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

organism: Escherichia coli

source_db: brenda

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

source_license: CC BY 4.0

km_unit: mM

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

enzyme: FMN-dependent NADH-azoreductase

status: unverified

source: brenda


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)

organism: Homo sapiens

substrate_name: mitomycin C

km_display: Not reported

ki_unit: mM

enzyme: NAD(P)H dehydrogenase (quinone)

substrate: mitomycin C


enzyme_display_name: nitrate reductase (NADH)

organism: Glycine max

substrate_name: nitrate

assay_conditions_summary: cofactor NADH

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


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


enzyme_display_name: L-ascorbate peroxidase

organism: Crocus sativus

protein_accession_database: UniProt

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

smiles: OO

assay_conditions_summary: pH 8

data_origin: experimental

enzyme: L-ascorbate peroxidase


substrate_name: L-ascorbate

substrate: L-ascorbate


organism: Citrus limon

source_db: oed

source: oed


kcat_over_km_origin: calculated


enzyme_display_name: UniProt P36969

substrate_name: tert-butyl hydroperoxide

source_db: skid

source_license: CC BY-NC-ND 4.0

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

smiles: CC(C)(C)OO

enzyme: UniProt P36969

substrate: tert-butyl hydroperoxide

source: skid


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


smiles: O=O

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

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

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

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

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

mutation_type: substitution

substrate: ferricytochrome b5


assay_conditions_summary: cofactor NADPH


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

assay_conditions_summary: pH 7

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


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


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

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

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)

source_db: uniprot

enzyme: Sulfhydrogenase 1 subunit alpha

source: uniprot


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


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

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

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

sequence_source: multiple

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)


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

source_databases_merged: brenda uniprot


enzyme_display_name: persulfide dioxygenase

substrate_name: S-sulfanylglutathione

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C161Y with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

enzyme: persulfide dioxygenase

substrate: S-sulfanylglutathione


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


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R163W with inferred residue-numbering offset -4 to reconstruct the assayed variant sequence.


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


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

substrate: L-Cysteine


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+

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_ec_organism_unique and applied mutation signature L367K to reconstruct the assayed variant sequence.

smiles: O=O

proof_lines: pH 7.4, mutant L367K, with substrate linoleic acid


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L367E to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, mutant L367E, with substrate linoleic acid


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L367W to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, mutant L367W, with substrate linoleic acid


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature L367F to reconstruct the assayed variant sequence.

proof_lines: pH 7.4, mutant L367F, with substrate linoleic acid


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

proof_lines: pH 7.4, wild-type enzyme, with substrate linoleic acid


organism: Sporotrichum pulverulentum


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R403L to reconstruct the assayed variant sequence.


substrate_name: methyl arachidonate

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

substrate: methyl arachidonate


enzyme_display_name: UniProt O15296

proof_lines: kcat is 2 sec(-1) for (5Z,8Z,11Z,14Z)-eicosatetraenoate. kcat is 2.1 sec(-1) for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-glycine. kcat is 2 sec(-1) for N-(5Z,8Z,11Z,14Z)-eicosatetraenoyl-alanine. kcat is 2 sec(-1) for N-(5Z,8Z,11Z,14Z)-eicosatet

enzyme: UniProt O15296


enzyme_display_name: Polyunsaturated fatty acid lipoxygenase ALOX15B

substrate_name: linoleate (isoform A at pH 7.4 and 20 degrees Celsius)

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


substrate_name: (5Z,8Z,11Z,14Z)-eicosatetraenoate (isoform A at pH 7.4 and 20 degrees Celsius)

smiles: CCC=CCC=CCC=CCC=CCCCCCCC(=O)[O-]

enzyme: Polyunsaturated fatty acid lipoxygenase ALOX15B


enzyme_display_name: Polyunsaturated fatty acid lipoxygenase ALOX15

proof_lines: kcat is 22.2 sec(-1) with (5Z,8Z,11Z,14Z)-eicosatetraenoate as substrate (PubMed:15123652). kcat is 1.34 sec(-1) with (12S)-hydroperoxy-(5Z,8Z,10E,14Z)-eicosatetraenoate as substrate (PubMed:15123652).


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

enzyme: Polyunsaturated fatty acid lipoxygenase ALOX15


proof_lines: kcat is 14.4 sec(-1) with (9Z,12Z)-octadecadienoate as substrate.


smiles: CCCCCC=CCC=CCC=CC=CC(CCCC(=O)[O-])O


smiles: CCCCCC=CCC=CCC=CC=CC(CCCC(=O)[O-])OO


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F353L to reconstruct the assayed variant sequence.


