organism: Ralstonia sp.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH

proof_lines: with benzaldehyde as cosubstrate, at pH 7.5 and 30°C

proof_lines: with cyclohexanone as cosubstrate, at pH 7.5 and 30°C


enzyme_display_name: alcohol dehydrogenase [NAD(P)+]

substrate_name: NADP+

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.

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

proof_lines: with benzyl alcohol as cosubstrate, at pH 9.0 and 30°C

enzyme: alcohol dehydrogenase [NAD(P)+]

substrate: NADP+

status: unverified

source: brenda


substrate_name: Cyclohexanol

assay_conditions_summary: pH 9; 303.15 K; cofactor NADPH

substrate: Cyclohexanol


substrate_name: cyclohexanone

substrate: cyclohexanone


substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: benzaldehyde

substrate: benzaldehyde


organism: Haloferax volcanii

substrate_name: NADPH

assay_conditions_summary: pH 6; cofactor NADPH

proof_lines: pH 6.0, temperature not specified in the publication

substrate: NADPH


assay_conditions_summary: pH 10; cofactor NADP+

proof_lines: pH 10.0, temperature not specified in the publication


smiles: CCCCO

assay_conditions_summary: pH 10


substrate_name: acetaldehyde

smiles: CC=O

assay_conditions_summary: pH 6

substrate: acetaldehyde


substrate_name: ethanol

smiles: CCO

substrate: ethanol


organism: Halobacterium salinarum

assay_conditions_summary: pH 6; 323.15 K; cofactor NADPH


assay_conditions_summary: pH 10; 323.15 K; cofactor NADP+


smiles: CCCO


organism: Thermococcus kodakarensis

substrate_name: NAD+

kcat_over_km_origin: calculated

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

assay_conditions_summary: pH 6; cofactor NAD+

proof_lines: with (RS)-1-phenylethanol as cosubstrate, at pH 6.0 and 70°C

proof_lines: with meso-2,3-butanediol as cosubstrate, at pH 6.0 and 70°C

data_origin: experimental

substrate: NAD+


assay_conditions_summary: pH 6; cofactor NADP+


substrate_name: acetoin

verification_status: corrected

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

assay_conditions_summary: pH 6; cofactor NADH

column_label: Table 4 row Acetoin (0-200); cosubstrate NADH (0.2); columns Apparent Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

table_label: Table 4

substrate: acetoin

status: corrected


substrate_name: NADH

column_label: Table 4 row NADH (0-0.4); cosubstrate Acetoin (100); columns Apparent Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).

substrate: NADH


column_label: Table 4 row NADPH (0-0.4); cosubstrate Acetoin (100); columns Apparent Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).


column_label: Table 4 row (RS)-1-Phenylethanol (0-200); cosubstrate NAD+ (1.0); columns Apparent Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1); footnote b.


smiles: CC(C(C)O)O

column_label: Table 4 row meso-2,3-Butanediol (0-250); cosubstrate NAD+ (1.0); columns Apparent Km (mM), kcat (s^-1), and kcat/Km (s^-1 mM^-1).


organism: Solanum tuberosum

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADP+


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: Salicylaldehyde

substrate: Salicylaldehyde


smiles: CCCC=CC=O


organism: Leuconostoc mesenteroides

assay_conditions_summary: cofactor NADP+

proof_lines:
oxidation of ethanol
oxidation of allyl alcohol


assay_conditions_summary: cofactor NADPH

proof_lines:
reduction of acrylaldehyde
reduction of acetaldehyde


assay_conditions_summary: cofactor NADH

proof_lines:
reduction of acetaldehyde
reduction of acrylaldehyde


assay_conditions_summary: cofactor NAD+

proof_lines:
oxidation of allyl alcohol
oxidation of ethanol


enzyme_display_name: glycerol dehydrogenase (NADP+)

organism: Rattus norvegicus

enzyme: glycerol dehydrogenase (NADP+)


substrate_name: D-glyceraldehyde

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

substrate: D-glyceraldehyde


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


organism: Neurospora crassa


organism: Cucumis melo


proof_lines:
cofactor NADH
cofactor NADPH


enzyme_display_name: gluconate 5-dehydrogenase

organism: Gluconacetobacter liquefaciens

enzyme: gluconate 5-dehydrogenase


substrate_name: D-gluconate

substrate: D-gluconate


organism: Halobacterium sp.

verification_status: verified

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

column_label: Table 2 row NADPH, column Km = 0.05 +/- 0.02 mM.

row_label: NADPH

table_label: Table 2: Kinetics of His-HsADH2

status: verified


column_label: Table 2 row NADP+, column Km = 0.2 +/- 0.03 mM.

normalized_value_unit_evidence: Km 0.2 mM.

row_label: NADP+


column_label: Table 2 row Acetaldehyde, column Km = 3.4 +/- 0.7 mM.

normalized_value_unit_evidence: Km 3.4 mM.

row_label: Acetaldehyde


column_label: Table 2 row 1-Propanol, column Km = 21.4 +/- 4 mM.


