substrate_name: diphenylsulfoxide

proof_lines: as electron acceptor under anaerobic conditions

substrate: diphenylsulfoxide


enzyme_display_name: aldehyde oxidase

organism: Cavia porcellus

substrate_name: ferricyanide

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.

proof_lines: as electron acceptor under aerobic conditions

enzyme: aldehyde oxidase

substrate: ferricyanide

status: unverified

source: brenda


organism: Cupriavidus necator


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


enzyme_display_name: cinnamoyl-CoA reductase

organism: Arabidopsis thaliana

substrate_name: caffeoyl-CoA

assay_conditions_summary: cofactor CoA

proof_lines:
recombinant fusion protein GST-AtCCR2
recombinant fusion protein GST-AtCCR1

enzyme: cinnamoyl-CoA reductase

substrate: caffeoyl-CoA


substrate_name: feruloyl-CoA

substrate: feruloyl-CoA


substrate_name: sinapoyl-CoA

substrate: sinapoyl-CoA


enzyme_display_name: Aldehyde oxidase 4

substrate_name: benzoic acid (BA) (at pH7, in the presence of NAD(+))

source_db: uniprot

protein_accession_database: UniProt

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

assay_conditions_summary: pH 7

proof_lines: kcat is 95.2 sec(-1) with benzoic acid (BA) as substrate, 1.904 sec(-1) with indole-3-acetaldehyde as substrate, and 436.5 sec(-1) with cinnamylaldehyde as substrate (at pH 7, PubMed:19297586).

data_origin: experimental

enzyme: Aldehyde oxidase 4

source: uniprot


substrate_name: indole-3-acetaldehyde (at pH7)

substrate: indole-3-acetaldehyde (at pH7)


substrate_name: cinnamylaldehyde (at pH7)

substrate: cinnamylaldehyde (at pH7)


enzyme_display_name: Indole-3-acetaldehyde oxidase

organism: Zea mays

substrate_name: (indol-3-yl)acetaldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)

verification_status: verified

assay_conditions_summary: pH 7.4; buffer pH 7.4

column_label: PMID 12226218 Table II row IAAld, Electron Acceptor O2, column Km (uM), value 3.2; paper abbreviation defines IAAld as indole-3-acetaldehyde; Methods specify product formation in pH 7.4 buffer at 30 deg C.

raw_value_unit_evidence: Km=3.2 uM in Table II row IAAld, O2 Km column.

row_label: IAAld / indole-3-acetaldehyde

table_label: Table II. Kinetic properties of maize AO with various substrates.

enzyme: Indole-3-acetaldehyde oxidase

status: verified


substrate_name: indol-3-aldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)

column_label: PMID 12226218 Table II row Indole-3-aldehyde, Electron Acceptor O2, column Km (uM), value 4.5; Methods specify product formation in pH 7.4 buffer at 30 deg C.

raw_value_unit_evidence: Km=4.5 uM in Table II row Indole-3-aldehyde, O2 Km column.


substrate_name: benzaldehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)

column_label: PMID 12226218 Table II row Benzaldehyde, Electron Acceptor O2, column Km (uM), value 1.5; Methods specify product formation in pH 7.4 buffer at 30 deg C.

raw_value_unit_evidence: Km=1.5 uM in Table II row Benzaldehyde, O2 Km column.

row_label: Benzaldehyde


substrate_name: protocatechualdehyde (at pH 7.4 and 30 degrees Celsius, with O2 as electron acceptor)

column_label: PMID 12226218 Table II row Protocatechualdehyde, Electron Acceptor O2, column Km (uM), value 2.9; Methods specify product formation in pH 7.4 buffer at 30 deg C.

raw_value_unit_evidence: Km=2.9 uM in Table II row Protocatechualdehyde, O2 Km column.

row_label: Protocatechualdehyde


substrate_name: phenylacetaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)

column_label: PMID 12226218 Table II row Phenylacetaldehyde, Electron Acceptor DCIP, column Km (uM), value 250; Methods specify pH 7.4 and 30 deg C assay conditions and DCIP/PMS electron-acceptor assay.

raw_value_unit_evidence: Km=250 uM in Table II row Phenylacetaldehyde, DCIP Km column.

row_label: Phenylacetaldehyde


substrate_name: butyraldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)

column_label: PMID 12226218 Table II row Butyraldehyde, Electron Acceptor DCIP, column Km (uM), value 26; Methods specify pH 7.4 and 30 deg C assay conditions and DCIP/PMS electron-acceptor assay.

raw_value_unit_evidence: Km=26 uM in Table II row Butyraldehyde, DCIP Km column.

row_label: Butyraldehyde


substrate_name: propionaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)

column_label: PMID 12226218 Table II row Propionaldehyde, Electron Acceptor DCIP, column Km (uM), value 74; Methods specify pH 7.4 and 30 deg C assay conditions and DCIP/PMS electron-acceptor assay.

raw_value_unit_evidence: Km=74 uM in Table II row Propionaldehyde, DCIP Km column.

row_label: Propionaldehyde


substrate_name: acetaldehyde (at pH 7.4 and 30 degrees Celsius, with DCIP as electron acceptor)

column_label: PMID 12226218 Table II row Acetaldehyde, Electron Acceptor DCIP, column Km (uM), value 345; Methods specify pH 7.4 and 30 deg C assay conditions and DCIP/PMS electron-acceptor assay.

raw_value_unit_evidence: Km=345 uM in Table II row Acetaldehyde, DCIP Km column.

row_label: Acetaldehyde


enzyme_display_name: salicylaldehyde dehydrogenase

organism: Pseudomonas putida

substrate_name: Salicylaldehyde

enzyme: salicylaldehyde dehydrogenase

substrate: Salicylaldehyde


proof_lines: pH and temperature not specified in the publication


enzyme_display_name: vanillin dehydrogenase

organism: Streptomyces sp. NL15-2K

substrate_name: Vanillin

enzyme: vanillin dehydrogenase

substrate: Vanillin


substrate_name: NAD+

assay_conditions_summary: pH 9.5; cofactor NAD+


organism: Lysinibacillus sphaericus

substrate_name: NADP+


proof_lines:
with NADP+
with NAD+


organism: Rattus norvegicus

proof_lines: in the presence of 1 mM nitrite, at pH 6.0 and 37°C


substrate_name: NADH

assay_conditions_summary: pH 6; 310.15 K; cofactor NADH

substrate: NADH


substrate_name: nitrite

proof_lines: in the presence of 0.1 mM NADH, at pH 6.0 and 37°C

proof_lines: in the presence of 0.05 mM 4-(dimethylamino)cinnamaldehyde, at pH 6.0 and 37°C

substrate: nitrite


organism: Thermus thermophilus

assay_conditions_summary: pH 7.4; 323.15 K; cofactor NADP+


assay_conditions_summary: pH 7.4; 323.15 K; cofactor NAD+


organism: Lathyrus oleraceus


substrate_name: D-glyceraldehyde 3-phosphate

smiles: C(C(C=O)O)OP(=O)(O)O

substrate: D-glyceraldehyde 3-phosphate


substrate_name: clothianidin

proof_lines: nitrosoguanidine formation, pH 7.4, 37°C

substrate: clothianidin


substrate_name: nitenpyram

substrate: nitenpyram


substrate_name: imidacloprid

substrate: imidacloprid


enzyme_display_name: pyruvate oxidase

organism: Lactiplantibacillus plantarum

enzyme: pyruvate oxidase


substrate_name: oxygen

smiles: O=O

substrate: oxygen


substrate_name: phosphate

substrate: phosphate


organism: Arachis hypogaea


organism: Triticum aestivum

proof_lines: enzyme from leaf before treatment with alkaline phosphatase

proof_lines: enzyme from endosperm before treatment with alkaline phosphatase

proof_lines: enzyme from leaf after treatment with alkaline phosphatase


proof_lines: enzyme from leaf before or after treatment with alkaline phosphatase

proof_lines: enzyme from endosperm before or after treatment with alkaline phosphatase


organism: Hevea brasiliensis


substrate: NAD+


substrate: NADP+


organism: Streptococcus pyogenes

assay_conditions_summary: pH 8.5; 298.15 K; cofactor NADP+


organism: Trypanosoma cruzi

assay_conditions_summary: pH 7.2; 301.15 K; cofactor NADP+


substrate_name: L-glutamate 5-semialdehyde

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

substrate: L-glutamate 5-semialdehyde


assay_conditions_summary: pH 7.2; 301.15 K; cofactor NAD+


enzyme_display_name: aspartate-semialdehyde dehydrogenase

substrate_name: L-4-aspartyl phosphate

km_display: Not reported

enzyme: aspartate-semialdehyde dehydrogenase

substrate: L-4-aspartyl phosphate


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Streptococcus pneumoniae

substrate_name: L-aspartate-semialdehyde

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

substrate: L-aspartate-semialdehyde


organism: Bos taurus


organism: Oryctolagus cuniculus

assay_conditions_summary: cofactor NADH


organism: Camelus dromedarius

assay_conditions_summary: pH 8.5; 298.15 K; buffer 50 mM tricine-NaOH; cofactor NAD+

proof_lines: in 50 mM tricine-NaOH buffer (pH 8.5) with 10 mM sodium arsenate, at 25°C


assay_conditions_summary: pH 8.5; 298.15 K; buffer 50 mM tricine-NaOH


enzyme_display_name: (methyl)glyoxal oxidase

organism: Thermothelomyces thermophilus

source_db: oed

kcat_over_km_origin: calculated

enzyme: (methyl)glyoxal oxidase

source: oed


substrate_name: glycerol

smiles: OCC(O)CO

substrate: glycerol


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Pseudomonas putida


substrate_name: pyruvate

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

substrate: pyruvate


substrate_name: 3-phospho-D-glyceroyl phosphate

substrate: 3-phospho-D-glyceroyl phosphate


organism: Plasmodium falciparum

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


substrate_name: NAD+


organism: Saccharomyces cerevisiae

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


smiles: CSCCC(=O)C(=O)O


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


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


smiles: C(C(CO)O)O


enzyme_display_name: dihydrolipoyl dehydrogenase

organism: Acrididae

substrate_name: Coenzyme A; 2-Oxoglutarate; NAD+

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

enzyme: dihydrolipoyl dehydrogenase

substrate: Coenzyme A; 2-Oxoglutarate; NAD+


enzyme_display_name: aldehyde dehydrogenase (quinone)

organism: Cupriavidus necator

substrate_name: Butyraldehyde

smiles: CCCC=O

enzyme: aldehyde dehydrogenase (quinone)

substrate: Butyraldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


substrate_name: pentanal

smiles: CCCCC=O

substrate: pentanal


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: formaldehyde

smiles: C=O

substrate: formaldehyde


enzyme_display_name: abscisic-aldehyde oxidase

organism: Lathyrus oleraceus

substrate_name: abscisic aldehyde

enzyme: abscisic-aldehyde oxidase

substrate: abscisic aldehyde


organism: Sus scrofa

substrate: NAD+


substrate_name: NADH

substrate: NADH


organism: Pseudomonas aeruginosa

substrate_name: octanal

smiles: CCCCCCCC=O

substrate: octanal


assay_conditions_summary: pH 9


organism: Lucilia sericata

substrate_name: NAD+; 2-Oxoglutarate; Coenzyme A

assay_conditions_summary: cofactor NAD+

substrate: NAD+; 2-Oxoglutarate; Coenzyme A


organism: Geobacillus stearothermophilus

substrate_name: Pyruvate; Thiamine diphosphate

substrate: Pyruvate; Thiamine diphosphate


substrate_name: Thiamine diphosphate; Pyruvate

substrate: Thiamine diphosphate; Pyruvate


organism: Homo sapiens

substrate_name: Coenzyme A; NAD+; Pyruvate

substrate: Coenzyme A; NAD+; Pyruvate


organism: Pisum sativum

substrate_name: NAD+; Pyruvate; Coenzyme A

ki_unit: mM

substrate: NAD+; Pyruvate; Coenzyme A


organism: Solanum tuberosum


substrate_name: Coenzyme A; Pyruvate; NAD+

substrate: Coenzyme A; Pyruvate; NAD+


substrate_name: Pyruvate; NAD+; Coenzyme A

substrate: Pyruvate; NAD+; Coenzyme A


organism: Corynebacterium glutamicum


organism: Rattus norvegicus


organism: Escherichia coli


substrate_name: NAD+; 4-Hydroxy-2-oxoglutarate; Coenzyme A


substrate_name: 4-Hydroxy-2-oxoglutarate; NAD+; Coenzyme A


organism: Mycobacterium tuberculosis

substrate_name: Pyruvate; Coenzyme A; NAD+

substrate: Pyruvate; Coenzyme A; NAD+


substrate_name: Coenzyme A; 2-Oxopentanoate; NAD+

substrate: Coenzyme A; 2-Oxopentanoate; NAD+


substrate_name: pyruvate

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

mutation_type: substitution

substrate: pyruvate


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


organism: Azotobacter vinelandii


substrate_name: NAD+; 4-Methylthio-2-oxobutanoate; Coenzyme A


substrate_name: Coenzyme A; NAD+; 2-Oxoglutarate

substrate: Coenzyme A; NAD+; 2-Oxoglutarate


substrate_name: NAD+; Coenzyme A; 2-Oxoglutarate

substrate: NAD+; Coenzyme A; 2-Oxoglutarate


substrate_name: Coenzyme A; 2-Oxoglutarate; NAD+

substrate: Coenzyme A; 2-Oxoglutarate; NAD+


substrate_name: 2-Oxoglutarate; NAD+; Coenzyme A

substrate: 2-Oxoglutarate; NAD+; Coenzyme A


substrate_name: 2-Oxoglutarate; Coenzyme A; NAD+

substrate: 2-Oxoglutarate; Coenzyme A; NAD+


organism: Synechococcus sp. PCC 7002

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


substrate_name: alpha-Ketovaline; NAD+; Coenzyme A

substrate: alpha-Ketovaline; NAD+; Coenzyme A


substrate_name: NAD+; Coenzyme A; alpha-Ketovaline

substrate: NAD+; Coenzyme A; alpha-Ketovaline


organism: Bos taurus


substrate_name: Coenzyme A; 4-Methyl-2-oxopentanoate; NAD+


substrate_name: Coenzyme A; NAD+; alpha-Ketovaline

substrate: Coenzyme A; NAD+; alpha-Ketovaline


organism: Thauera butanivorans

smiles: CCCCO


organism: Acetobacter aceti

substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Gluconobacter sp.