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


organism: Sus scrofa

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M367V with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.


substrate_name: anandamide (Sf9-expressed enzyme)

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

substrate: anandamide (Sf9-expressed enzyme)


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


organism: Pseudomonas aeruginosa

proof_lines: pH 6.5, 22°C, recombinant His6-tagged enzyme

source_databases_merged: brenda skid


proof_lines: pH 7.5, 22°C, recombinant His6-tagged enzyme

proof_lines: pH 7.0, 22°C, recombinant His6-tagged enzyme


assay_conditions_summary: buffer HEPES


enzyme_display_name: UniProt Q5PXQ6

proof_lines: 5-chlorohydroxyquinols and 6-chloro-chlorohydroxyquinols are also substrates.

enzyme: UniProt Q5PXQ6


assay_conditions_summary: pH 7.5; 294.15 K; cofactor ATP

proof_lines: pH 7.5, 25°C, HPLC analysis, 8-HETE formation

proof_lines: pH 7.5, 25°C, UV?Vis spectrophotometric analysis

proof_lines: pH 8.0, temperature not specified in the publication


smiles: CCCCCC=CCC=CCC=CC=CC(CCCC(=O)O)OO

proof_lines: pH 7.5, 21°C, recombinant enzyme, with 0.2 mM ATP


substrate_name: O2; Arachidonate

substrate: O2; Arachidonate


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

source_databases_merged: sabio_rk skid uniprot


substrate_name: Arachidonate; O2

substrate: Arachidonate; O2


sequence_variant_note: Mutation signature L353L could not be applied safely because the resolved sequence does not match the expected reference residue(s).


enzyme_display_name: Polyunsaturated fatty acid lipoxygenase ALOX12

substrate_name: arachidonic acid

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

column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row pl12-LO / Arachidonic acid; Km 9.5 +/- 0.7 uM; normalized km 0.0095 mM; enzyme label: human platelet-type 12-LO

row_label: pl12-LO / Arachidonic acid


substrate_name: N-arachidonoylglycine

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

column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row pl12-LO / N-Arachidonyl glycine; Km 10.1 +/- 0.8 uM; normalized km 0.0101 mM; enzyme label: human platelet-type 12-LO

row_label: pl12-LO / N-Arachidonyl glycine

enzyme: Polyunsaturated fatty acid lipoxygenase ALOX12

substrate: N-arachidonoylglycine


substrate_name: N-arachidonoyl-L-alanine

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

column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row pl12-LO / N-Arachidonyl alanine; Km 15.7 +/- 0.8 uM; normalized km 0.0157 mM; enzyme label: human platelet-type 12-LO

row_label: pl12-LO / N-Arachidonyl alanine

substrate: N-arachidonoyl-L-alanine


substrate_name: N-arachidonoyl-gamma-aminobutyric acid

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

column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row pl12-LO / N-Arachidonyl-gamma-aminobutyric acid; Km 10.9 +/- 0.5 uM; normalized km 0.0109 mM; enzyme label: human platelet-type 12-LO

substrate: N-arachidonoyl-gamma-aminobutyric acid


proof_lines: pH 7.5, 25°C, UV-Vis spectrophotometric analysis

source_databases_merged: sabio_rk brenda uniprot


organism: Nocardioides simplex

substrate_name: Benzene-1,2,4-triol; O2

substrate: Benzene-1,2,4-triol; O2


substrate: arachidonic acid


column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row h15-LO-2 / N-Arachidonyl glycine; Km 11.0 +/- 0.4 uM; normalized km 0.011 mM; enzyme label: human 15-LO-2

row_label: h15-LO-2 / N-Arachidonyl glycine


column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row h15-LO-2 / N-Arachidonyl alanine; Km 6 +/- 3 uM; normalized km 0.006 mM; enzyme label: human 15-LO-2

row_label: h15-LO-2 / N-Arachidonyl alanine


column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row h15-LO-2 / N-Arachidonyl-gamma-aminobutyric acid; Km 8 +/- 2 uM; normalized km 0.008 mM; enzyme label: human 15-LO-2