column_label: Table 2 row Ethanol, column Km = 107.9 +/- 10 mM.

row_label: Ethanol


organism: Gluconobacter oxydans

assay_conditions_summary: pH 9.7; 310.15 K; cofactor NADP+

proof_lines: oxidation, pH 9.7, 37°C, Vmax: 2.1 micromol/min/mg


assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

proof_lines: reduction, pH 7.0, 30°C, Vmax: 101 micromol/min/mg


proof_lines: reduction, pH 7.0, 30°C, Vmax: 77.9 micromol/min/mg


substrate_name: L-arabitol

smiles: C(C(C(C(CO)O)O)O)O

proof_lines: oxidation, pH 9.7, 37°C, Vmax: 8.67 micromol/min/mg

substrate: L-arabitol


organism: Thermococcus sibiricus

substrate_name: NADP+

assay_conditions_summary: pH 10.5; 333.15 K; cofactor NADP+

proof_lines: 60°C, pH 10.5, cosubstrate: 2,5-hexandiol

substrate: NADP+


substrate_name: D-xylose

substrate: D-xylose


organism: Oryctolagus cuniculus

substrate_name: H+; D-Glyceraldehyde; NADPH

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

substrate: H+; D-Glyceraldehyde; NADPH


organism: Haloarcula marismortui


enzyme_display_name: octanol dehydrogenase

organism: Saccharomyces cerevisiae

enzyme: octanol dehydrogenase


smiles: CCCCCCCCO


protein_accession_database: UniProt

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W23A to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W23M to reconstruct the assayed variant sequence.


enzyme_display_name: (R)-aminopropanol dehydrogenase

organism: Bacillus subtilis

enzyme: (R)-aminopropanol dehydrogenase


smiles: CC(CN)O


organism: Moniezia expansa

smiles: CCCCCCC=CC=O


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Clostridium beijerinckii

substrate_name: Butanal

smiles: CCCC=O

proof_lines: enzyme from strain NRRL B592, at pH 7.5 and 25°C

substrate: Butanal


organism: Pseudomonas sp.


proof_lines: with D,L-1-aminopropan-2-ol as substrate


organism: Lactobacillus delbrueckii

proof_lines: reverse reaction, pH 6.5, 25°C, crude extract


proof_lines: soluble extract of disintegrated mitochondria


organism: Lactiplantibacillus plantarum


substrate_name: D-glucuronate

substrate: D-glucuronate


organism: Lactobacillus acidophilus

assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADPH


enzyme_display_name: Carbonyl reductase [NADPH] 1

organism: Sus scrofa

substrate_name: prostaglandin E2

source_db: uniprot

proof_lines: kcats are 2 min(-1), 285 min(-1), 460 min(-1), 58 min(-1) for prostaglandin E2, menadione, 9,1 O-phenanthrene-quinone and 4-nitrobenzaldehyde as substrates, respectively.

enzyme: Carbonyl reductase [NADPH] 1

substrate: prostaglandin E2

source: uniprot


substrate_name: menadione

substrate: menadione


substrate_name: NADPH

substrate: NADPH


organism: Homo sapiens

substrate_name: all-trans-retinal

column_label: PMID 12435598 AbstractText / Crossref abstract; metric segment reports only a retinoid apparent Km range, not a row-specific all-trans-retinal cell. The package/export value 0.08 mM is outside the normalized paper range 0.00008 to 0.0004 mM.

normalized_value_unit_evidence: Retinoid range 0.08 to 0.4 uM = 0.00008 to 0.0004 mM; exported/package Km is 0.08 mM.

raw_value_unit_evidence: PubMed/Crossref abstract prose reports retinoid apparent Km values between 0.08 uM and 0.4 uM; no exact substrate-specific retinol/retinal cell was recovered.

row_label: retinoid range; all-trans-retinal not individually mapped in accessible prose

table_label: Abstract/prose apparent Km sentence

substrate: all-trans-retinal


sequence_source: multiple

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

source_databases_merged: brenda uniprot


substrate_name: all-trans-retinol

column_label: PMID 12435598 AbstractText / Crossref abstract; metric segment reports only a retinoid apparent Km range, not a row-specific all-trans-retinol cell. The package/export value 0.4 mM is outside the normalized paper range 0.00008 to 0.0004 mM.

normalized_value_unit_evidence: Retinoid range 0.08 to 0.4 uM = 0.00008 to 0.0004 mM; exported/package Km is 0.4 mM.

row_label: retinoid range; all-trans-retinol not individually mapped in accessible prose

substrate: all-trans-retinol


assay_conditions_summary: pH 7.4; cofactor NADP+

column_label: PMID 12435598 AbstractText / Crossref abstract; metric segment apparent Km for NADP+; raw value 0.65 uM; normalized value 0.00065 mM. This contradicts the package/export Km 0.65 mM.

normalized_value_unit_evidence: 0.65 uM = 0.00065 mM; exported/package Km is 0.65 mM.