organism: Gluconacetobacter diazotrophicus

substrate_name: acetic acid

smiles: CC(=O)O

substrate: acetic acid


organism: Gluconobacter oxydans


organism: Picosynechococcus sp. PCC 7002


organism: Rhizorhabdus wittichii

substrate_name: Butanal

assay_conditions_summary: pH 8

substrate: Butanal


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


organism: Geobacillus stearothermophilus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature S283C with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.


organism: Synechocystis sp. PCC 6803

proof_lines: presence of 0.002 mM inhibitor N-((1-((4-amino-2-methylpyrimidin-5-yl)methyl)-5-iodo-1H-1,2,3-triazol-4-yl)methyl)-4-nitrobenzenesulfonamide, pH 7.2, 37°C


organism: Urocitellus richardsonii

proof_lines: overall reaction, enzyme from euthermic animals, 22°C, pH 7.8

proof_lines: overall reaction, enzyme from hibernating animals, 37°C, pH 7.8

proof_lines: overall reaction, enzyme from euthermic animals, 37°C, pH 7.8


organism: Trametes cinnabarina

substrate_name: glyoxylic acid

assay_conditions_summary: pH 6

column_label: Table 2 row Glyoxylic acid; PciGLOX2 Km (mM) column = 0.1

row_label: Glyoxylic acid

table_label: Table 2

substrate: glyoxylic acid


substrate_name: methylglyoxal

column_label: Table 2 row Methylglyoxal; PciGLOX3 Km (mM) column = 0.1

row_label: Methylglyoxal

substrate: methylglyoxal


substrate_name: Glyoxal

smiles: C(=O)C=O

column_label: Table 2 row Glyoxal; PciGLOX3 Km (mM) column = 0.7

row_label: Glyoxal

substrate: Glyoxal


substrate_name: glycerol

column_label: Table 2 row Glycerol; PciGLOX3 Km (mM) column = 5.5

row_label: Glycerol

substrate: glycerol


enzyme_display_name: Abscisic-aldehyde oxidase

organism: Arabidopsis thaliana

substrate_name: abscisic aldehyde

proof_lines: All these kinetic values were obtained with AO-delta dimer.

enzyme: Abscisic-aldehyde oxidase

substrate: abscisic aldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


enzyme_display_name: Pyruvate dehydrogenase E1 component subunit beta, mitochondrial

organism: Chaetomium thermophilum (strain DSM 1495 / CBS 144.50 / IMI 039719)

substrate_name: pyruvate

assay_conditions_summary: cofactor CoA

substrate: pyruvate


enzyme_display_name: Pyruvate dehydrogenase E1 component subunit alpha, mitochondrial


enzyme_display_name: Multifunctional 2-oxoglutarate metabolism enzyme

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

column_label: PMCID PMC1180764 Results prose; enzyme Rv1248c/Kgd; substrate alpha-ketoglutarate/2-oxoglutarate; metric Km; raw value 480 microM; normalized value 0.48 mM; Figure 1B linked as alpha-ketoglutarate Km determination.

normalized_value_unit_evidence: 480 microM normalized to 0.48 mM.

raw_value_unit_evidence: PMC HTML reports Kgd Km values for alpha-ketoglutarate, TPP, and Mg2+ as 480, 19, and 196 microM, respectively.

row_label: Rv1248c/Kgd alpha-ketoglutarate Km

table_label: PMC HTML Results prose and Figure 1B-D (PMID 16027371; PMCID PMC1180764)


substrate_name: magnesium ions

column_label: PMCID PMC1180764 Results prose; enzyme Rv1248c/Kgd; substrate Mg2+/magnesium ions; metric Km; raw value 196 microM; normalized value 0.196 mM; Figure 1D linked as Mg2+ Km determination.

normalized_value_unit_evidence: 196 microM normalized to 0.196 mM.

row_label: Rv1248c/Kgd Mg2+ Km

enzyme: Multifunctional 2-oxoglutarate metabolism enzyme

substrate: magnesium ions


substrate_name: thiamine pyrophosphate

column_label: PMCID PMC1180764 Results prose; enzyme Rv1248c/Kgd; substrate TPP/thiamine pyrophosphate; metric Km; raw value 19 microM; normalized value 0.019 mM; Figure 1C linked as TPP Km determination.

normalized_value_unit_evidence: 19 microM normalized to 0.019 mM.

row_label: Rv1248c/Kgd TPP Km

substrate: thiamine pyrophosphate


organism: Homo sapiens

substrate_name: alpha-Ketovaline

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

substrate: alpha-Ketovaline


sequence_variant_note: Mutation signature S292E could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S292N could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Mutation signature S302A could not be applied safely because the resolved sequence does not match the expected reference residue(s).


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


enzyme_display_name: Pyruvate dehydrogenase E1 component subunit alpha, somatic form, mitochondrial


organism: Phanerodontia chrysosporium

smiles: CC(=O)C=O


enzyme_display_name: Pyruvate dehydrogenase E1 component

organism: Corynebacterium glutamicum (strain ATCC 13032 / DSM 20300 / JCM 1318 / BCRC 11384 / CCUG 27702 / LMG 3730 / NBRC 12168 / NCIMB 10025 / NRRL B-2784 / 534)

column_label: Primary paper Figure 4 prose states that for AceE and pyruvate a Km value of 0.066 +/- 0.06 mM was derived.

raw_value_unit_evidence: Km raw_value=0.066 +/- 0.06 raw_unit=mM

row_label: AceE with pyruvate kinetic characterization

table_label: Figure 4: Dehydrogenase activities of AceE and OdhA

enzyme: Pyruvate dehydrogenase E1 component


proof_lines:
wild-type enzyme, pH 7.0, 25°C
wild-type, pH 7.0, 30°C


organism: Mycolicibacterium smegmatis (strain ATCC 700084 / mc(2)155)

substrate_name: alpha-ketoglutarate

column_label: Results prose reports recombinant KGD (MSMEG_5049) with maximal ferricyanide reductase activity 1.6 s^-1 or 690 nmol min^-1 mg^-1 and Km for alpha-ketoglutarate of 540 uM (Fig. 6A).

raw_value_unit_evidence: Km raw_value=540 raw_unit=uM

row_label: Recombinant KGD (MSMEG_5049)

table_label: Results prose and Fig. 6A - Inhibition of KGD by GarA

substrate: alpha-ketoglutarate


enzyme_display_name: 2-oxoglutarate dehydrogenase E1/E2 component

column_label: Primary paper Figure 4 prose states that for OdhA and 2-oxoglutarate a Km of 0.014 +/- 0.003 mM was derived.

raw_value_unit_evidence: Km raw_value=0.014 +/- 0.003 raw_unit=mM

row_label: OdhA with 2-oxoglutarate kinetic characterization


proof_lines: recombinant wild-type component E1b, pH 7.5, 22°C

proof_lines: recombinant wild-type E1b component, pH 7.5, 22°C


proof_lines: recombinant component E1b mutant Y300Aalpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutant R287Aalpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutant R301Aalpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutants R301Aalpha and D295Aalpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutant D295Aalpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutant Y300Falpha, pH 7.5, 22°C


proof_lines: recombinant component E1b mutants R301Aalpha and Y300Falpha, pH 7.5, 22°C


organism: Escherichia coli

substrate_name: E2p lipoyl domain

substrate: E2p lipoyl domain


organism: Azotobacter vinelandii

substrate_name: lipoyl domain

proof_lines: acyl group transfer reaction, recombinant wild-type pyruvate dehydrogenase

substrate: lipoyl domain


mutation_signature: recombinant pyruvate dehydrogenase with N-terminal deletion acyl group transfer reaction / recombinant pyruvate dehydrogenase with N-terminal deletion

mutation_type: deletion

proof_lines: acyl group transfer reaction, recombinant pyruvate dehydrogenase with N-terminal deletion


proof_lines: recombinant wild-type pyruvate dehydrogenase


mutation_signature: recombinant pyruvate dehydrogenase with N-terminal deletion recombinant pyruvate dehydrogenase with N-terminal deletion


proof_lines: mutant enzyme H407A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K403E, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme E401K, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K410E, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme N404A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme E401A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K403A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K410A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme Q408A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K411E, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: mutant enzyme K411A, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: wild type enzyme, with 2,6-dichlorophenolindophenol, at 30°C


proof_lines: recombinant E1b component mutant H291Qalpha, pH 7.5, 22°C


proof_lines: recombinant E1b component mutant H291Aalpha, pH 7.5, 22°C


proof_lines: recombinant E1b component mutant H291Nalpha, pH 7.5, 22°C


substrate_name: 2-oxo-5-hexenoic acid

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

substrate: 2-oxo-5-hexenoic acid


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


proof_lines: mutant E1o-H298D/E2o-H348Q, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant E1o-H298D/E2o-S333M, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant E1o-H298D/E2o-H348Y, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant E1o-H298D, pH not specified in the publication, temperature not specified in the publication


proof_lines: mutant E1o-H298D/E2o-H348F, pH not specified in the publication, temperature not specified in the publication


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


organism: Pseudomonas putida


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


organism: Rattus norvegicus

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


substrate_name: NAD+

substrate: NAD+


substrate_name: Unknown

substrate: Unknown


substrate_name: coenzyme A

substrate: coenzyme A


substrate_name: L-2-aminoadipate 6-semialdehyde

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

substrate: L-2-aminoadipate 6-semialdehyde


organism: Sus scrofa


enzyme_display_name: retinal dehydrogenase

enzyme: retinal dehydrogenase


substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Gallus gallus

substrate_name: retinal

substrate: retinal


proof_lines:
isoform RALDH2, at pH 8.2 and 25°C
isoform RALDH3, at pH 8.2 and 25°C
isoform RALDH1, at pH 8.2 and 25°C


enzyme_display_name: formaldehyde dehydrogenase

substrate_name: formaldehyde

proof_lines: enzyme immobilized on MPS-4, pH 7.0, 22?

proof_lines: enzyme immobilized on phenyl-functionalized MPS-4, pH 7.0, 22?

proof_lines: enzyme immobilized on methyl-functionalized MPS-4, pH 7.0, 22?

enzyme: formaldehyde dehydrogenase

substrate: formaldehyde


enzyme_display_name: cinnamoyl-CoA reductase

substrate_name: p-Coumaroyl-CoA

substrate: p-Coumaroyl-CoA


proof_lines: with feruloyl-CoA as substrate, noncompetitive inhibition

proof_lines: with sinapoyl-CoA as substrate, noncompetitive inhibition

proof_lines: with feruloyl-CoA as substrate, uncompetitive inhibition


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


enzyme_display_name: phenylacetaldehyde dehydrogenase

enzyme: phenylacetaldehyde dehydrogenase


organism: Pseudomonas sp.