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

column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row lk12-LO / Arachidonic acid; Km 7.8 +/- 1.3 uM; normalized km 0.0078 mM; enzyme label: porcine leukocyte-type 12-LO

row_label: lk12-LO / Arachidonic acid


column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row lk12-LO / N-Arachidonyl glycine; Km 8.0 +/- 0.7 uM; normalized km 0.008 mM; enzyme label: porcine leukocyte-type 12-LO

row_label: lk12-LO / N-Arachidonyl glycine


column_label: Table 2. Kinetic parameters of metabolism of arachidonate and arachidonyl amino acids; row lk12-LO / N-Arachidonyl-gamma-aminobutyric acid; Km 7.8 +/- 0.7 uM; normalized km 0.0078 mM; enzyme label: porcine leukocyte-type 12-LO


organism: Rhodococcus sp

substrate_name: catechol (at pH 8.1 and 8 degrees Celsius)

proof_lines:
Rhodococcus ohp operon
catechol


substrate_name: 3-methylcatechol (at pH 8.1 and 8 degrees Celsius)


enzyme_display_name: cysteamine dioxygenase

substrate_name: cysteamine

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

smiles: C(CS)N

enzyme: cysteamine dioxygenase

substrate: cysteamine


smiles: O=O


substrate_name: arachidonate

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature L183E/L187E to reconstruct the assayed variant sequence.

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

substrate: arachidonate


substrate_name: linoleic acid

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

assay_conditions_summary: pH 7.4; buffer HEPES

column_label: Results prose/Table 1 reports linoleic acid Km 12.1 microM and Vm 545 units/mg protein for reticulocyte LOX.

raw_value_unit_evidence: Km raw_value=12.1 microM raw_unit=microM

row_label: rabbit reticulocyte lipoxygenase / linoleic acid

table_label: ScienceDirect full text Table 1 / Results prose


substrate_name: dilinoleoyl phosphatidylcholine

substrate: dilinoleoyl phosphatidylcholine


enzyme_display_name: UniProt O32085

organism: Bacillus subtilis

substrate_name: L-cysteine

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

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)

enzyme: UniProt O32085

substrate: L-cysteine


substrate_name: cysteine

substrate: cysteine


enzyme_display_name: cysteine dioxygenase

substrate_name: L-Cysteine

enzyme: cysteine dioxygenase

substrate: L-Cysteine


substrate_name: eicosa-5,8,11,14,17-pentaenoate (at pH 7.0 and 37 degrees Celsius)


enzyme_display_name: pyrogallol 1,2-oxygenase

substrate_name: 1,2,3-Trihydroxybenzene; O2

enzyme: pyrogallol 1,2-oxygenase

substrate: 1,2,3-Trihydroxybenzene; O2


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)


column_label: Table 1 columns CDO construct, pH optimum, Cysteine Km (mM), kcat (s^-1), and kcat/Km (mM^-1 s^-1); row SCO3035.

normalized_value_unit_evidence: kcat 0.33 s^-1; Km 1.2 mM; printed kcat/Km 0.3 s^-1 mM^-1.

raw_value_unit_evidence: Table 1 row SCO3035: Cysteine Km 1.2 mM; kcat 0.33 s^-1; kcat/Km 0.3 mM^-1 s^-1.

row_label: SCO3035 (Streptomyces coelicolor A3(2) CDO homolog)


substrate_name: linoleate

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

proof_lines:
11-thialinoleic acid
human reticulocyte 15-lipoxygenase-1
linoleic acid

substrate: linoleate


proof_lines:
human 12-lipoxygenase
human 15-lipoxygenase-1
human 15-lipoxygenase-2


enzyme_display_name: UniProt P32440

organism: Methanothermobacter marburgensis

enzyme: UniProt P32440


substrate: linoleic acid


enzyme_display_name: catechol 1,2-dioxygenase

organism: Corynebacterium glutamicum

substrate_name: catechol

column_label: Abstract reports Km and Vmax were 4.24 micromol l(-1) and 3.7 micromol l(-1) min(-1) mg(-1).

raw_value_unit_evidence: Km raw_value=4.24 micromol l(-1) raw_unit=microM

row_label: Catechol 1,2-dioxygenase / catechol

table_label: PubMed XML abstract PMID 15168857

enzyme: catechol 1,2-dioxygenase

substrate: catechol


organism: Stenotrophomonas maltophilia

assay_conditions_summary: pH 8


organism: Cupriavidus campinensis


enzyme_display_name: 2-aminoethanethiol dioxygenase

organism: Mus musculus

assay_conditions_summary: pH 8; buffer 50 mM Tris borate

column_label: Official ScienceDirect article page, Figure 4D legend and Results paragraph, cysteamine concentration-dependence assay at pH 8.0, reports Km = 3.8 mM for ADO protein.

normalized_value_unit_evidence: Paper Figure 4D/Results Km is 3.8 mM, matching the export Km 3.8 mM.

raw_value_unit_evidence: Figure 4D legend and Results paragraph report Km = 3.8 mM for cysteamine dioxygenase activity of ADO.

