzyme: UniProt P32754


enzyme_display_name: Gentisate 1,2 dioxygenase 2

substrate_name: gentisate

column_label: Table 1 row Gentisate, column Km (uM) under GDO-II gives 113.38 +/- 5.65

row_label: Gentisate

table_label: Table 1

enzyme: Gentisate 1,2 dioxygenase 2

substrate: gentisate


column_label: Table 1 row 3-Bromogentisate, column Km (uM) under GDO-II gives 29.27 +/- 1.38


column_label: Table 1 row 3-Isopropylgentisate, column Km (uM) under GDO-II gives 31.28 +/- 2.45


column_label: Table 1 row 3-Methylgentisate, column Km (uM) under GDO-II gives 54.80 +/- 1.85


organism: Staphylococcus aureus

substrate_name: bacillithiol persulfide

column_label: Table 2 row BSSH; columns Km (x10^-3 M), kcat (s^-1), kcat/Km (table efficiency column)

normalized_value_unit_evidence: Paper row normalizes to Km 1.8 mM; kcat 19.7 s^-1; kcat/Km 10.9 s^-1 mM^-1, but exported row has Km 0.0018 mM and kcat/Km 10944.444444444445

row_label: BSSH

table_label: Table 2. Kinetic characterization of the coupled persulfide dioxygenase-persulfide transferase activity of wild-type CstB

substrate: bacillithiol persulfide


substrate_name: CoASSH

assay_conditions_summary: pH 6; 298.15 K; cofactor CoA

column_label: Table 2 row CoASSH; columns Km (x10^-3 M), kcat (s^-1), kcat/Km (table efficiency column)

normalized_value_unit_evidence: Paper row normalizes to Km 1.1 mM; kcat 19.3 s^-1; kcat/Km 17.5 s^-1 mM^-1, but exported row has Km 0.0011 mM and kcat/Km 17545.454545454544

row_label: CoASSH

substrate: CoASSH


column_label: Table 2 row GSSH; columns Km (x10^-3 M), kcat (s^-1), kcat/Km (table efficiency column)

normalized_value_unit_evidence: Paper row normalizes to Km 7.8 mM; kcat 6.5 s^-1; kcat/Km 0.8 s^-1 mM^-1, but exported row has Km 0.0078 mM and kcat/Km 833.3333333333334

row_label: GSSH


substrate_name: S-sulfanyl-L-cysteine

column_label: Table 2 row CSSH; columns Km (x10^-3 M), kcat (s^-1), kcat/Km (table efficiency column); footnote b

normalized_value_unit_evidence: Paper row normalizes to Km 20 mM; kcat 28 s^-1; kcat/Km 1.4 s^-1 mM^-1, but exported row has kcat 5.0 s^-1, Km 0.02 mM, and kcat/Km 250

raw_value_unit_evidence: CSSH row: Km 20 +/- 21 x10^-3 M; kcat 28 +/- 27 s^-1; kcat/Km 1.4 +/- 2.0 x10^3 M^-1 s^-1; footnote b says very low activity made Km and Vmax difficult to measure accurately

row_label: CSSH

substrate: S-sulfanyl-L-cysteine


enzyme_display_name: gentisate 1,2-dioxygenase

organism: Pseudomonas alcaligenes

assay_conditions_summary: pH 7.4; 296.15 K; buffer 0.1 M phosphate

column_label: Table row P25X (Pseudomonas alcaligenes); Gentisate lists K_m 92 ± 5 uM, kcat 2,433 ± 39 min^-1 site^-1, and kcat/K_m 44.08 ± 3 in 10^4 s^-1 M^-1. The table labels the substrate as gentisate, the synonym for 2,5-dihydroxybenzoate.

normalized_value_unit_evidence: Km normalized_value=0.092 normalized_unit=mM; kcat normalized_value=40.55 normalized_unit=s^-1; kcat/Km normalized_value=440.8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=92 ± 5 raw_unit=uM; kcat raw_value=2,433 ± 39 raw_unit=min^-1 site^-1; kcat/Km raw_value=44.08 ± 3 raw_unit=10^4 s^-1 M^-1

table_label: Kinetic properties table for P25X and P35X gentisate 1,2-dioxygenases

enzyme: gentisate 1,2-dioxygenase


column_label: Table row P25X (Pseudomonas alcaligenes); 3-Bromogentisate lists K_m 15 ± 1 uM, kcat 613 ± 12 min^-1 site^-1, and kcat/K_m 68.11 ± 5 in 10^4 s^-1 M^-1.