substrate_name: formate

proof_lines: with reduced methyl viologen as cosubstrate, pH and temperature not specified in the publication

substrate: formate


enzyme_display_name: long-chain acyl-protein thioester reductase

organism: Photobacterium phosphoreum

substrate_name: tetradecanoyl-CoA

substrate: tetradecanoyl-CoA


substrate_name: NADPH

enzyme: long-chain acyl-protein thioester reductase

substrate: NADPH


enzyme_display_name: coniferyl-aldehyde dehydrogenase

substrate_name: coniferyl aldehyde

enzyme: coniferyl-aldehyde dehydrogenase

substrate: coniferyl aldehyde


proof_lines: wild-type enzyme and mutant enzyme D297A


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


organism: Acinetobacter baumannii

substrate_name: succinate semialdehyde

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

substrate: succinate semialdehyde


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+


assay_conditions_summary: pH 8.5; 295.15 K; buffer 100 mM sodium phosphate

proof_lines: in 100 mM sodium phosphate buffer, pH 8.0, 30°C


assay_conditions_summary: pH 8.5; 295.15 K; cofactor NADP+


assay_conditions_summary: pH 7.5; 294.15 K; cofactor NAD+

proof_lines: overall reaction of bifunctional enzyme, pH 7.5, 21°C


enzyme_display_name: glutamyl-tRNA reductase

substrate_name: L-glutamyl-tRNAGlu

enzyme: glutamyl-tRNA reductase

substrate: L-glutamyl-tRNAGlu


assay_conditions_summary: pH 8.1; 310.15 K; cofactor NADPH


enzyme_display_name: aldehyde oxidase

organism: Mesocricetus auratus

enzyme: aldehyde oxidase


substrate_name: benzaldehyde

substrate: benzaldehyde


organism: Escherichia coli K-12


assay_conditions_summary: pH 9; 310.15 K; cofactor NADP+


organism: Oryctolagus cuniculus

substrate_name: cinchonidine

assay_conditions_summary: pH 7.4; 310.15 K; buffer 80 mM phosphate

proof_lines: wild type enzyme, in 80 mM phosphate buffer, pH 7.4, at 37°C

substrate: cinchonidine


enzyme_display_name: pyruvate oxidase

organism: Lactobacillus delbrueckii

substrate_name: pyruvate

proof_lines: presence of phosphatidylethanolamine, pH 5.6, 25°C

substrate: pyruvate


substrate_name: phosphate

substrate: phosphate


organism: Lactiplantibacillus plantarum


substrate_name: Unknown

substrate: Unknown


organism: Mus musculus

proof_lines: apparent Kcat-value of recombinant mAOX3, pH 7.4, 25°C

proof_lines: apparent Kcat-value of native mAOX3, pH 7.4, 25°C


substrate_name: thiamine diphosphate

substrate: thiamine diphosphate


organism: Homo sapiens

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

proof_lines:
enzyme-specific activity, pH 7.5, 37°C
overall-assay, pH 7.5, 37°C


proof_lines:
enzyme-specific activity, pH 7.5, 37°C
overall-assay, pH 7.5, 37°C
at pH 7.0 and 37°C


organism: Bos taurus


assay_conditions_summary: pH 7

proof_lines: preparation from liver, low affinity state, pH 7, temperature not specified in the publication

proof_lines: preparation from liver, pH 7, temperature not specified in the publication

proof_lines: preparation from heart, pH 7, temperature not specified in the publication


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

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


organism: Brassica oleracea


substrate_name: alpha-ketoisovaleric acid

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

substrate: alpha-ketoisovaleric acid


enzyme_display_name: pyruvate dehydrogenase (quinone)

organism: Escherichia coli

substrate_name: ferricyanide

proof_lines: without activation of the flavoprotein by proteolytic reactions, i.e. trypsin or chymotrypsin, pH and temperature not specified in the publication

proof_lines: with activation of the flavoprotein by proteolytic reactions, i.e. trypsin or chymotrypsin, pH and temperature not specified in the publication

enzyme: pyruvate dehydrogenase (quinone)

substrate: ferricyanide


proof_lines: pH and temperature not specified in the publication


substrate_name: NAD+

substrate: NAD+


substrate_name: coenzyme A

substrate: coenzyme A


substrate_name: acetaldehyde

smiles: CC=O

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris/HCl

proof_lines: at 25°C in 50 mM Tris/HCl buffer, pH 8.0

substrate: acetaldehyde


organism: Arabidopsis thaliana


enzyme_display_name: 2-oxoglutarate synthase

organism: Sulfolobus sp.

enzyme: 2-oxoglutarate synthase


proof_lines:
80°C, pH 7.5, natural enzyme
80°C, pH 7.5, recombinant enzyme


enzyme_display_name: pyruvate synthase (ferredoxin)

organism: Chlamydomonas reinhardtii

substrate_name: oxidized ferredoxin 2

assay_conditions_summary: pH 7; 298.15 K; buffer 25 mM potassium phosphate

proof_lines: in 25 mM potassium phosphate buffer (pH 7.0), 0.2 mM thiamine diphosphate, 1 mM MgCl2, at 25°C

proof_lines: in 100 mM potassium phosphate buffer, pH 6.8, temperature not specified in the publication

enzyme: pyruvate synthase (ferredoxin)

substrate: oxidized ferredoxin 2


substrate_name: CoA

assay_conditions_summary: pH 7; 298.15 K; buffer 25 mM potassium phosphate; cofactor CoA

substrate: CoA


assay_conditions_summary: pH 6.8; 298.15 K; buffer 100 mM potassium phosphate


organism: Caldicellulosiruptor bescii

substrate_name: oxidized ferredoxin

substrate: oxidized ferredoxin


substrate_name: glyceraldehyde 3-phosphate

smiles: C(C(C=O)O)OP(=O)(O)O

substrate: glyceraldehyde 3-phosphate


enzyme_display_name: aldehyde ferredoxin oxidoreductase

organism: Aromatoleum aromaticum

assay_conditions_summary: pH 8; 301.15 K; cofactor NAD+

proof_lines: native enzyme, pH 8.0, 28°C, with oxidized benzyl viologen

enzyme: aldehyde ferredoxin oxidoreductase


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


proof_lines: native enzyme, pH 8.0, 28°C, with benzaldehyde


substrate_name: Oxidized benzyl viologen

substrate: Oxidized benzyl viologen


organism: Magnetococcus marinus

substrate_name: succinyl-CoA

assay_conditions_summary: pH 7; cofactor CoA

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

substrate: succinyl-CoA


substrate_name: reduced ferredoxin

substrate: reduced ferredoxin


proof_lines: mutant E45Q, pH 7.5, temperature not specified in the publication


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

proof_lines: wild-type, pH 8.5, temperature not specified in the publication


proof_lines: mutant Y436F, pH 7.5, temperature not specified in the publication


organism: Aeropyrum pernix

substrate_name: pyruvate

substrate: pyruvate


organism: Citrobacter sp.

proof_lines: enzyme immobilized in alginate hydrogel, at pH 7.0 and 30°C


assay_conditions_summary: pH 7; 303.15 K; cofactor CoA


organism: Hydrogenobacter thermophilus

proof_lines: isozyme Kor, in 10 mM MOPS, pH 6.8, at 70°C

proof_lines: isozyme For, in 10 mM MOPS, pH 6.8, at 70°C


enzyme_display_name: aerobic carbon monoxide dehydrogenase

organism: Oligotropha carboxidovorans

substrate_name: Carbon monoxide; Ubiquinone-1; H2O

enzyme: aerobic carbon monoxide dehydrogenase

substrate: Carbon monoxide; Ubiquinone-1; H2O


substrate_name: Carbon monoxide dehydrogenase; 1,4-Benzoquinone


enzyme_display_name: pyruvate synthase

organism: Methanococcus maripaludis

substrate_name: oxaloacetate

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

enzyme: pyruvate synthase

substrate: oxaloacetate


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


enzyme_display_name: anaerobic carbon-monoxide dehydrogenase

organism: Afipia carboxidovorans

substrate_name: methylene blue

enzyme: anaerobic carbon-monoxide dehydrogenase

substrate: methylene blue


enzyme_display_name: anaerobic carbon monoxide dehydrogenase

proof_lines: Ag+-substituted enzyme, at pH 7.2 and 25°C

enzyme: anaerobic carbon monoxide dehydrogenase


organism: Archaeoglobus fulgidus

substrate_name: D-glyceraldehyde 3-phosphate

proof_lines: cosubstrate: benzyl viologen, 50°C, pH not specified in the publication

substrate: D-glyceraldehyde 3-phosphate


organism: Prosthecochloris vibrioformis f. thiosulfatophilum

assay_conditions_summary: cofactor CoA

proof_lines: pH and temperature not specified in the publication


organism: Pyrobaculum aerophilum

protein_accession_database: NCBI Protein

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


substrate_name: benzyl viologen

substrate: benzyl viologen


organism: Pyrococcus furiosus

substrate_name: glutaric dialdehyde

smiles: C(CC=O)CC=O

proof_lines: pH 8.4, 80°C, formaldehyde ferredoxin oxidoreductase, benzyl viologen as electron acceptor

substrate: glutaric dialdehyde


substrate_name: Succinic semialdehyde

substrate: Succinic semialdehyde


substrate_name: phenylpropionaldehyde

substrate: phenylpropionaldehyde


substrate_name: Indoleacetaldehyde

substrate: Indoleacetaldehyde


substrate_name: acetaldehyde

proof_lines: pH 8.4, 85°C, benzyl viologen as electron acceptor

substrate: acetaldehyde


substrate_name: propionaldehyde

smiles: CCC=O

substrate: propionaldehyde


enzyme_display_name: Pyruvate:ferredoxin oxidoreductase

organism: Moorella thermoacetica (strain ATCC 39073 / JCM 9320)

substrate_name: methyl viologen (in the oxidative decarboxylation of pyruvate)

proof_lines: kcat is 3.2 sec(-1) for the synthesis of pyruvate from acetyl-CoA and CO2 with methyl viologen as electron donor (PubMed:10878009). kcat is 2.0 sec(-1) for the synthesis of pyruvate from acetyl-CoA and CO2 with reduced ferredoxin as electro

enzyme: Pyruvate:ferredoxin oxidoreductase


organism: Rhodospirillum rubrum

substrate_name: CO

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature C451S to reconstruct the assayed variant sequence.

smiles: [Co]

substrate: CO


column_label: Primary paper prose reports the KM for CO of wild-type CODH as 32 uM; 32 uM = 0.032 mM.

raw_value_unit_evidence: Km raw_value=32 raw_unit=uM

row_label: Wild-type CODH / CO

table_label: PMID 16283394 Detailed characterization of C451S CODH prose


substrate_name: crotonaldehyde

sequence_source: multiple

smiles: CC=CC=O

proof_lines: pH 8.4, 80°C, with methyl viologen as electron acceptor

proof_lines: Significant activity only with aliphatic and aromatic aldehydes and only at low concentration (0.5 mM).

source_databases_merged: brenda uniprot

substrate: crotonaldehyde


substrate_name: glyceraldehyde

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

proof_lines: pH 8.4, 65°C, with methyl viologen as electron acceptor

substrate: glyceraldehyde


enzyme_display_name: Tungsten-containing formaldehyde ferredoxin oxidoreductase

organism: Thermococcus litoralis (strain ATCC 51850 / DSM 5473 / JCM 8560 / NS-C)

substrate_name: formaldehyde

smiles: C=O

proof_lines: Significant activity only with aliphatic aldehydes up to C3 and only at high concentration (15 mM).

substrate: formaldehyde


proof_lines: formaldehyde ferredoxin oxidoreductase, pH 8.4, 80°C, with benzyl viologen as electron acceptor


substrate_name: acetyl-CoA

substrate: acetyl-CoA


substrate_name: pyruvate

substrate: pyruvate


organism: Pseudomonas putida


proof_lines: with ferredoxin as electron acceptor, pH 8.4, 70°C

proof_lines: with benzyl viologen as electron acceptor, pH 8.4, 70°C


enzyme_display_name: formaldehyde dismutase

organism: Methanosarcina barkeri

substrate_name: H2O; Propanal

enzyme: formaldehyde dismutase

substrate: H2O; Propanal


enzyme_display_name: Acetyl-CoA decarbonylase/synthase complex subunit alpha 1

organism: Methanosarcina barkeri (strain Fusaro / DSM 804)

substrate_name: CO (at 37 degrees Celsius)

column_label: Abstract states analysis of enzyme kinetic properties revealed an apparent Km of 5 mM for CO and a Vmax of 1300 U/mg of protein.

raw_value_unit_evidence: Km raw_value=5 raw_unit=mM

row_label: Methanosarcina barkeri carbon monoxide dehydrogenase with CO

table_label: PubMed abstract PMID 6425262

substrate: CO (at 37 degrees Celsius)


enzyme_display_name: Carbon monoxide dehydrogenase large chain

organism: Afipia carboxidovorans (strain ATCC 49405 / DSM 1227 / KCTC 32145 / OM5)

column_label: PMC Table 1, row 1,4-benzoquinone, column Km (uM), reports 16.4; Materials/Methods paragraph P13 gives the steady-state assay conditions.

raw_value_unit_evidence: Km raw_value=16.4 raw_unit=uM

row_label: Table 1 row: 1,4-benzoquinone

table_label: PMC Table 1: Kinetic parameters of CODH oxidation by various quinones


enzyme_display_name: Carbon monoxide dehydrogenase small chain


enzyme_display_name: Carbon monoxide dehydrogenase medium chain


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


enzyme_display_name: 2-oxoacid oxidoreductase (ferredoxin)

organism: Sulfolobus sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I255V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.

enzyme: 2-oxoacid oxidoreductase (ferredoxin)


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature P253F with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I255S with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature P254G with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T256S with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T256A with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature T256V with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I255L with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature I255M with inferred residue-numbering offset +22 to reconstruct the assayed variant sequence.


organism: Thermococcus profundus

substrate_name: coenzyme A

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

column_label: Catalytic Properties prose reports apparent Km for coenzyme A as 21 uM; 21 uM = 0.021 mM.