row_label: wild-type ADO with cysteamine at pH 8.0

table_label: Figure 4. Kinetic analyses of purified wild-type ADO protein

enzyme: 2-aminoethanethiol dioxygenase


enzyme_display_name: persulfide dioxygenase

organism: Acidithiobacillus caldus

substrate_name: glutathione

enzyme: persulfide dioxygenase

substrate: glutathione


enzyme_display_name: UniProt O31266

organism: Paenarthrobacter nitroguajacolicus

proof_lines:
Raw SKiD Env: Temp=5°C, pH=6.5
Raw SKiD Env: Temp=5°C, pH=10.5
Raw SKiD Env: Temp=-----, pH=-----

enzyme: UniProt O31266


enzyme_display_name: UniProt B3U4H7

organism: Nitrospira defluvii

substrate_name: Chlorite

smiles: [O-]Cl=O

enzyme: UniProt B3U4H7

substrate: Chlorite


enzyme_display_name: UniProt B8HNS6

organism: Cyanothece sp. PCC 7425

proof_lines:
Raw SKiD Env: Temp=30°C, pH=7
Raw SKiD Env: Temp=30°C, pH=9
Raw SKiD Env: Temp=25°C, pH=5

enzyme: UniProt B8HNS6


enzyme_display_name: UniProt Q8PDA8

organism: Xanthomonas campestris

enzyme: UniProt Q8PDA8


substrate_name: L-tryptophan

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

substrate: L-tryptophan


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


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)


organism: Homo sapiens

substrate_name: S-carboxymethyl-L-cysteine

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

proof_lines:
human hepatic cytosol
S-oxidations
l-Cysteine

substrate: S-carboxymethyl-L-cysteine


organism: Pseudomonas aeruginosa

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


enzyme_display_name: indoleamine 2,3-dioxygenase

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

proof_lines: H55A mutant enzyme, O2 not present at a saturating level

enzyme: indoleamine 2,3-dioxygenase


proof_lines: H55S mutant enzyme, O2 not present at a saturating level


proof_lines: pH and temperature not specified in the publication


substrate_name: L-Trp

substrate: L-Trp


enzyme_display_name: 4-hydroxymandelate synthase

substrate_name: 4-nitrophenylpyruvic acid

enzyme: 4-hydroxymandelate synthase

substrate: 4-nitrophenylpyruvic acid


substrate_name: 2-oxo-4-phenylbutanoic acid

substrate: 2-oxo-4-phenylbutanoic acid


substrate_name: phenylpyruvic acid

substrate: phenylpyruvic acid


organism: Blepharisma stoltei

proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme H127E


proof_lines: pH 8.0, temperature not specified in the publication, wild-type enzyme


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme N127T


proof_lines: pH 8.0, temperature not specified in the publication, mutant enzyme E132H


proof_lines: HOD mutant H102L, pH not specified in the publication, temperature not specified in the publication


proof_lines: HOD mutant H38A, pH not specified in the publication, temperature not specified in the publication


proof_lines: HOD mutant S101A, pH not specified in the publication, temperature not specified in the publication


proof_lines: HOD mutant H251A, pH not specified in the publication, temperature not specified in the publication


proof_lines: HOD mutant D126A, pH not specified in the publication, temperature not specified in the publication


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


enzyme_display_name: chlorite O2-lyase

proof_lines:
mutant enzyme Q74E, at pH 9.0 and 30°C
mutant enzyme Q74E, at pH 7.0 and 30°C
mutant enzyme Q74E, at pH 5.0 and 30°C

enzyme: chlorite O2-lyase


proof_lines:
wild type enzyme, at pH 9.0 and 30°C
wild type enzyme, at pH 7.0 and 30°C
wild type enzyme, at pH 5.0 and 30°C


proof_lines:
mutant enzyme Q74V, at pH 9.0 and 30°C
mutant enzyme Q74V, at pH 7.0 and 30°C
mutant enzyme Q74V, at pH 5.0 and 30°C


enzyme_display_name: UniProt A0A0M3KL46

organism: Magnetospirillum sp.

proof_lines:
Raw SKiD Env: Temp=10°C, pH=6.5
Raw SKiD Env: Temp=10°C, pH=6
Raw SKiD Env: Temp=10°C, pH=5.5

enzyme: UniProt A0A0M3KL46


substrate_name: D-tryptophan

substrate: D-tryptophan


organism: Paenarthrobacter ilicis


proof_lines: 30°C, pH 8.0, with 3-hydroxy-2-methyl-1H-quinolin-4-one


organism: Micromonospora sp.