normalized_value_unit_evidence: Km normalized_value=0.015 normalized_unit=mM; kcat normalized_value=10.217 normalized_unit=s^-1; kcat/Km normalized_value=681.1 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=15 ± 1 raw_unit=uM; kcat raw_value=613 ± 12 raw_unit=min^-1 site^-1; kcat/Km raw_value=68.11 ± 5 raw_unit=10^4 s^-1 M^-1


column_label: Table row P25X (Pseudomonas alcaligenes); 3-Isopropylgentisate lists K_m 53 ± 2 uM, kcat 1,573 ± 25 min^-1 site^-1, and kcat/K_m 49.47 ± 3 in 10^4 s^-1 M^-1.

normalized_value_unit_evidence: Km normalized_value=0.053 normalized_unit=mM; kcat normalized_value=26.217 normalized_unit=s^-1; kcat/Km normalized_value=494.7 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=53 ± 2 raw_unit=uM; kcat raw_value=1,573 ± 25 raw_unit=min^-1 site^-1; kcat/Km raw_value=49.47 ± 3 raw_unit=10^4 s^-1 M^-1


column_label: Table row P25X (Pseudomonas alcaligenes); 3-Methylgentisate lists K_m 76 ± 3 uM, kcat 3,098 ± 50 min^-1 site^-1, and kcat/K_m 67.94 ± 4 in 10^4 s^-1 M^-1.

normalized_value_unit_evidence: Km normalized_value=0.076 normalized_unit=mM; kcat normalized_value=51.633 normalized_unit=s^-1; kcat/Km normalized_value=679.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=76 ± 3 raw_unit=uM; kcat raw_value=3,098 ± 50 raw_unit=min^-1 site^-1; kcat/Km raw_value=67.94 ± 4 raw_unit=10^4 s^-1 M^-1


organism: Pseudomonas putida

column_label: Table row P35X (Pseudomonas putida); Gentisate lists K_m 143 ± 7 uM, kcat 3,376 ± 41 min^-1 site^-1, and kcat/K_m 39.34 ± 2 in 10^4 s^-1 M^-1. The table labels the substrate as gentisate, the synonym for 2,5-dihydroxybenzoate.

normalized_value_unit_evidence: Km normalized_value=0.143 normalized_unit=mM; kcat normalized_value=56.267 normalized_unit=s^-1; kcat/Km normalized_value=393.4 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=143 ± 7 raw_unit=uM; kcat raw_value=3,376 ± 41 raw_unit=min^-1 site^-1; kcat/Km raw_value=39.34 ± 2 raw_unit=10^4 s^-1 M^-1

row_label: P35X (Pseudomonas putida); Gentisate


column_label: Table row P35X (Pseudomonas putida); 3-Bromogentisate lists K_m 11 ± 0.3 uM, kcat 833 ± 16 min^-1 site^-1, and kcat/K_m 126.21 ± 2 in 10^4 s^-1 M^-1.

normalized_value_unit_evidence: Km normalized_value=0.011 normalized_unit=mM; kcat normalized_value=13.883 normalized_unit=s^-1; kcat/Km normalized_value=1262.1 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=11 ± 0.3 raw_unit=uM; kcat raw_value=833 ± 16 raw_unit=min^-1 site^-1; kcat/Km raw_value=126.21 ± 2 raw_unit=10^4 s^-1 M^-1


column_label: Table row P35X (Pseudomonas putida); 3-Isopropylgentisate lists K_m 4.3 ± 0.03 uM, kcat 129 ± 3 min^-1 site^-1, and kcat/K_m 50.00 ± 1 in 10^4 s^-1 M^-1.

normalized_value_unit_evidence: Km normalized_value=0.0043 normalized_unit=mM; kcat normalized_value=2.15 normalized_unit=s^-1; kcat/Km normalized_value=500.0 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=4.3 ± 0.03 raw_unit=uM; kcat raw_value=129 ± 3 raw_unit=min^-1 site^-1; kcat/Km raw_value=50.00 ± 1 raw_unit=10^4 s^-1 M^-1


column_label: Table row P35X (Pseudomonas putida); 3-Methylgentisate lists K_m 36 ± 1 uM, kcat 2,015 ± 32 min^-1 site^-1, and kcat/K_m 93.28 ± 4 in 10^4 s^-1 M^-1.