raw_value_unit_evidence: Km raw_value=21 raw_unit=uM

row_label: Prose segment: apparent Km for coenzyme A

table_label: PMID 15713889 Catalytic Properties prose

substrate: coenzyme A


column_label: Catalytic Properties prose reports apparent Km for 2-ketoisovalerate as 170 uM; 170 uM = 0.17 mM.

raw_value_unit_evidence: Km raw_value=170 raw_unit=uM

row_label: Prose segment: apparent Km for 2-ketoisovalerate


enzyme_display_name: Formaldehyde dismutase

substrate_name: ethanol (at 30 degrees Celsius and pH 7.0)

smiles: CCO

proof_lines: Does not catalyze oxidation of methanol at pH 7.0.

enzyme: Formaldehyde dismutase


substrate_name: 1-propanol (at 30 degrees Celsius and pH 7.0)

smiles: CCCO


substrate_name: 1-butanol (at 30 degrees Celsius and pH 7.0)

smiles: CCCCO


substrate_name: 1-pentanol (at 30 degrees Celsius and pH 7.0)

smiles: CCCCCCO


substrate_name: cyclohexanol (at 30 degrees Celsius and pH 7.0)


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase subunit beta

organism: Saccharolobus solfataricus

proof_lines: kcat is 452 min(-1) for 2-oxoglutarate as substrate. kcat is 144 min(-1) for pyruvate as substrate. kcat is 93 min(-1) for 2-oxobutyrate as substrate.


enzyme: 2-oxoacid:ferredoxin oxidoreductase subunit beta


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


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase subunit alpha


enzyme: 2-oxoacid:ferredoxin oxidoreductase subunit alpha


organism: Homo sapiens

substrate_name: Butanal

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

smiles: CCCC=O

proof_lines:
class II enzyme
isoenzyme beta1,beta1
isoenzyme gamma2,gamma2

substrate: Butanal


organism: Aromatoleum aromaticum

substrate_name: acetaldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: NAD+

column_label: Table 4 row NAD+; columns Km, kcat, kcat/Km; footnote says BV/NAD+ kinetic parameters were assayed with 1 mM benzaldehyde substrate.

raw_value_unit_evidence: Table 4 row NAD+ reports Km 63 uM, kcat 54 s^-1, kcat/Km 0.86 uM^-1 s^-1.

row_label: NAD+

table_label: Table 4. Apparent kinetic parameters of AORAa

substrate: NAD+


substrate_name: Oxidized benzyl viologen

column_label: Table 4 row BV; columns Km, kcat, kcat/Km; footnote says BV/NAD+ kinetic parameters were assayed with 1 mM benzaldehyde substrate.

raw_value_unit_evidence: Table 4 row BV reports Km 23 uM, kcat 91 s^-1, kcat/Km 3.96 uM^-1 s^-1.

row_label: BV

substrate: Oxidized benzyl viologen


substrate_name: phenylacetaldehyde

column_label: Table 4 row Phenylacetaldehyde with electron acceptor BV; columns Km, kcat, kcat/Km.

raw_value_unit_evidence: Table 4 phenylacetaldehyde/BV row reports Km 82 uM, kcat 81 s^-1, kcat/Km 0.99 uM^-1 s^-1.

row_label: Phenylacetaldehyde; electron acceptor BV

substrate: phenylacetaldehyde


organism: Halobacterium salinarum


organism: Sulfurisphaera tokodaii

substrate_name: CoA

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K173A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8.5; cofactor CoA

substrate: CoA


organism: Sulfolobus sp

proof_lines: kcat is 51 sec(-1) for pyruvate as substrate (PubMed:11683888). kcat is 19 sec(-1) for 2-oxoglutarate as substrate (PubMed:11683888).


substrate_name: 2-oxoglutarate (at pH 6.8 and 50 degrees Celsius)


substrate: 2-oxoglutarate (at pH 6.8 and 50 degrees Celsius)


enzyme_display_name: Oxalate oxidoreductase subunit delta

substrate_name: oxalate

proof_lines: Kinetic parameters determined with the heterodimer oxalate oxidoreductase complex.

enzyme: Oxalate oxidoreductase subunit delta

substrate: oxalate


enzyme_display_name: Oxalate oxidoreductase subunit alpha

enzyme: Oxalate oxidoreductase subunit alpha


enzyme_display_name: Oxalate oxidoreductase subunit beta

enzyme: Oxalate oxidoreductase subunit beta


substrate_name: pyruvate (at pH 6.8 and 50 degrees Celsius)


substrate: pyruvate (at pH 6.8 and 50 degrees Celsius)


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha

organism: Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)

substrate_name: pyruvate

column_label: Table 1; row label: StOFOR1; column label: Pyruvate / Km (mM); raw value 0.32 +/- 0.08 mM; normalized value 0.32 mM.

normalized_value_unit_evidence: Km=0.32 mM as reported in Table 1.

raw_value_unit_evidence: Table 1; StOFOR1 row; Pyruvate / Km (mM) = 0.32 +/- 0.08 mM.

row_label: StOFOR1 row / Pyruvate / Km (mM) column

table_label: Table 1. Kinetic parameters of StOFOR1, its mutants, and StOFOR2 for each substrate


column_label: Table 1; row label: StOFOR1; column label: 2-Oxoglutarate / Km (mM); raw value 2.1 +/- 0.3 mM; normalized value 2.1 mM.

normalized_value_unit_evidence: Km=2.1 mM as reported in Table 1.

raw_value_unit_evidence: Table 1; StOFOR1 row; 2-Oxoglutarate / Km (mM) = 2.1 +/- 0.3 mM.

row_label: StOFOR1 row / 2-Oxoglutarate / Km (mM) column

enzyme: 2-oxoacid:ferredoxin oxidoreductase 1, subunit alpha


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta


enzyme: 2-oxoacid:ferredoxin oxidoreductase 1, subunit beta


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha

column_label: Table 1; row label: StOFOR2; column label: Pyruvate / Km (mM); raw value 1.6 +/- 0.3 mM; normalized value 1.6 mM.

normalized_value_unit_evidence: Km=1.6 mM as reported in Table 1.

raw_value_unit_evidence: Table 1; StOFOR2 row; Pyruvate / Km (mM) = 1.6 +/- 0.3 mM.

row_label: StOFOR2 row / Pyruvate / Km (mM) column


column_label: Table 1; row label: StOFOR2; column label: 2-Oxoglutarate / Km (mM); raw value 15 +/- 2 mM; normalized value 15.0 mM.

normalized_value_unit_evidence: Km=15.0 mM as reported in Table 1.

raw_value_unit_evidence: Table 1; StOFOR2 row; 2-Oxoglutarate / Km (mM) = 15 +/- 2 mM.

row_label: StOFOR2 row / 2-Oxoglutarate / Km (mM) column

enzyme: 2-oxoacid:ferredoxin oxidoreductase 2, subunit alpha


organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

substrate_name: pyruvate (at 80 degrees Celsius)

column_label: Prose after Table 2; metric K_m; enzyme complex Ape1473/1472; substrate pyruvate.

normalized_value_unit_evidence: Normalized Km for pyruvate = 0.38 mM for Ape1473/1472.

raw_value_unit_evidence: Prose after Table 2 reports Km for pyruvate of 0.38 mM for Ape1473/1472.

row_label: OFOR2 Q9YBX7/Q9YBX8 alpha/beta complex; pyruvate substrate

table_label: Prose following Table 2: substrate specificity and kinetic parameters

substrate: pyruvate (at 80 degrees Celsius)


substrate_name: 2-oxoglutarate (at 80 degrees Celsius)

column_label: Prose after Table 2; metric K_m; enzyme complex Ape1473/1472; substrate 2-oxoglutarate.

normalized_value_unit_evidence: Normalized Km for 2-oxoglutarate = 0.50 mM for Ape1473/1472.

raw_value_unit_evidence: Prose after Table 2 reports Km for 2-oxoglutarate of 0.50 mM for Ape1473/1472.

row_label: OFOR2 Q9YBX7/Q9YBX8 alpha/beta complex; 2-oxoglutarate substrate

substrate: 2-oxoglutarate (at 80 degrees Celsius)


column_label: Prose after Table 2; metric K_m; enzyme complex Ape2126/2128; substrate pyruvate.

normalized_value_unit_evidence: Normalized Km for pyruvate = 0.24 mM for Ape2126/2128.

raw_value_unit_evidence: Prose after Table 2 reports Km for pyruvate of 0.24 mM for Ape2126/2128.

row_label: OFOR1 Q9YA13/Q9YA11 alpha/beta complex; pyruvate substrate


enzyme_display_name: 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta


enzyme: 2-oxoacid:ferredoxin oxidoreductase 2, subunit beta


enzyme_display_name: aldehyde ferredoxin oxidoreductase

organism: Thermococcus sp.

substrate_name: acetate

enzyme: aldehyde ferredoxin oxidoreductase

substrate: acetate


substrate_name: glyceraldehyde

proof_lines: pH 8.4, 45°C, benzyl viologen as electron acceptor

substrate: glyceraldehyde


substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


substrate_name: crotonaldehyde

substrate: crotonaldehyde


substrate_name: Indoleacetaldehyde

substrate: Indoleacetaldehyde


substrate_name: methyl viologen

substrate: methyl viologen


substrate_name: benzyl viologen

substrate: benzyl viologen


substrate_name: oxidized ferredoxin

proof_lines: ES-1 ferredoxin, pH 8.4, 85°C, with crotonaldehyde

substrate: oxidized ferredoxin


substrate_name: isovalerylaldehyde

smiles: CC(C)CC=O

substrate: isovalerylaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: formaldehyde

substrate: formaldehyde


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


substrate_name: propionaldehyde

substrate: propionaldehyde


organism: Thermococcus litoralis

substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: pyruvate

substrate: pyruvate


substrate_name: indolpyruvate

substrate: indolpyruvate


substrate_name: phenylpyruvate

substrate: phenylpyruvate


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


substrate_name: phenylglyoxalate

substrate: phenylglyoxalate


substrate_name: hydroxyphenylpyruvate

substrate: hydroxyphenylpyruvate


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


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


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


substrate_name: CoA

assay_conditions_summary: pH 6.9; 358.15 K; cofactor CoA

substrate: CoA


substrate_name: isobutyryl-CoA

assay_conditions_summary: pH 7; 358.15 K; cofactor CoA

substrate: isobutyryl-CoA


enzyme_display_name: pyruvate synthase (ferredoxin)

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

enzyme: pyruvate synthase (ferredoxin)


proof_lines:
80°C, pH 7.5, recombinant enzyme
80°C, pH 7.5, natural enzyme


organism: Pyrococcus sp.


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


substrate_name: phenylglyoxylate

substrate: phenylglyoxylate


enzyme_display_name: formaldehyde dismutase

substrate_name: Butanal

assay_conditions_summary: pH 7.5; cofactor NAD+

column_label: Table 1 row Class I beta1beta1 for butanal gives kcat 75 min^-1, Km 2.1 mM, and kcat/Km 36 mM^-1 min^-1.

normalized_value_unit_evidence: 75 min^-1 = 1.25 s^-1; Km remains 2.1 mM; kcat/Km is 0.595238 from 1.25/2.1; printed table ratio rounds to 0.600 s^-1 mM^-1 from paired kcat/Km cells.

raw_value_unit_evidence: Table 1 row Class I beta1beta1 reports kcat 75 min^-1, Km 2.1 mM, and kcat/Km 36 mM^-1 min^-1 for butanal dismutation.

row_label: Class I beta1beta1

table_label: Table 1: Kinetic constants for elimination of butanal by dismutation

substrate: Butanal


column_label: Table 1 row Class I gamma2gamma2 for butanal gives kcat 1300 min^-1, Km 1.2 mM, and kcat/Km 1100 mM^-1 min^-1.

normalized_value_unit_evidence: 1300 min^-1 = 21.6667 s^-1; Km remains 1.2 mM; kcat/Km is 18.0556 from 21.6667/1.2; printed table ratio rounds to 18.333 s^-1 mM^-1 from paired kcat/Km cells.

raw_value_unit_evidence: Table 1 row Class I gamma2gamma2 reports kcat 1300 min^-1, Km 1.2 mM, and kcat/Km 1100 mM^-1 min^-1 for butanal dismutation.

row_label: Class I gamma2gamma2


column_label: Table 1 row Class II for butanal gives kcat 60 min^-1, Km 13 mM, and kcat/Km 5 mM^-1 min^-1.

normalized_value_unit_evidence: 60 min^-1 = 1.0 s^-1; Km remains 13 mM; kcat/Km is 0.083333 printed-ratio normalized; Km is the required metric s^-1 mM^-1 from paired kcat/Km cells.

raw_value_unit_evidence: Table 1 row Class II reports kcat 60 min^-1, Km 13 mM, and kcat/Km 5 mM^-1 min^-1 for butanal dismutation.

row_label: Class II


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


normalized_value_unit_evidence: 1300 min^-1 = 21.667 s^-1; Km remains 1.2 mM; kcat/Km is 18.0558 from 21.667/1.2; printed table ratio rounds to 18.333 s^-1 mM^-1 from paired kcat/Km cells.