substrate_name: serotonin

substrate: serotonin


substrate_name: indole

substrate: indole


organism: Arabidopsis thaliana

substrate_name: 3-(4-Hydroxyphenyl)pyruvate; O2

substrate: 3-(4-Hydroxyphenyl)pyruvate; O2


organism: Azospira oryzae

substrate_name: chloride

substrate: chloride


organism: Dechloromonas agitata


substrate_name: Unknown

substrate: Unknown


organism: Pseudomonas fluorescens


organism: Klebsiella pneumoniae


organism: Nitrobacter winogradskyi


organism: Anopheles gambiae


organism: Branchiostoma floridae


organism: Brevibacillus brevis


organism: Cyanothece sp. PCC 7425


organism: Delftia acidovorans

assay_conditions_summary: pH 7

proof_lines:
pH 7.0
activated by 0.033 mM Cd2+


organism: Gallus gallus

substrate_name: O2; L-Tryptophan

substrate: O2; L-Tryptophan


organism: Meriones unguiculatus

proof_lines:
indoleamine 2,3-dioxygenase
pH 6.5, 37°C


organism: Monosiga brevicollis


organism: Haliotis diversicolor


organism: Mus musculus

assay_conditions_summary: pH 7.4; 310.15 K; buffer 100 mM phosphate; cofactor NADPH

proof_lines: IDO2, pH and temperature not specified in the publication


organism: Pelodiscus sinensis japonicus


organism: Streptomyces parvulus


assay_conditions_summary: pH 7.5; 310.15 K; buffer 100 mM phosphate; cofactor NADPH

proof_lines:
pH 7.5, 37°C, 5 min incubation time
pH 6.5, 37°C
37°C, pH 6.5


organism: Nematostella vectensis


organism: Paenarthrobacter nitroguajacolicus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E224A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196K with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196K/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant Y196K/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196R with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196R/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant Y196R/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y196A/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant Y196A/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S101A with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S101A/C69S with inferred residue-numbering offset -32 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant S101A/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H102Q with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H102Q/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant H102Q/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S220N with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S220N/C69S with inferred residue-numbering offset -32 to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant S220N/C69S


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F219Y with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F219Y/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant F219Y/C69S


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature C69S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E224A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E224A/C69S to reconstruct the assayed variant sequence.

proof_lines: pH 8.0, 30°C, recombinant mutant E224A/C69S


organism: Amycolatopsis orientalis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T214P to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature I216N with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S201A to reconstruct the assayed variant sequence.


enzyme_display_name: acetylacetone-cleaving enzyme

organism: Acinetobacter johnsonii

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y70F to reconstruct the assayed variant sequence.

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

enzyme: acetylacetone-cleaving enzyme


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F59A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F115A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F119A to reconstruct the assayed variant sequence.


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


assay_conditions_summary: pH 7.5; buffer 20 mM Tris/HCl

proof_lines: wild type enzyme, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y70A/R80A/E98A to reconstruct the assayed variant sequence.

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

proof_lines: pH 7.5, 25°C, recombinant mutant Y70A/R80A/E98A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y70F/R80A/E98A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant mutant Y70F/R80A/E98A


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E98Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E98A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R80A/E98A to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 25°C, recombinant mutant R80A/E98A


sequence_variant_note: Mutation signature T107A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R80A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y70A to reconstruct the assayed variant sequence.


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

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


organism: Nitrospira defluvii

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R137A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature R137K with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.


enzyme_display_name: UniProt P14902

organism: Homo sapiens

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

proof_lines: Catalytic efficiency for L-tryptophan is 150 times higher than for D-tryptophan.

enzyme: UniProt P14902


enzyme_display_name: Indoleamine 2,3-dioxygenase 1

proof_lines: Catalytic efficiency for L-tryptophan is 90 times higher than for D-tryptophan.

enzyme: Indoleamine 2,3-dioxygenase 1


organism: Oryctolagus cuniculus

substrate_name: D-Trp

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

assay_conditions_summary: pH 6

substrate: D-Trp


smiles: CCCC(=O)C(=CO)O

proof_lines:
Co2+ bound enzyme, pH 7.0, 25°C
Ni2+ bound enzyme, pH 7.0, 25°C


organism: Pseudomonas putida

substrate_name: O2; 3-Hydroxy-1H-quinolin-4-one

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

substrate: O2; 3-Hydroxy-1H-quinolin-4-one


organism: Anolis carolinensis

substrate_name: L-Tryptophan; O2

substrate: L-Tryptophan; O2


organism: Aspergillus oryzae

assay_conditions_summary: pH 6.5; 310.15 K; buffer 500 ul of 50 mM potassium phosphate