normalized_value_unit_evidence: Km normalized_value=0.036 normalized_unit=mM; kcat normalized_value=33.583 normalized_unit=s^-1; kcat/Km normalized_value=932.8 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: K_m raw_value=36 ± 1 raw_unit=uM; kcat raw_value=2,015 ± 32 raw_unit=min^-1 site^-1; kcat/Km raw_value=93.28 ± 4 raw_unit=10^4 s^-1 M^-1


organism: Homo sapiens

substrate_name: S-Sulfanylglutathione

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D196N with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.

substrate: S-Sulfanylglutathione


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature T152I to reconstruct the assayed variant sequence.


enzyme_display_name: Persulfide dioxygenase ETHE1, mitochondrial

substrate_name: glutathione persulfide (GSSH)

sequence_variant_note: Mutation signature D196N matches the mutant residue at offset +0 and the reference residue at offset -8; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: glutathione persulfide (GSSH)


enzyme_display_name: Gentisate 1,2-dioxygenase

organism: Ralstonia sp

column_label: Table 3 row Gentisate, column Km (uM): 22.4.

table_label: Table 3. Substrate specificity of NagI GDO

enzyme: Gentisate 1,2-dioxygenase


column_label: Table 3 row 3-Methylgentisate, column Km (uM): 10.7.


column_label: Table 3 row 3-Bromogentisate, column Km (uM): 5.3.

raw_value_unit_evidence: Km = 5.3 uM


organism: Methanopyrus kandleri

substrate_name: H+

assay_conditions_summary: pH 7

substrate: H+


enzyme_display_name: arachidonate 5-lipoxygenase

organism: Hordeum vulgare

substrate_name: arachidonic acid

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

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)O

enzyme: arachidonate 5-lipoxygenase

substrate: arachidonic acid


substrate_name: Unknown

substrate: Unknown


substrate_name: arachidonate

smiles: CCCCCC=CCC=CCC=CCC=CCCCC(=O)[O-]

substrate: arachidonate


organism: Saccharolobus solfataricus

column_label: Required kcat_over_km is metric-labeled in the primary table as kcat/KM 1.4 uM^-1*s^-1; this disagrees with exported kcat_over_km 1444.4444444444446 s^-1*mM^-1.

normalized_value_unit_evidence: kcat 5.2 s^-1 and KM 0.0036 mM match; paper kcat/KM normalizes to 1400 s^-1*mM^-1, not target 1444.4444444444446 s^-1*mM^-1.

table_label: Table 1: Kinetic parameters measured at 25 and 60 C for catechol, 3-MC, and 4-MC


substrate_name: catechol

column_label: All required metrics are exact primary Table 1 cells for SsoC2,3O at 25 C with catechol.

raw_value_unit_evidence: Table 1 row SsoC2,3O (25 C), column Catechol: kcat 1.3 +/- 0.1 s^-1; KM 1.6 +/- 0.2 uM; kcat/KM 0.81 uM^-1*s^-1.

row_label: SsoC2,3O (25 C); Catechol

substrate: catechol


column_label: All required metrics are exact primary Table 1 cells for SsoC2,3O at 60 C with catechol.

raw_value_unit_evidence: Table 1 row SsoC2,3O (60 C), column Catechol: kcat 7.8 +/- 0.6 s^-1; KM 5.9 +/- 0.5 uM; kcat/KM 1.3 uM^-1*s^-1.

row_label: SsoC2,3O (60 C); Catechol


column_label: All required metrics are exact primary Table 1 cells for SsoC2,3O at 25 C with 4-MC.


column_label: All required metrics are primary Table 1 cells for SsoC2,3O at 60 C with 4-MC; exported KM is the rounded mM form of 11.7 uM.

normalized_value_unit_evidence: kcat 4.7 s^-1; KM 0.0117 mM (rounds to exported 0.012 mM); kcat/KM 400 s^-1*mM^-1.


substrate_name: 2,3-dihydroxyphenylpropionic acid (at 20 degrees Celsius and pH 8)

column_label: Table II; row 2,3-Dihydroxyphenylpropionate; column Km (uM); cell value 26.

normalized_value_unit_evidence: Km 26 uM = 0.026 mM exactly.

raw_value_unit_evidence: Table II; row 2,3-Dihydroxyphenylpropionate; column Km (uM): 26 uM.

table_label: Table II. Substrate specificity of MhpB


column_label: Table II; row 3-Methylcatechol; column Km (uM); cell value 90.

normalized_value_unit_evidence: Km 90 uM = 0.090 mM exactly.