normalized_value_unit_evidence: 60 min^-1 = 1.0 s^-1; Km remains 13 mM; kcat/Km is 0.076923 from 1.0/13; printed table ratio rounds to 0.083333 s^-1 mM^-1 from paired kcat/Km cells.


organism: Methylobacterium sp. FD1


enzyme_display_name: UniProt Q96XT4

source_db: skid

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

assay_conditions_summary: pH 8.5; 353.15 K; cofactor CoA

source_databases_merged: skid uniprot

enzyme: UniProt Q96XT4

source: skid


organism: Pseudomonas putida


substrate_name: ethanol

substrate: ethanol


substrate_name: methanol

smiles: CO

substrate: methanol


organism: Archaeoglobus fulgidus

substrate_name: oxidized ferredoxin

substrate: oxidized ferredoxin


assay_conditions_summary: pH 7.5; 338.15 K; cofactor CoA


organism: Methanothermobacter thermautotrophicus

assay_conditions_summary: pH 8; 338.15 K; cofactor CoA

proof_lines: pH 8.0, 65°C, substrate phenylpyruvate, benzyl viologen as electron acceptor


proof_lines: pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, enzyme StOFOR1

proof_lines: pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, enzyme StOFOR2


proof_lines: pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, mutant enzyme StOFOR1 with mutation S41A in alpha-subunit


proof_lines: pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, mutant enzyme StOFOR1 with mutation T349L in alpha-subunit


proof_lines: pH 8.5, 80°C, cosubstrate: oxidized methyl viologen, mutant enzyme StOFOR1 with mutation K49I in alpha-subunit


organism: Pyrococcus furiosus


assay_conditions_summary: pH 8.4; 353.15 K; cofactor CoA


enzyme_display_name: carboxylate reductase

organism: Neomoorella thermoacetica

proof_lines: 4-methylbenzoate, with reduced carbamoyl methyl viologen as cosubstrate

proof_lines: with carbamoyl methyl viologen as cosubstrate

enzyme: carboxylate reductase


proof_lines: with reduced carbamoyl methyl viologen as cosubstrate


substrate_name: terephthalate

substrate: terephthalate


substrate_name: acetate

substrate: acetate


substrate_name: propanoate

substrate: propanoate


substrate_name: benzoate

proof_lines: with reduced carbamoyl methyl viologen as cosubstrate, pH 4.5

proof_lines: with reduced carbamoyl methyl viologen as cosubstrate, pH 5.5

substrate: benzoate


proof_lines: pyridine-4-carboxylate, with reduced carbamoyl methyl viologen as cosubstrate


substrate_name: acetaldehyde

proof_lines: with benzyl viologen as cosubstrate, at 85°C

substrate: acetaldehyde


substrate_name: glyceraldehyde

proof_lines: with benzyl viologen as cosubstrate, at 45°C

substrate: glyceraldehyde


substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


substrate_name: crotonaldehyde

smiles: CC=CC=O

substrate: crotonaldehyde


substrate_name: indolecetaldehyde

proof_lines: with crotonaldehyde as cosubstrate, at 85°C

substrate: indolecetaldehyde


substrate_name: methyl viologen

substrate: methyl viologen


substrate_name: benzyl viologen

substrate: benzyl viologen


substrate_name: Isovaleraldehyde

substrate: Isovaleraldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: methanal

substrate: methanal


substrate_name: phenylacetaldehyde

substrate: phenylacetaldehyde


substrate_name: propanal

smiles: CCC=O

substrate: propanal


substrate_name: Indoleacetaldehyde

substrate: Indoleacetaldehyde


organism: Methanosarcina barkeri

substrate_name: CoA

assay_conditions_summary: pH 7; 310.15 K; cofactor CoA

substrate: CoA


substrate_name: oxidized ferredoxin

proof_lines: 37°C, pH 7.0, ferredoxin from Clostridium pasteurianum

substrate: oxidized ferredoxin


substrate_name: pyruvate

substrate: pyruvate


organism: Methanococcus maripaludis


substrate_name: oxaloacetate

substrate: oxaloacetate


assay_conditions_summary: pH 8.6; 310.15 K; cofactor CoA


organism: Peptoclostridium acidaminophilum


substrate_name: Butyraldehyde

substrate: Butyraldehyde


substrate_name: DL-glyceraldehyde

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

substrate: DL-glyceraldehyde


substrate_name: propionaldehyde

substrate: propionaldehyde


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: Glutaraldehyde

smiles: C(CC=O)CC=O

substrate: Glutaraldehyde


proof_lines: terephthalaldehyde, with carbamoyl methyl viologen as cosubstrate


substrate_name: Butanal

substrate: Butanal


proof_lines: 3,4-dimethoxy-5-hydroxybenzaldehyde, with carbamoyl methyl viologen as cosubstrate


substrate_name: ES-1 ferredoxin

proof_lines: acetaldehyde, with carbamoyl methyl viologen as cosubstrate

substrate: ES-1 ferredoxin


substrate_name: cinnamaldehyde

substrate: cinnamaldehyde


proof_lines: reduced carbamoyl methyl viologen, with benzoate as cosubstrate


smiles: C=O

proof_lines: 4-fluorobenzoate, with reduced carbamoyl methyl viologen as cosubstrate

proof_lines: 4-methoxybenzoate, with reduced carbamoyl methyl viologen as cosubstrate


substrate_name: cinnamate

substrate: cinnamate


substrate_name: methyl viologen

proof_lines: 3-methoxybenzoate, with reduced carbamoyl methyl viologen as cosubstrate

substrate: methyl viologen


organism: Clostridium formicaceticum

substrate_name: Butanoate

smiles: CCCC(=O)[O-]

substrate: Butanoate


substrate_name: propanoate

substrate: propanoate


substrate_name: benzoate

substrate: benzoate


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: propanal

substrate: propanal


proof_lines: with NH2CO-methyl viologen as cosubstrate, molybdenum-containing enzyme


proof_lines: with NH2CO-methyl viologen as cosubstrate, tungsten-containing enzyme


organism: Megalodesulfovibrio gigas


substrate_name: furfural

substrate: furfural


substrate_name: benzyl viologen

substrate: benzyl viologen


substrate_name: octaldehyde

smiles: CCCCCCCC=O

proof_lines: 25°C, pH 8.0, enzyme in aqueous solution

proof_lines: 25°C, pH 8.0, enzyme in sodium bis(2-ethylhexyl) sulfosuccinate reverse micelles, hydratation degree 26

substrate: octaldehyde


substrate_name: decylaldehyde

substrate: decylaldehyde


enzyme_display_name: Aldehyde oxidoreductase molybdenum-binding subunit PaoC

organism: Escherichia coli (strain K12)

proof_lines: kcat is 84 sec(-1) with cinnamaldehyde as substrate (PubMed:19368556). kcat is 97 sec(-1) with benzaldehyde as substrate (PubMed:19368556). kcat is 125 sec(-1) with vanillin as substrate (PubMed:19368556). kcat is 36.64 sec(-1) with vanilli


enzyme: Aldehyde oxidoreductase molybdenum-binding subunit PaoC


substrate_name: vanillin

substrate: vanillin


substrate_name: crotonaldehyde

substrate: crotonaldehyde


proof_lines:
pH 7.6, 35°C
Kis value, pH 7.6, 35°C
Raw SKiD Env: Temp=35°C, pH=7.6

source_databases_merged: brenda skid


organism: Pseudomonas nitroreducens


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

assay_conditions_summary: pH 7.6; 308.15 K; buffer 50 mM Tris-HCl

proof_lines: in 50 mM Tris-HCl buffer (pH 7.6), at 37°C


substrate_name: Salicylaldehyde

column_label: Table 3 'Kinetic parameters of DgAOR substrates and related compounds, which are substrates of other Mo-enzymes of the XO family' (J Biol Inorg Chem 2015, 20(2): 219-229, journal page 224); Table 3, substrate row '2-OH benzaldehyde (Salicylaldehyde)': column 'Kcat (s^-1)' = 0.44; column 'KM (uM)' = 1.6; column 'Kcat/KM' = 0.275; column 'Observation' = -.

normalized_value_unit_evidence: kcat: printed Table 3 cell 0.44 s^-1; already in s^-1, no conversion; the value is 0.44 s^(-1) and the exported value is 0.44 s^(-1). Km: printed Table 3 cell 1.6 uM; 1.6 / 1000 = 0.0016 mM; the exported value is 0.0016 mM. Kcat/KM: printed Table 3 cell 0.275 with a bare column header; the exported value is 275.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 224), Table 3, substrate row '2-OH benzaldehyde (Salicylaldehyde)': Kcat = 0.44 s^-1; KM = 1.6 uM

substrate: Salicylaldehyde


proof_lines:
pH 7.6, 35°C
Raw SKiD Env: Temp=35°C, pH=7.6


proof_lines:
DgAOR
Table 3


column_label: Table 3 'Kinetic parameters of DgAOR substrates and related compounds, which are substrates of other Mo-enzymes of the XO family' (J Biol Inorg Chem 2015, 20(2): 219-229, journal page 224); Table 3, substrate row 'benzaldehyde': column 'Kcat (s^-1)' = 5.7; column 'KM (uM)' = 25; column 'Kcat/KM' = 0.228; column 'Observation' = Substrate inhibition (KiS = 0.8 mM).

normalized_value_unit_evidence: kcat: printed Table 3 cell 5.7 s^-1; already in s^-1, no conversion; the value is 5.7 s^(-1) and the exported value is 5.7 s^(-1). Km: printed Table 3 cell 25 uM; 25 / 1000 = 0.025 mM; the exported value is 0.025 mM. Kcat/KM: printed Table 3 cell 0.228 with a bare column header; the exported value is 228.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 3 (journal page 224), Table 3, substrate row 'benzaldehyde': Kcat = 5.7 s^-1; KM = 25 uM

row_label: Table 3, substrate row 'benzaldehyde'


organism: Sulfurisphaera tokodaii

smiles: C(C(C=O)O)OP(=O)(O)O

proof_lines: cosubstrate methyl viologen, pH 7.0, 70°C


substrate_name: D-glyceraldehyde

proof_lines: cosubstrate 2,6-dichlorophenolindophenol, pH 7.0, 70°C

substrate: D-glyceraldehyde


substrate_name: Indoleacetaldehyde

substrate: Indoleacetaldehyde


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: Indolepyruvate

substrate: Indolepyruvate


substrate_name: benzylviologen

column_label: PMC XML abstract metric sentence gives Km for benzylviologen as 0.55 mM

normalized_value_unit_evidence: PMC XML abstract Km normalized_value=0.55 normalized_unit=mM

raw_value_unit_evidence: PMC XML abstract: benzylviologen was used as an artificial electron acceptor (apparent Km, 0.55 mM)

row_label: benzylviologen artificial electron acceptor sentence

table_label: PMC XML abstract

substrate: benzylviologen


proof_lines: Acetaldehyde, propionaldehyde, and benzaldehyde were excellent substrates


enzyme_display_name: Glyceraldehyde dehydrogenase large chain

organism: Sulfolobus acidocaldarius (strain ATCC 33909 / DSM 639 / JCM 8929 / NBRC 15157 / NCIMB 11770)

substrate_name: propionaldehyde (at 80 degrees Celsius and pH 6.7)


substrate_name: D,L-glyceraldehyde (at 80 degrees Celsius and pH 6.7)

enzyme: Glyceraldehyde dehydrogenase large chain


enzyme_display_name: Glyceraldehyde dehydrogenase small chain

substrate: propionaldehyde (at 80 degrees Celsius and pH 6.7)


enzyme: Glyceraldehyde dehydrogenase small chain

substrate: D,L-glyceraldehyde (at 80 degrees Celsius and pH 6.7)


enzyme_display_name: Glyceraldehyde dehydrogenase medium chain


enzyme: Glyceraldehyde dehydrogenase medium chain


organism: Oleidesulfovibrio alaskensis


enzyme_display_name: 2-oxoglutarate synthase

organism: Thermococcus litoralis

substrate_name: oxidized ferredoxin

proof_lines: pH 8.4, 80°C, ferredoxin from Pyrococcus furiosus

enzyme: 2-oxoglutarate synthase

substrate: oxidized ferredoxin


substrate_name: CoA

substrate: CoA


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: p-hydroxyphenylpyruvate

substrate: p-hydroxyphenylpyruvate


enzyme_display_name: anaerobic carbon monoxide dehydrogenase

substrate_name: CO

smiles: [Co]

enzyme: anaerobic carbon monoxide dehydrogenase

substrate: CO


substrate_name: methyl viologen

substrate: methyl viologen


enzyme_display_name: formylmethanofuran dehydrogenase

substrate_name: formylmethanofuran

proof_lines:
in presence of 0.5 M KH2PO4
in presence of 2 M KH2PO4

enzyme: formylmethanofuran dehydrogenase

substrate: formylmethanofuran


substrate_name: formate

substrate: formate


substrate_name: Formamide

smiles: C(=O)N

substrate: Formamide


substrate_name: methylformamide

smiles: CNC=O

substrate: methylformamide


enzyme_display_name: 2-oxoacid oxidoreductase (ferredoxin)

organism: Saccharolobus solfataricus

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

enzyme: 2-oxoacid oxidoreductase (ferredoxin)


substrate_name: pyruvate

substrate: pyruvate


organism: Thermococcus guaymasensis


organism: Desulfomicrobium sp.