column_label: Table 1: Kinetic parameters of bacterially-expressed fungal IDOs (J Mol Evol 2011, volume 72, pages 160-168); printed column heads enzyme form | pH | L-Trp VmaxTON (min^-1) | L-Trp Km | L-Trp VmaxTON/Km (uM^-1/min) | D-Trp VmaxTON (min^-1) | D-Trp Km (mM) | D-Trp VmaxTON/Km (uM^-1/min); the table footnote defines TON as turnover number (mol of product/mol of holoenzyme/min). Table 1, enzyme-form row A. oryzae IDOa at pH 6.5, L-Trp column group; column VmaxTON (min^-1) = 50.4; column Km (uM) = 154; column VmaxTON/Km (uM^-1/min) = 0.3. captured primary segment: A. oryzae IDOa | L-Trp | kcat (VmaxTON) 50.4 min^-1 | Km 154 uM | kcat/Km (VmaxTON/Km) 0.3 uM^-1 min^-1

normalized_value_unit_evidence: Km: printed Table 1 cell 154 uM; 1 uM is 0.001 mM, so 154 / 1000 = 0.154 mM; the exported value is 0.154 mM. kcat: printed Table 1 cell 50.4 min^-1; 1 min^-1 is 1/60 s^-1, so 50.4 / 60 = 0.84 s^(-1); the exported value is 0.84 s^(-1). kcat/Km: printed Table 1 cell 0.3 uM^-1 min^-1; 1 uM^-1 min^-1 is 1000/60 s^-1 mM^-1, so 0.3 x 1000 / 60 = 5.0 s^(-1)*mM^(-1). The live export row carries no catalytic-efficiency field, so this pass exports none; the printed cell is transcribed in the typed kcat_over_km_provenance only.

raw_value_unit_evidence: Table 1, enzyme-form row A. oryzae IDOa at pH 6.5, L-Trp column group: Km = 154 uM; kcat (printed VmaxTON) = 50.4 min^-1; printed kcat/Km (printed VmaxTON/Km) = 0.3 uM^-1 min^-1.


organism: Branchiostoma floridae


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E69Q to reconstruct the assayed variant sequence.

proof_lines: mutant enzyme E69Q, using 0.2 mM pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C


proof_lines: native enzyme, using 0.09 mM 1,1,1-trifluoro-pentane-2,4-dione in 20 mM Tris/HCl buffer at pH 7.5 and 25°C


proof_lines:
apparent value at 25°C
Strep-tagged enzyme
recombinant enzyme


organism: Ornithorhynchus anatinus


organism: Danio rerio


organism: Monodelphis domestica


organism: Monosiga brevicollis


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


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D120A to reconstruct the assayed variant sequence.

proof_lines: QDO mutant D120A, pH not specified in the publication, temperature not specified in the publication


organism: Dechloromonas aromatica (nom. nud.)

substrate_name: Chlorite

proof_lines: kcat is 4.53 min(-1) with chlorite as substrate.

substrate: Chlorite


enzyme_display_name: Chlorite dismutase

organism: Ideonella dechloratans

enzyme: Chlorite dismutase


organism: Stutzerimonas chloritidismutans

proof_lines: 100 mM sodium phosphate buffer, pH 6.0, 25°C


organism: Oryzias latipes


organism: Saccharomyces cerevisiae


organism: Sulculus diversicolor


organism: Xenopus laevis


organism: Klebsiella oxytoca

substrate_name: O2; 1,2-Dihydroxyhex-1-en-3-one

column_label: Table 3 columns are ARD and ARD'. In the ARD column, KmII (uM)=50 and kcat (s^-1)=5.0 x 10^2; Figure 1 caption identifies ARD (Ni2+) initial velocity versus II at constant O2.

normalized_value_unit_evidence: KmII normalized_value=0.05 normalized_unit=mM; kcat normalized_value=500 normalized_unit=s^-1

raw_value_unit_evidence: KmII raw_value=50 raw_unit=uM; kcat raw_value=5.0 x 10^2 raw_unit=s^-1

row_label: ARD column; KmII row and kcat row

table_label: ACS PDF page 5 / journal page 6383, Table 3: Kinetic Constants of ARD and ARD'

substrate: O2; 1,2-Dihydroxyhex-1-en-3-one


organism: Oryza sativa

substrate_name: 1,2-Dihydroxy-3-ketopent-1-ene; O2

substrate: 1,2-Dihydroxy-3-ketopent-1-ene; O2


organism: Acinetobacter johnsonii


enzyme_display_name: 9-cis-epoxycarotenoid dioxygenase

organism: Vigna unguiculata

enzyme: 9-cis-epoxycarotenoid dioxygenase


enzyme_display_name: 9-cis-epoxycarotenoid dioxygenase 1, chloroplastic

organism: Zea mays

substrate_name: 9-cis antheraxanthin

proof_lines: Vmax with 9-cis violaxanthin as substrate is more than twice the Vmax with 9-cis neoxanthin as substrate.