raw_value_unit_evidence: Table II; row 3-Methylcatechol; column Km (uM): 90 uM.

substrate: 3-methylcatechol (at 20 degrees Celsius and pH 8)


enzyme_display_name: arachidonate 12-lipoxygenase

smiles: CCCCC/C=C\C/C=C\C/C=C\C/C=C\CCCC(=O)O

enzyme: arachidonate 12-lipoxygenase


enzyme_display_name: arachidonate 15-lipoxygenase

enzyme: arachidonate 15-lipoxygenase


enzyme_display_name: chloridazon-catechol dioxygenase

organism: Phenylobacterium immobile

enzyme: chloridazon-catechol dioxygenase


organism: Brevibacterium fuscum

proof_lines:
homoprotocatechuate 2,3-dioxygenase
3,4-dihydroxyphenylacetate
single-turnover kinetics


proof_lines:
homoprotocatechuate 2,3-dioxygenase
4-nitrocatechol
transient kinetics


enzyme_display_name: stizolobinate synthase

organism: Stizolobium hassjoo

substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

enzyme: stizolobinate synthase

substrate: NADP+


organism: Solanum tuberosum


substrate_name: bishomo-gamma-linolenic acid

smiles: CCCCCC=CCC=CCC=CCCCCCCC(=O)O

substrate: bishomo-gamma-linolenic acid


substrate_name: linoleic acid

smiles: CCCCCC=CCC=CCCCCCCCC(=O)O

substrate: linoleic acid


substrate_name: 1-linoleoyl lysophosphatidic acid

substrate: 1-linoleoyl lysophosphatidic acid


enzyme_display_name: hydroxyquinol 1,2-dioxygenase

organism: Streptomyces rochei

substrate_name: Hydroxyquinol

enzyme: hydroxyquinol 1,2-dioxygenase

substrate: Hydroxyquinol


organism: Glycine max


organism: Myxococcus fulvus

substrate_name: 5,8,11,14,17-eicosapentaenoic acid

smiles: CCC=CCC=CCC=CCC=CCC=CCCCC(=O)O

proof_lines: pH 7.4, temperature not specified in the publication

substrate: 5,8,11,14,17-eicosapentaenoic acid


organism: Pimelobacter simplex


organism: Oncorhynchus mykiss


substrate_name: Linoleate; O2

assay_conditions_summary: pH 7.5; 298.15 K; buffer 25 mM HEPES

proof_lines: pH 7.5, temperature not specified in the publication

proof_lines: apparent value, Ki above 0.00001 mM, in 25 mM HEPES buffer (pH 7.5), 0.01% (v/v) Triton X-100, at 23°C

substrate: Linoleate; O2


organism: Plexaura porosa


organism: Azotobacter sp.


organism: Cutaneotrichosporon cutaneum


organism: Homo sapiens

proof_lines:
at 15°C, normalized to iron content
at pH 7
at pH 8


organism: Oryctolagus cuniculus

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P12530 and applied mutation signature L367K to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; buffer 13S-HpODE (2 uM) in 0.1 M potassium phosphate

column_label: Table 1 (Enzyme characteristics of different mutants), row 'L367K'; column 'kcat, s^-1' = 0.3 +/- 0.01; column 'kcat/KM^S, s^-1 uM^-1' with the footnote '*S, linoleic acid.' = 0.08 +/- 0.01; column 'KM^O2, uM' = 9.0 +/- 1.8; column 'kcat/KM^O2, s^-1 uM^-1' = 0.03 +/- 0.01.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.3 s^-1; the printed unit is already s^-1 and no unit conversion applies; the exported value is 0.3 s^(-1). Km: printed Table 1 cell 9.0 uM; 9.0 / 1000 = 0.009 mM; the exported value is 0.009 mM. kcat/Km: printed Table 1 cell 0.03 s^-1 uM^-1; 1 s^-1 uM^-1 is 1000 s^-1 mM^-1, so 0.03 x 1000 = 30.0 s^-1 mM^-1. The quotient of the same row's two printed component cells is 0.3 / 0.009 = 33.333333333333336 s^-1 mM^-1, which is the exported catalytic efficiency; that quotient expressed in the printed unit is 0.03333333333333333 s^-1 uM^-1, and the printed cell 0.03 is that quotient rounded to the two decimals the table prints.

row_label: Table 1, row 'L367K'

table_label: Table 1: Enzyme characteristics of different mutants (Proc Natl Acad Sci U S A 2007, 104(33):13319-13324)