assay_conditions_summary: pH 8.5; 308.15 K; cofactor CoA


organism: Hydrogenobacter thermophilus

assay_conditions_summary: pH 7.6; 343.15 K; cofactor CoA


assay_conditions_summary: pH 5.3; 278.15 K; cofactor CoA

proof_lines: turnover mumber for CO/CO2 exchange reaction


substrate_name: acetyl-CoA

proof_lines:
CO/acetyl-CoA exchange reaction
acetyl-CoA/CoA exchange reaction

substrate: acetyl-CoA


enzyme_display_name: UniProt Q28943

organism: Sus scrofa

substrate_name: NADPH

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q28943

substrate: NADPH


substrate_name: Uracil

proof_lines:
Raw SKiD Env: Temp=20°C, pH=7
Raw SKiD Env: Temp=30°C, pH=7.5

substrate: Uracil


substrate_name: thymine

substrate: thymine


enzyme_display_name: Fumarate reductase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: fumarate

enzyme: Fumarate reductase 1

substrate: fumarate


organism: Neomoorella thermoacetica

proof_lines: inhibition of CO/acetyl-CoA exchange reaction


substrate_name: propionyl-CoA

substrate: propionyl-CoA


organism: Methanothrix soehngenii


substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


organism: Methanosarcina mazei


substrate_name: propionaldehyde

proof_lines:
25 C, pH 8.2
steady-state kinetic analysis
propionaldehyde

substrate: propionaldehyde


substrate_name: acetaldehyde

smiles: CC=O

substrate: acetaldehyde


enzyme_display_name: DELTA4-3-oxosteroid 5beta-reductase

organism: Digitalis canariensis

assay_conditions_summary: cofactor NADPH

enzyme: DELTA4-3-oxosteroid 5beta-reductase


substrate_name: progesterone

substrate: progesterone


substrate_name: cortisol

substrate: cortisol


substrate_name: cortexone

substrate: cortexone


enzyme_display_name: dihydropyrimidine dehydrogenase (NADP+)

organism: Cupriavidus necator

enzyme: dihydropyrimidine dehydrogenase (NADP+)


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


enzyme_display_name: dihydropyrimidine dehydrogenase (NAD+)

organism: Escherichia coli

substrate_name: H+; Uracil; NADH

assay_conditions_summary: cofactor NADH

enzyme: dihydropyrimidine dehydrogenase (NAD+)

substrate: H+; Uracil; NADH


enzyme_display_name: dihydrouracil dehydrogenase (NAD(+))

enzyme: dihydrouracil dehydrogenase (NAD(+))


substrate_name: Dihydrothymine

substrate: Dihydrothymine


substrate_name: Thymine

substrate: Thymine


enzyme_display_name: acyl-CoA dehydrogenase (NADP+)

organism: Rattus norvegicus

enzyme: acyl-CoA dehydrogenase (NADP+)


substrate_name: crotonyl-CoA

assay_conditions_summary: cofactor CoA

substrate: crotonyl-CoA


organism: Bos taurus

substrate_name: trans-crotonyl-CoA

substrate: trans-crotonyl-CoA


substrate_name: butyryl-CoA

substrate: butyryl-CoA


substrate_name: acetyl-CoA

substrate: acetyl-CoA


enzyme_display_name: fumarate reductase (NADH)

organism: Ruminobacter amylophilus

substrate_name: NADH

enzyme: fumarate reductase (NADH)

substrate: NADH


substrate_name: fumarate

substrate: fumarate


organism: Shewanella frigidimarina

proof_lines:
mutant H61M, pH 9.0, 25°C
mutant H61M, pH 7.5, 25°C
mutant H61M, pH 6.0, 25°C


proof_lines:
mutant H61A, pH 9.0, 25°C
mutant H61A, pH 7.5, 25°C
mutant H61A, pH 7.2, 25°C


proof_lines: mutant H61M, pH 7.2 and pH 7.5, 25°C, and mutant H61A, pH 6.0, pH 7.2, pH 7.5, and pH 9.0, 25°C


organism: Pelophylax lessonae

substrate_name: testosterone

substrate: testosterone


substrate_name: NADPH

substrate: NADPH


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: meso-tartrate dehydrogenase

substrate_name: (+)-tartrate

assay_conditions_summary: cofactor NAD+

proof_lines:
thio-NAD+ as coenzyme
NAD+ as coenzyme
3-acetylpyridine-NAD+ as coenzyme

enzyme: meso-tartrate dehydrogenase

substrate: (+)-tartrate


substrate_name: D-malate

substrate: D-malate


organism: Mycolicibacterium smegmatis


organism: Pseudomonas putida

substrate_name: NAD+

substrate: NAD+


substrate_name: meso-tartrate

substrate: meso-tartrate


organism: Capsella rubella

assay_conditions_summary: pH 6; 313.15 K; cofactor NADPH


assay_conditions_summary: pH 6; 313.15 K; cofactor NADH

proof_lines: mutant R63K/R64H, cofactor NADPH, pH 6, 40°C

proof_lines: mutant R63K/R64H, cofactor NADH, pH 6, 40°C


enzyme_display_name: cucurbitacin DELTA23-reductase

organism: Cucurbita maxima

enzyme: cucurbitacin DELTA23-reductase


organism: Sus scrofa

substrate_name: meso-Tartrate; NAD+

substrate: meso-Tartrate; NAD+


organism: Candida albicans

proof_lines:
reductase type I
reductase type II


proof_lines:
mutant H505A, pH 6.0, 25°C
mutant H505A, pH 7.2, 25°C
mutant H505A, pH 7.5, 25°C


proof_lines:
wild-type enzyme, pH 9.0, 25°C
wild-type enzyme, pH 7.5, 25°C
wild-type enzyme, pH 7.2, 25°C


proof_lines:
mutant H505Y, pH 9.0, 25°C
mutant H505Y, pH 7.2, 25°C
mutant H505Y, pH 7.5, 25°C


organism: Bufo gargarizans

substrate_name: progesterone

substrate: progesterone


organism: Arabidopsis thaliana

proof_lines: kcat is 10.11 min(-1) with progesterone as substrate. kcat is 66.85 min(-1) with 2-cyclohexen-1-one as substrate.


substrate_name: cortisol

substrate: cortisol


substrate_name: cortexone

substrate: cortexone


organism: Homo sapiens

substrate_name: androstenedione

substrate: androstenedione


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y132F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature V309F with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


substrate_name: cholestenone

verification_status: corrected

assay_conditions_summary: pH 6; 310.15 K; buffer pH 6; cofactor NADPH

column_label: Table 1: Substrate specificity of AKR1D1 (Steroids 2011, 76(5):484-490), PDF page 14 of 15, substrate line 'Cholestenone'; column 'Type' = C27; column 'kcat (min^-1)' = 0.60; column 'Km (uM)' = 0.3; column 'Ki (uM)' = N.D.; column 'kcat/Km (min^-1 uM^-1)' = 1.98.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.3 uM; 1 uM is one thousandth of 1 mM, so 0.3 / 1000 = 0.0003 mM. kcat: printed Table 1 cell 0.60 min^-1; the printed head is per minute, so 0.60 / 60 = 0.01 s^(-1). kcat/Km: printed Table 1 cell 1.98 min^-1 uM^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 1.98 times 1000 divided by 60 = 33 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate line 'Cholestenone': kcat cell = 0.60 min^-1; Km cell = 0.3 uM; printed kcat/Km cell = 1.98 min^-1 uM^-1.

row_label: Table 1, substrate line 'Cholestenone' (steroid class C27)

table_label: Table 1: Substrate specificity of AKR1D1 (Steroids 2011, 76(5):484-490), PDF page 14 of 15; printed column heads Substrate, Type, kcat (min^-1), Km (uM), Ki (uM) and kcat/Km (min^-1 uM^-1)

substrate: cholestenone

status: corrected


substrate_name: corticosterone

column_label: Table 1: Substrate specificity of AKR1D1 (Steroids 2011, 76(5):484-490), PDF page 14 of 15, substrate line 'Corticosterone'; column 'Type' = C21; column 'kcat (min^-1)' = 1.9; column 'Km (uM)' = 2.2; column 'Ki (uM)' = N.D.; column 'kcat/Km (min^-1 uM^-1)' = 0.87.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.2 uM; 1 uM is one thousandth of 1 mM, so 2.2 / 1000 = 0.0022 mM. kcat: printed Table 1 cell 1.9 min^-1; the printed head is per minute, so 1.9 / 60 = 0.0316666666667 s^(-1). kcat/Km: printed Table 1 cell 0.87 min^-1 uM^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.87 times 1000 divided by 60 = 14.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate line 'Corticosterone': kcat cell = 1.9 min^-1; Km cell = 2.2 uM; printed kcat/Km cell = 0.87 min^-1 uM^-1.

row_label: Table 1, substrate line 'Corticosterone' (steroid class C21)

substrate: corticosterone


column_label: Table 1: Substrate specificity of AKR1D1 (Steroids 2011, 76(5):484-490), PDF page 14 of 15, substrate line '4-Cholesten-7alpha-ol-3-one'; column 'Type' = C27; column 'kcat (min^-1)' = 2.0; column 'Km (uM)' = 0.8; column 'Ki (uM)' = N.D.; column 'kcat/Km (min^-1 uM^-1)' = 2.53.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.8 uM; 1 uM is one thousandth of 1 mM, so 0.8 / 1000 = 0.0008 mM. kcat: printed Table 1 cell 2.0 min^-1; the printed head is per minute, so 2.0 / 60 = 0.0333333333333 s^(-1). kcat/Km: printed Table 1 cell 2.53 min^-1 uM^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 2.53 times 1000 divided by 60 = 42.1666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate line '4-Cholesten-7alpha-ol-3-one': kcat cell = 2.0 min^-1; Km cell = 0.8 uM; printed kcat/Km cell = 2.53 min^-1 uM^-1.

row_label: Table 1, substrate line '4-Cholesten-7alpha-ol-3-one' (steroid class C27)


column_label: Table 1: Substrate specificity of AKR1D1 (Steroids 2011, 76(5):484-490), PDF page 14 of 15, substrate line '1,4-Androstadien-17beta-ol-3-one'; column 'Type' = C19; column 'kcat (min^-1)' = 2.1; column 'Km (uM)' = 3.2; column 'Ki (uM)' = N.A.; column 'kcat/Km (min^-1 uM^-1)' = 0.66.

normalized_value_unit_evidence: Km: printed Table 1 cell 3.2 uM; 1 uM is one thousandth of 1 mM, so 3.2 / 1000 = 0.0032 mM. kcat: printed Table 1 cell 2.1 min^-1; the printed head is per minute, so 2.1 / 60 = 0.035 s^(-1). kcat/Km: printed Table 1 cell 0.66 min^-1 uM^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.66 times 1000 divided by 60 = 11 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate line '1,4-Androstadien-17beta-ol-3-one': kcat cell = 2.1 min^-1; Km cell = 3.2 uM; printed kcat/Km cell = 0.66 min^-1 uM^-1.

row_label: Table 1, substrate line '1,4-Androstadien-17beta-ol-3-one' (steroid class C19)


column_label: Table 1: Substrate specificity of AKR1D1 (Steroids 2011, 76(5):484-490), PDF page 14 of 15, substrate line '4-Estren-17beta-ol-3-one'; column 'Type' = C18; column 'kcat (min^-1)' = 2.7; column 'Km (uM)' = 3.0; column 'Ki (uM)' = 18.6; column 'kcat/Km (min^-1 uM^-1)' = 0.91.

normalized_value_unit_evidence: Km: printed Table 1 cell 3.0 uM; 1 uM is one thousandth of 1 mM, so 3.0 / 1000 = 0.003 mM. kcat: printed Table 1 cell 2.7 min^-1; the printed head is per minute, so 2.7 / 60 = 0.045 s^(-1). kcat/Km: printed Table 1 cell 0.91 min^-1 uM^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.91 times 1000 divided by 60 = 15.1666666667 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate line '4-Estren-17beta-ol-3-one': kcat cell = 2.7 min^-1; Km cell = 3.0 uM; printed kcat/Km cell = 0.91 min^-1 uM^-1.

row_label: Table 1, substrate line '4-Estren-17beta-ol-3-one' (steroid class C18)


column_label: Table 1: Substrate specificity of AKR1D1 (Steroids 2011, 76(5):484-490), PDF page 14 of 15, substrate line 'Cortisol'; column 'Type' = C21; column 'kcat (min^-1)' = 2.7; column 'Km (uM)' = 13.1; column 'Ki (uM)' = N.D.; column 'kcat/Km (min^-1 uM^-1)' = 0.21.

normalized_value_unit_evidence: Km: printed Table 1 cell 13.1 uM; 1 uM is one thousandth of 1 mM, so 13.1 / 1000 = 0.0131 mM. kcat: printed Table 1 cell 2.7 min^-1; the printed head is per minute, so 2.7 / 60 = 0.045 s^(-1). kcat/Km: printed Table 1 cell 0.21 min^-1 uM^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.21 times 1000 divided by 60 = 3.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate line 'Cortisol': kcat cell = 2.7 min^-1; Km cell = 13.1 uM; printed kcat/Km cell = 0.21 min^-1 uM^-1.