substrate: 9-cis antheraxanthin


enzyme_display_name: Acireductone dioxygenase

organism: Mus musculus

substrate_name: 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one (using iron as cofactor)

proof_lines: kcat is 114.3 sec(-1) with 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one as substrate (using iron as cofactor) (PubMed:26858196). kcat is 7.55 sec(-1) with 1,2-dihydroxy-5-(methylsulfanyl)pent-1-en-3-one as substrate (using cobalt as cofa

enzyme: Acireductone dioxygenase


substrate_name: 9-cis violaxanthin

column_label: ScienceDirect HTML, Table 1, row 9cViol, column Km (uM).

raw_value_unit_evidence: Table 1 9cViol Km (uM): 58 uM

enzyme: 9-cis-epoxycarotenoid dioxygenase 1, chloroplastic

substrate: 9-cis violaxanthin


organism: Homo sapiens

column_label: Table 3 (journal page 2161), row 'IDO1, 1-Me-D-Trp': column 'kcat (s-1)' = 0.095; column 'Km (lM)' = 660; the table prints no kcat/Km column.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.095 s^-1 needs no conversion and is the exported 0.095 s^(-1). Km: printed Table 3 cell 660 uM divided by 1000 is 0.66 mM. kcat/Km: Table 3 prints no ratio cell for this row, so the ratio is the exact quotient of the same row's two printed cells, 0.095 / 0.66 = 0.14393939393939392 s^-1 mM^-1.

raw_value_unit_evidence: The reviewed primary row is in Table 3, journal page 2161. The printed enzyme/substrate row is IDO1, 1-Me-D-Trp. The assay enzyme is recombinant human IDO1. The varied substrate is 1-Me-D-Trp. The Table 3 assay condition is 100 mM KPi pH 6.5, 25 C, aerobic. Table 3, IDO1, 1-Me-D-Trp: kcat 0.095 s^-1. Table 3, IDO1, 1-Me-D-Trp: Km 660 uM. Table 3 prints kcat and Km only for IDO1, 1-Me-D-Trp and carries no catalytic-efficiency column, so this paper prints no ratio cell for that row.

row_label: IDO1, 1-Me-D-Trp

table_label: Table 3: kinetic parameters, journal page 2161


proof_lines:
indoleamine 2,3-dioxygenase-2
substrate specificity
tryptophan derivatives


column_label: Table 1 (journal page 2158), row 'IDO2, 5-F-D,L-Trp': column 'kcat (s-1)' = 0.049; column 'Km (lM)' = 1768; column 'kcat/Km (M-1s-1)' = 28.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.049 s^-1 needs no conversion and is the exported 0.049 s^(-1). Km: printed Table 1 cell 1768 uM divided by 1000 is 1.768 mM. kcat/Km: printed Table 1 cell 28 M^-1 s^-1 multiplied by 0.001 is 0.028 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.049 / 1.768, is 0.027714932126696835 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, 5-F-D,L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is 5-F-D,L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, 5-F-D,L-Trp: kcat 0.049 s^-1. Table 1, IDO2, 5-F-D,L-Trp: Km 1768 uM. Table 1, IDO2, 5-F-D,L-Trp: printed kcat/Km 28 M^-1 s^-1.

row_label: IDO2, 5-F-D,L-Trp

table_label: Table 1: kinetic parameters, journal page 2158


column_label: Table 1 (journal page 2158), row 'IDO2, 5-MeO-D,L-Trp': column 'kcat (s-1)' = 0.161; column 'Km (lM)' = 547; column 'kcat/Km (M-1s-1)' = 294.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.161 s^-1 needs no conversion and is the exported 0.161 s^(-1). Km: printed Table 1 cell 547 uM divided by 1000 is 0.547 mM. kcat/Km: printed Table 1 cell 294 M^-1 s^-1 multiplied by 0.001 is 0.294 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.161 / 0.547, is 0.29433272394881166 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, 5-MeO-D,L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is 5-MeO-D,L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, 5-MeO-D,L-Trp: kcat 0.161 s^-1. Table 1, IDO2, 5-MeO-D,L-Trp: Km 547 uM. Table 1, IDO2, 5-MeO-D,L-Trp: printed kcat/Km 294 M^-1 s^-1.