row_label: Table 1, substrate line 'Cortisol' (steroid class C21)


column_label: Table 1: Substrate specificity of AKR1D1 (Steroids 2011, 76(5):484-490), PDF page 14 of 15, substrate line 'Delta4-Androstene-3,17-dione'; column 'Type' = C19; column 'kcat (min^-1)' = 6.0; column 'Km (uM)' = 0.9; column 'Ki (uM)' = 4.3; column 'kcat/Km (min^-1 uM^-1)' = 6.72.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.9 uM; 1 uM is one thousandth of 1 mM, so 0.9 / 1000 = 0.0009 mM. kcat: printed Table 1 cell 6.0 min^-1; the printed head is per minute, so 6.0 / 60 = 0.1 s^(-1). kcat/Km: printed Table 1 cell 6.72 min^-1 uM^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 6.72 times 1000 divided by 60 = 112 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate line 'Delta4-Androstene-3,17-dione': kcat cell = 6.0 min^-1; Km cell = 0.9 uM; printed kcat/Km cell = 6.72 min^-1 uM^-1.

row_label: Table 1, substrate line 'Delta4-Androstene-3,17-dione' (steroid class C19)


substrate_name: Epitestosterone

assay_conditions_summary: pH 6; 310.15 K; buffer 100 mM potassium phosphate; cofactor NADPH

column_label: Table 1: Substrate specificity of AKR1D1 (Steroids 2011, 76(5):484-490), PDF page 14 of 15, substrate line 'Epitestosterone'; column 'Type' = C19; column 'kcat (min^-1)' = 6.0; column 'Km (uM)' = 2.9; column 'Ki (uM)' = 10.0; column 'kcat/Km (min^-1 uM^-1)' = 2.09.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.9 uM; 1 uM is one thousandth of 1 mM, so 2.9 / 1000 = 0.0029 mM. kcat: printed Table 1 cell 6.0 min^-1; the printed head is per minute, so 6.0 / 60 = 0.1 s^(-1). kcat/Km: printed Table 1 cell 2.09 min^-1 uM^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 2.09 times 1000 divided by 60 = 34.8333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate line 'Epitestosterone': kcat cell = 6.0 min^-1; Km cell = 2.9 uM; printed kcat/Km cell = 2.09 min^-1 uM^-1.

row_label: Table 1, substrate line 'Epitestosterone' (steroid class C19)

substrate: Epitestosterone


substrate_name: aldosterone

column_label: Table 1: Substrate specificity of AKR1D1 (Steroids 2011, 76(5):484-490), PDF page 14 of 15, substrate line 'Aldosterone'; column 'Type' = C21; column 'kcat (min^-1)' = 9.0; column 'Km (uM)' = 2.5; column 'Ki (uM)' = 66.5; column 'kcat/Km (min^-1 uM^-1)' = 3.68.

normalized_value_unit_evidence: Km: printed Table 1 cell 2.5 uM; 1 uM is one thousandth of 1 mM, so 2.5 / 1000 = 0.0025 mM. kcat: printed Table 1 cell 9.0 min^-1; the printed head is per minute, so 9.0 / 60 = 0.15 s^(-1). kcat/Km: printed Table 1 cell 3.68 min^-1 uM^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 3.68 times 1000 divided by 60 = 61.3333333333 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate line 'Aldosterone': kcat cell = 9.0 min^-1; Km cell = 2.5 uM; printed kcat/Km cell = 3.68 min^-1 uM^-1.

row_label: Table 1, substrate line 'Aldosterone' (steroid class C21)

substrate: aldosterone


substrate_name: cortisone

column_label: Table 1: Substrate specificity of AKR1D1 (Steroids 2011, 76(5):484-490), PDF page 14 of 15, substrate line 'Cortisone'; column 'Type' = C21; column 'kcat (min^-1)' = 11.7; column 'Km (uM)' = 15.1; column 'Ki (uM)' = N.D.; column 'kcat/Km (min^-1 uM^-1)' = 0.78.

normalized_value_unit_evidence: Km: printed Table 1 cell 15.1 uM; 1 uM is one thousandth of 1 mM, so 15.1 / 1000 = 0.0151 mM. kcat: printed Table 1 cell 11.7 min^-1; the printed head is per minute, so 11.7 / 60 = 0.195 s^(-1). kcat/Km: printed Table 1 cell 0.78 min^-1 uM^-1; 1 uM^-1 is 1000 mM^-1 and one per-minute rate is one sixtieth of the same per-second rate, so 0.78 times 1000 divided by 60 = 13 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, substrate line 'Cortisone': kcat cell = 11.7 min^-1; Km cell = 15.1 uM; printed kcat/Km cell = 0.78 min^-1 uM^-1.

row_label: Table 1, substrate line 'Cortisone' (steroid class C21)

substrate: cortisone


proof_lines:
in presence of uracil
in presence of 5-fluorouracil
in presence of thymine


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature P133R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6

proof_lines: mutant P133R, pH not specified in the publication, temperature not specified in the publication


substrate_name: testosterone

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

substrate: testosterone


assay_conditions_summary: pH 8; cofactor NADPH

column_label: Table 2 row rAtSt5betaR / Pro, columns km (microM), Kcat (min^-1), and Kcat/km (M^-1 s^-1) report 268 +/- 23, 10.11 +/- 2.99, and 628 respectively.

raw_value_unit_evidence: Table 2 row rAtSt5betaR Pro: km = 268 +/- 23 microM; Kcat = 10.11 +/- 2.99 min^-1; Kcat/km = 628 M^-1 s^-1

row_label: rAtSt5betaR / Pro


column_label: Table 2 row rAtSt5betaR / CH, columns km (microM), Kcat (min^-1), and Kcat/km (M^-1 s^-1) report 116 +/- 2, 66.85 +/- 3.78, and 9607 respectively.

raw_value_unit_evidence: Table 2 row rAtSt5betaR CH: km = 116 +/- 2 microM; Kcat = 66.85 +/- 3.78 min^-1; Kcat/km = 9607 M^-1 s^-1

row_label: rAtSt5betaR / CH


enzyme_display_name: NADH:fumarate oxidoreductase

organism: Klebsiella variicola (strain 342)

substrate_name: NADH

enzyme: NADH:fumarate oxidoreductase

substrate: NADH


organism: Mus musculus

sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset +13, so it is treated as a source-provided variant sequence.

assay_conditions_summary: pH 7

proof_lines:
isoform AKR1D4L, pH 7, 37°C
isoform AKR1D4S, pH 7, 37°C


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

column_label: Table II. Substrate specificity of delta-4-3-ketosteroid 5beta-reductase. Substrate row 'Cortisol'; column 'kcat (min-1)' = 0.49; column 'Km (uM)' = 11.0; column 'kcat / Km (min-1 uM-1)' = 0.045.

normalized_value_unit_evidence: kcat: printed cell 0.49 min-1 -> 0.008166666666666666 s^(-1); the exported value is 0.00817. Km: printed cell 11.0 uM -> 0.011 mM; the exported value is 0.011. kcat/Km: printed cell 0.045 min-1 uM-1 -> 0.75 s^(-1)*mM^(-1); the exported value is 0.7427272727272728.

raw_value_unit_evidence: Table II, decoded plain-numeral transcription (journal page 7522, PDF page 4), substrate row 'Cortisol': kcat = 0.49 min-1; Km = 11.0 uM; printed kcat / Km = 0.045 min-1 uM-1.


column_label: Table II. Substrate specificity of delta-4-3-ketosteroid 5beta-reductase. Substrate row '7a,12a-Dihydroxy-4-cholesten-3-one'; column 'kcat (min-1)' = 0.77; column 'Km (uM)' = 12.2; column 'kcat / Km (min-1 uM-1)' = 0.063.

raw_value_unit_evidence: Table II, decoded plain-numeral transcription (journal page 7522, PDF page 4), substrate row '7a,12a-Dihydroxy-4-cholesten-3-one': kcat = 0.77 min-1; Km = 12.2 uM; printed kcat / Km = 0.063 min-1 uM-1.


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: Delta(4)-3-oxosteroid 5beta-reductase

row_label: Table II, decoded plain-numeral transcription (journal page 7522, PDF page 4), substrate row '7a,12a-Dihydroxy-4-cholesten-3-one'

table_label: Table II. Substrate specificity of delta-4-3-ketosteroid 5beta-reductase

enzyme: Delta(4)-3-oxosteroid 5beta-reductase


column_label: Table II. Substrate specificity of delta-4-3-ketosteroid 5beta-reductase. Substrate row '7a-Hydroxy-4-cholesten-3-one'; column 'kcat (min-1)' = 0.60; column 'Km (uM)' = 9.10; column 'kcat / Km (min-1 uM-1)' = 0.066.

normalized_value_unit_evidence: kcat: printed cell 0.60 min-1 -> 0.01 s^(-1); the exported value is 0.01. Km: printed cell 9.10 uM -> 0.0091 mM; the exported value is 0.009. kcat/Km: printed cell 0.066 min-1 uM-1 -> 1.1 s^(-1)*mM^(-1); the exported value is 1.1111111111111112.

raw_value_unit_evidence: Table II, decoded plain-numeral transcription (journal page 7522, PDF page 4), substrate row '7a-Hydroxy-4-cholesten-3-one': kcat = 0.60 min-1; Km = 9.10 uM; printed kcat / Km = 0.066 min-1 uM-1.


substrate_name: Cortisol

column_label: Table II columns Substrate, kcat, Km, and kcat/Km; row Cortisol.

normalized_value_unit_evidence: Normalized from Table II: kcat=0.00817 s^-1; Km=0.0110 mM; kcat/Km=0.750 s^-1 mM^-1.

raw_value_unit_evidence: Table II row Cortisol: kcat=0.49 umol product/min/umol enzyme; Km=11.0 uM; kcat/Km=0.045.

row_label: Cortisol

table_label: Table II

substrate: Cortisol


column_label: Table II columns Substrate, kcat, Km, and kcat/Km; row Cortisone.

normalized_value_unit_evidence: Normalized from Table II: kcat=0.0375 s^-1; Km=0.0217 mM; kcat/Km=1.733 s^-1 mM^-1.

raw_value_unit_evidence: Table II row Cortisone: kcat=2.25 umol product/min/umol enzyme; Km=21.7 uM; kcat/Km=0.104.

row_label: Cortisone


substrate_name: Progesterone

column_label: Table II columns Substrate, kcat, Km, and kcat/Km; row Progesterone.

normalized_value_unit_evidence: Normalized from Table II: kcat=0.0302 s^-1; Km=0.00219 mM; kcat/Km=13.767 s^-1 mM^-1.

raw_value_unit_evidence: Table II row Progesterone: kcat=1.81 umol product/min/umol enzyme; Km=2.19 uM; kcat/Km=0.826.

row_label: Progesterone

substrate: Progesterone


column_label: Table II columns Substrate, kcat, Km, and kcat/Km; row 4-Androstene-3,17-dione.

normalized_value_unit_evidence: Normalized from Table II: kcat=0.0337 s^-1; Km=0.00485 mM; kcat/Km=6.933 s^-1 mM^-1.

raw_value_unit_evidence: Table II row 4-Androstene-3,17-dione: kcat=2.02 umol product/min/umol enzyme; Km=4.85 uM; kcat/Km=0.416.


column_label: Table II columns Substrate, kcat, Km, and kcat/Km; row Testosterone.

normalized_value_unit_evidence: Normalized from Table II: kcat=0.0208 s^-1; Km=0.00240 mM; kcat/Km=8.683 s^-1 mM^-1.

raw_value_unit_evidence: Table II row Testosterone: kcat=1.25 umol product/min/umol enzyme; Km=2.40 uM; kcat/Km=0.521.

row_label: Testosterone


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature P133R to reconstruct the assayed variant sequence.


column_label: Table 1 row WT - Cortisone reports kcat 9.9 min^-1, Km 15.1 uM, and kcat/Km 0.66 min^-1 uM^-1.

normalized_value_unit_evidence: kcat 0.165 s^-1; Km 0.0151 mM; explicit-column kcat/Km 11.0 s^-1 mM^-1

row_label: WT - Cortisone

table_label: Table 1


column_label: Table 1 row WT - Testosterone reports kcat 0.7 min^-1, Km 2.7 uM, and kcat/Km 0.263 min^-1 uM^-1.

row_label: WT - Testosterone


substrate_name: Uracil

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C126A to reconstruct the assayed variant sequence.

substrate: Uracil


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H673N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H673Q to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S670A with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature V309F with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y132F to reconstruct the assayed variant sequence.


organism: Digitalis lanata

column_label: Table 1; Progesterone row; Km (mM) column 0.120 +/- 0.048.

normalized_value_unit_evidence: Paper reports progesterone Km 0.120 mM.

raw_value_unit_evidence: Progesterone row; Km 0.120 +/- 0.048 mM

row_label: Progesterone row

table_label: Table 1: Substrate specificity of the r5beta-POR


column_label: Table 1; Cortisol row; Km (mM) column 0.291 +/- 0.102.

normalized_value_unit_evidence: Paper reports cortisol Km 0.291 mM.

raw_value_unit_evidence: Cortisol row; Km 0.291 +/- 0.102 mM

row_label: Cortisol row


column_label: Table 1; 4-Androstene-3,17-dion row; Km (mM) column 0.228 +/- 0.069.

normalized_value_unit_evidence: Paper reports 4-androstene-3,17-dione Km 0.228 mM.

row_label: 4-Androstene-3,17-dion row


column_label: Table 1; Cortexone row; Km (mM) column 1.597 +/- 0.275.

normalized_value_unit_evidence: Paper reports cortexone Km 1.597 mM.

raw_value_unit_evidence: Cortexone row; Km 1.597 +/- 0.275 mM

row_label: Cortexone row


column_label: Table 1; NADPH row; Km (mM) column 0.008 +/- 0.002.

normalized_value_unit_evidence: Paper reports NADPH Km 0.008 mM.

row_label: NADPH row


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


organism: Ovis aries

assay_conditions_summary: pH 7.4; cofactor NADPH

column_label: Abstract states kinetic parameters were determined with uracil as 17.46 microM and 0.14 EU/mL.

raw_value_unit_evidence: Km raw_value=17.46 microM raw_unit=microM

row_label: Sheep liver DPD / uracil

table_label: PubMed XML abstract


column_label: Abstract states kinetic parameters were determined with NADPH as 22.97 microM and 0.17 EU/mL.

raw_value_unit_evidence: Km raw_value=22.97 microM raw_unit=microM

row_label: Sheep liver DPD / NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature C671S with inferred residue-numbering offset +13 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; 293.15 K; cofactor NADPH


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


substrate_name: thymine

substrate: thymine


organism: Digitalis purpurea

column_label: Full text reports the apparent Km for NADPH as 7.9 +/- 0.3 uM and Fig. 5b is the NADPH kinetic plot

raw_value_unit_evidence: apparent Km for NADPH raw_value=7.9 +/- 0.3 raw_unit=uM

row_label: Recombinant P5betaR-MBP protein

table_label: ScienceDirect full text Results and discussion / Fig. 5b


column_label: Full text reports the apparent Km for progesterone as 39.1 +/- 1.1 uM and Fig. 5a is the progesterone kinetic plot

raw_value_unit_evidence: apparent Km for progesterone raw_value=39.1 +/- 1.1 raw_unit=uM

table_label: ScienceDirect full text Results and discussion / Fig. 5a


enzyme_display_name: NAD-dependent dihydropyrimidine dehydrogenase subunit PreA

organism: Escherichia coli (strain K12)

substrate_name: uracil

substrate: uracil


enzyme: NAD-dependent dihydropyrimidine dehydrogenase subunit PreA


substrate_name: DHT

assay_conditions_summary: pH 11

substrate: DHT


substrate_name: DHU

substrate: DHU


enzyme_display_name: NAD-dependent dihydropyrimidine dehydrogenase subunit PreT


enzyme: NAD-dependent dihydropyrimidine dehydrogenase subunit PreT


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R63K/R64H to reconstruct the assayed variant sequence.


column_label: Table 3; wild type CrSt5betaR1 row under NADPH; Kcat/KM column

raw_value_unit_evidence: paper Table 3 row wild type CrSt5betaR1 under NADPH: KM=0.4428 mM; Kcat=0.23 s^-1; Kcat/KM=520 M^-1 S^-1

row_label: wild type CrSt5betaR1 with NADPH and 2-cyclohexen-1-one

table_label: Table 3


assay_conditions_summary: pH 8; 313.15 K; cofactor NADPH

column_label: Table 2 row rAtSt5betaR / CH, columns km (microM), Kcat (min^-1), and Kcat/km (M^-1 s^-1) report 116 +/- 2, 66.85 +/- 3.78, and 9607 respectively.

raw_value_unit_evidence: Table 2 row rAtSt5betaR CH: km = 116 +/- 2 microM; Kcat = 66.85 +/- 3.78 min^-1; Kcat/km = 9607 M^-1 s^-1

row_label: rAtSt5betaR / CH

table_label: Table 2


substrate_name: progesterone

column_label: Table 2 row rAtSt5betaR / Pro, columns km (microM), Kcat (min^-1), and Kcat/km (M^-1 s^-1) report 268 +/- 23, 10.11 +/- 2.99, and 628 respectively.

raw_value_unit_evidence: Table 2 row rAtSt5betaR Pro: km = 268 +/- 23 microM; Kcat = 10.11 +/- 2.99 min^-1; Kcat/km = 628 M^-1 s^-1

row_label: rAtSt5betaR / Pro

substrate: progesterone


substrate_name: Boldenone

proof_lines: AKR1D1 finasteride testosterone

substrate: Boldenone


assay_conditions_summary: cofactor NADPH

column_label: Abstract reports affinity constants (Km) for NADPH and thymine were approximately 10 and 1 micromol/l, respectively.

raw_value_unit_evidence: Km raw_value=approximately 1 micromol/l raw_unit=micromol/l

row_label: human blood mononuclear cell dihydropyrimidine dehydrogenase / thymine

table_label: PubMed XML abstract PMID 2528450


organism: Enterococcus faecalis

assay_conditions_summary: buffer ionic strength adjusted to 0

column_label: Abstract states the Km value of the enzyme for reduced flavin mononucleotide was 2 x 10(-4) M as determined with a 26-fold preparation.

raw_value_unit_evidence: Km raw_value=2x10(-4) raw_unit=M

row_label: Streptococcus faecalis fumarate reductase with reduced flavin mononucleotide (FMNH2)

table_label: PubMed/PMC abstract PMID 4960892


substrate_name: cortisol

substrate: cortisol


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


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

proof_lines: pH 7.5, 30°C, recombinant wild-type enzyme

proof_lines: wild-type, aerobic conditions, pH 7.0, 20°C

proof_lines: wild-type, anaerobic conditions, pH 7.0, 20°C


assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH


proof_lines: mutant C671S, anaerobic conditions, pH 7.0, 20°C


proof_lines: mutant C671S, aerobic conditions, pH 7.0, 20°C


organism: Escherichia coli

substrate_name: Dihydrothymine

substrate: Dihydrothymine


organism: Pyrococcus furiosus

substrate_name: CoA

assay_conditions_summary: pH 8.4; 353.15 K; cofactor CoA

proof_lines:
pH 8.4, 80°C, substrate indolepyruvate
pH 8.4, 80°C, substrate phenylpyruvate

substrate: CoA


substrate_name: Ferredoxin

substrate: Ferredoxin


enzyme_display_name: anaerobic carbon monoxide dehydrogenase

organism: Methanosarcina barkeri

substrate_name: 2,3,5-triphenyltetrazolium chloride

proof_lines:
below 0.5 mM
pH 7.0, 25°C

enzyme: anaerobic carbon monoxide dehydrogenase

substrate: 2,3,5-triphenyltetrazolium chloride


substrate_name: methyl viologen

substrate: methyl viologen


organism: Aeropyrum pernix

substrate_name: pyruvate

substrate: pyruvate


organism: Sulfurisphaera tokodaii

assay_conditions_summary: pH 8.5; 353.15 K; cofactor CoA


enzyme_display_name: formylmethanofuran dehydrogenase

organism: Methanothermobacter thermautotrophicus

substrate_name: oxidized carbamoylviologen

enzyme: formylmethanofuran dehydrogenase

substrate: oxidized carbamoylviologen


substrate_name: methanofuran

substrate: methanofuran


organism: Sus scrofa


substrate_name: NADPH

proof_lines:
in presence of 2,6-dihydrouracil
in presence of 5-fluorouracil
in presence of uracil

substrate: NADPH


organism: Bos taurus


substrate_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; buffer 50 mM Tris/HCl; cofactor NAD+

proof_lines: at 25°C in 50 mM Tris/HCl buffer, pH 8.0

substrate: NAD+


enzyme_display_name: formaldehyde dismutase

organism: Pseudomonas putida

substrate_name: formaldehyde

enzyme: formaldehyde dismutase

substrate: formaldehyde


substrate_name: Unknown

substrate: Unknown


enzyme_display_name: aspartate-semialdehyde dehydrogenase

assay_conditions_summary: pH 8.6; 310.15 K; cofactor NADP+

proof_lines: competitive inhibitor with respect to NADP+

proof_lines: 0.2 M Tris, 1 mM EDTA, pH 8.6, 15 mM phosphate, 0.15 mM NADP+, 37°C

enzyme: aspartate-semialdehyde dehydrogenase


organism: Streptococcus pneumoniae

assay_conditions_summary: pH 8.6; 295.15 K; buffer and 200 mM KCl, at 22°C

proof_lines: Ki above 4 mM in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C


organism: Vibrio cholerae serotype O1


organism: Methanothermobacter wolfeii

substrate_name: N-formylmethanofuran

proof_lines: formylmethanofuran, tungsten-substituted molybdenum enzyme and non-substituted molybdenum enzyme

proof_lines: methylviologen, tungsten-substituted molybdenum enzyme

substrate: N-formylmethanofuran


substrate_name: methylviologen

proof_lines: methylviologen, tungsten-substituted molybdenum enzyme and non-substituted molybdenum enzyme

substrate: methylviologen


organism: Trypanosoma cruzi

substrate_name: D-glyceraldehyde 3-phosphate

assay_conditions_summary: pH 7.5; 298.15 K; buffer TEA-HCl

proof_lines: in the absence of DMSO and methanol, in TEA-HCl buffer (pH 7.5) at 25°C

proof_lines: in the presence of 5% (v/v) DMSO, in TEA-HCl buffer (pH 7.5) at 25°C

proof_lines: in the presence of 5% (v/v) methanol, in TEA-HCl buffer (pH 7.5) at 25°C

substrate: D-glyceraldehyde 3-phosphate


organism: Mus musculus

substrate_name: D-Glyceraldehyde 3-phosphate; Phosphate; NAD+

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

assay_conditions_summary: cofactor NAD+

proof_lines: versus NAD+, pH and temperature not specified in the publication

proof_lines: versus D-glyceraldehyde 3-phosphate, pH and temperature not specified in the publication


assay_conditions_summary: pH 8

proof_lines: pH and temperature not specified in the publication


organism: Oryctolagus cuniculus

substrate_name: thio-NAD+

substrate: thio-NAD+


organism: Vibrio cholerae

proof_lines: Ki above 4 mM, in 120 mM CHES (pH 8.6) buffer and 200 mM KCl, at 22°C


organism: Homo sapiens

proof_lines: recombinant dN-GAPDS enzyme mutant D311N, pH 8.9, 20°C


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NAD+

proof_lines:
free enzyme
free enzyme, at pH 7.5 and 25°C
free enzyme,25°C, pH 8.6


enzyme_display_name: UniProt Q3JQY0

organism: Burkholderia pseudomallei

enzyme: UniProt Q3JQY0


substrate_name: crotonyl-CoA

substrate: crotonyl-CoA


enzyme_display_name: UniProt Q8Z9U1

organism: Yersinia pestis

enzyme: UniProt Q8Z9U1


enzyme_display_name: UniProt P0AEK4

organism: Escherichia coli

substrate_name: NADH

enzyme: UniProt P0AEK4

substrate: NADH


enzyme_display_name: UniProt Q9BH77

organism: Plasmodium falciparum

enzyme: UniProt Q9BH77


enzyme_display_name: UniProt Q7MAW0

organism: Porphyromonas gingivalis

enzyme: UniProt Q7MAW0


enzyme_display_name: prephenate dehydrogenase

organism: Methanohalophilus mahii

substrate_name: NADP+

enzyme: prephenate dehydrogenase

substrate: NADP+


enzyme_display_name: UniProt Q8DUW0

organism: Streptococcus mutans

enzyme: UniProt Q8DUW0


substrate_name: prephenate

substrate: prephenate


organism: Sus scrofa


substrate_name: phosphate

proof_lines: pH 8.8, enzyme isolated of healthy patients

proof_lines: pH 8.8, enzyme isolated of sarcoma tissue

substrate: phosphate


assay_conditions_summary: pH 8.9; 298.15 K; cofactor NAD+

proof_lines: pH 8.9, 25°C, substrate D-glyceraldehyde 3-phosphate


assay_conditions_summary: cofactor NADH


organism: Candida maltosa


enzyme_display_name: 2,5-dioxovalerate dehydrogenase

organism: Pseudomonas putida

substrate_name: alpha-Ketoglutaric semialdehyde

enzyme: 2,5-dioxovalerate dehydrogenase

substrate: alpha-Ketoglutaric semialdehyde


organism: Carthamus tinctorius

substrate_name: crotonyl-[acyl-carrier protein]

substrate: crotonyl-[acyl-carrier protein]


assay_conditions_summary: cofactor CoA


enzyme_display_name: prephenate dehydrogenase (NADP+)

organism: Methanothrix harundinacea

proof_lines: mutant Q227E, pH 7.6, temperature not specified in the publication

enzyme: prephenate dehydrogenase (NADP+)


substrate_name: L-arogenate

substrate: L-arogenate


proof_lines: wild-type, pH 7.6, temperature not specified in the publication