row_label: IDO2, 5-MeO-D,L-Trp


column_label: Table 1 (journal page 2158), row 'IDO2, 5-Me-D,L-Trp': column 'kcat (s-1)' = 0.36; column 'Km (lM)' = 1570; column 'kcat/Km (M-1s-1)' = 229.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.36 s^-1 needs no conversion and is the exported 0.36 s^(-1). Km: printed Table 1 cell 1570 uM divided by 1000 is 1.57 mM. kcat/Km: printed Table 1 cell 229 M^-1 s^-1 multiplied by 0.001 is 0.229 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.36 / 1.57, is 0.22929936305732482 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, 5-Me-D,L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is 5-Me-D,L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, 5-Me-D,L-Trp: kcat 0.36 s^-1. Table 1, IDO2, 5-Me-D,L-Trp: Km 1570 uM. Table 1, IDO2, 5-Me-D,L-Trp: printed kcat/Km 229 M^-1 s^-1.

row_label: IDO2, 5-Me-D,L-Trp


column_label: Table 1 (journal page 2158), row 'IDO2, 6-Me-D,L-Trp': column 'kcat (s-1)' = 0.108; column 'Km (lM)' = 3457; column 'kcat/Km (M-1s-1)' = 31.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.108 s^-1 needs no conversion and is the exported 0.108 s^(-1). Km: printed Table 1 cell 3457 uM divided by 1000 is 3.457 mM. kcat/Km: printed Table 1 cell 31 M^-1 s^-1 multiplied by 0.001 is 0.031 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.108 / 3.457, is 0.031240960370263235 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, 6-Me-D,L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is 6-Me-D,L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, 6-Me-D,L-Trp: kcat 0.108 s^-1. Table 1, IDO2, 6-Me-D,L-Trp: Km 3457 uM. Table 1, IDO2, 6-Me-D,L-Trp: printed kcat/Km 31 M^-1 s^-1.

row_label: IDO2, 6-Me-D,L-Trp


substrate_name: D-Tryptophan

substrate: D-Tryptophan


column_label: Table 1 (journal page 2158), row 'IDO2, 1-Me-L-Trp': column 'kcat (s-1)' = 0.011; column 'Km (lM)' = 696; column 'kcat/Km (M-1s-1)' = 16.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.011 s^-1 needs no conversion and is the exported 0.011 s^(-1). Km: printed Table 1 cell 696 uM divided by 1000 is 0.696 mM. kcat/Km: printed Table 1 cell 16 M^-1 s^-1 multiplied by 0.001 is 0.016 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.011 / 0.696, is 0.015804597701149427 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, 1-Me-L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is 1-Me-L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, 1-Me-L-Trp: kcat 0.011 s^-1. Table 1, IDO2, 1-Me-L-Trp: Km 696 uM. Table 1, IDO2, 1-Me-L-Trp: printed kcat/Km 16 M^-1 s^-1.

row_label: IDO2, 1-Me-L-Trp


substrate_name: L-Tryptophan

column_label: Table 1 (journal page 2158), row 'IDO2, L-Trp': column 'kcat (s-1)' = 0.103; column 'Km (lM)' = 6809; column 'kcat/Km (M-1s-1)' = 15.

normalized_value_unit_evidence: kcat: printed Table 1 cell 0.103 s^-1 needs no conversion and is the exported 0.103 s^(-1). Km: printed Table 1 cell 6809 uM divided by 1000 is 6.809 mM. kcat/Km: printed Table 1 cell 15 M^-1 s^-1 multiplied by 0.001 is 0.015 s^-1 mM^-1, and the exact quotient of the same two printed cells, 0.103 / 6.809, is 0.015127037744162138 s^-1 mM^-1, which is the value this row carries.

raw_value_unit_evidence: The reviewed primary row is in Table 1, journal page 2158. The printed enzyme/substrate row is IDO2, L-Trp. The assay enzyme is recombinant human IDO2. The varied substrate is L-Trp. The Table 1 assay condition is 100 mM KPi pH 7.5, 25 C, aerobic. Table 1, IDO2, L-Trp: kcat 0.103 s^-1. Table 1, IDO2, L-Trp: Km 6809 uM. Table 1, IDO2, L-Trp: printed kcat/Km 15 M^-1 s^-1.

row_label: IDO2, L-Trp

substrate: L-Tryptophan


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F163A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F164A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F226A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F226Y to reconstruct the assayed variant sequence.