raw_value_unit_evidence: PubMed/Crossref abstract prose reports apparent Km for NADP+ as 0.65 uM.


substrate_name: NAD+

assay_conditions_summary: pH 7.4; cofactor NAD+

column_label: PMID 12435598 AbstractText / Crossref abstract; metric segment apparent Km for NAD+; raw value 1200 uM; normalized value 1.2 mM. This contradicts the package/export Km 1060.0 mM.

normalized_value_unit_evidence: 1200 uM = 1.2 mM; exported/package Km is 1060.0 mM.

raw_value_unit_evidence: PubMed/Crossref abstract prose reports apparent Km for NAD+ as 1200 uM.

row_label: NAD+

substrate: NAD+


substrate_name: NADH

assay_conditions_summary: pH 7.4; cofactor NADH

column_label: PMID 12435598 AbstractText / Crossref abstract; metric segment apparent Km for NADH; raw value 1060 uM; normalized value 1.06 mM. This contradicts the package/export Km 1200.0 mM.

normalized_value_unit_evidence: 1060 uM = 1.06 mM; exported/package Km is 1200.0 mM.

raw_value_unit_evidence: PubMed/Crossref abstract prose reports apparent Km for NADH as 1060 uM.

row_label: NADH

substrate: NADH


enzyme_display_name: Glycerol dehydrogenase

organism: Escherichia coli (strain K12)

substrate_name: glycerol (at 25 degrees Celsius and pH 7)

proof_lines: The catalytic efficiency of the reverse reaction (dihydroxyacetone reduction) is more than 100-fold higher than that of the forward direction (glycerol oxidation).

enzyme: Glycerol dehydrogenase


substrate_name: dihydroxyacetone (at 25 degrees Celsius and pH 7)

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


substrate_name: glycolaldehyde (at 25 degrees Celsius and pH 7)

smiles: C(C=O)O


substrate_name: methylglyoxal (at 25 degrees Celsius and pH 7)


enzyme_display_name: Aldo-keto reductase family 1 member A1

substrate_name: S-nitroso-CoA

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 959 min(-1) for S-nitroso-CoA as substrate (PubMed:30538128). kcat is 604 min(-1) for D-glucuronate as substrate (PubMed:30538128). kcat is 306 min(-1) for D,L-glyceraldehyde as substrate (PubMed:30538128). kcat is 948 min(-1) for S

enzyme: Aldo-keto reductase family 1 member A1

substrate: S-nitroso-CoA


substrate_name: D,L-glyceraldehyde

substrate: D,L-glyceraldehyde


enzyme_display_name: ribitol 2-dehydrogenase

organism: Cereibacter sphaeroides

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+

enzyme: ribitol 2-dehydrogenase


substrate_name: D-ribulose

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

substrate: D-ribulose


substrate_name: ribitol

substrate: ribitol


organism: Pantoea agglomerans


substrate_name: allitol

smiles: C(C(C(C(C(CO)O)O)O)O)O

substrate: allitol


enzyme_display_name: Sorbitol dehydrogenase

substrate_name: sorbitol

proof_lines: kcat is 1.7 sec(-1) for the oxidation of D-sorbitol at pH 7.1, and 5.2 sec(-1) at pH 10.0. kcat is 5.9 sec(-1) the oxidation of xylitol as substrate at pH 10.0. kcat is 5.3 sec(-1) the oxidation of L-threitol as substrate at pH 10.0. kcat i

enzyme: Sorbitol dehydrogenase

substrate: sorbitol


substrate_name: NAD(+)

substrate: NAD(+)


assay_conditions_summary: pH 7.1; cofactor NADH


smiles: CC(CO)O


smiles: CCC(CO)O


smiles: C(C(CN)O)O


substrate_name: NAD(+) (with DL-1,2-propanediol as substrate)


organism: Gluconobacter oxydans

substrate_name: D-arabitol

substrate: D-arabitol


substrate_name: D-sorbitol

substrate: D-sorbitol


substrate_name: D-gluconic acid

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

substrate: D-gluconic acid


enzyme_display_name: Aldo-keto reductase family 1 member C4

organism: Macaca fuscata fuscata

proof_lines: kcat is 4.9 min(-1) for 5-beta-pregnan-20-alpha-ol-3-one as substrate. kcat is 4.9 min(-1) for 3alpha-hydroxy-5alpha-androstan-17-one as substrate. kcat is 23 min(-1) for 5alpha-pregnane-3alpha,21-diol-20-one.

enzyme: Aldo-keto reductase family 1 member C4


substrate_name: (s)-tetralol

substrate: (s)-tetralol


organism: Streptomyces exfoliatus

substrate_name: progesterone

proof_lines: in reversed micelles, value depends on type of detergent

proof_lines: in aqueous solution, value increases with increasing ionic strength

substrate: progesterone


substrate_name: NADH


enzyme_display_name: Aldo-keto reductase family 1 member C3

proof_lines: kcat is 0.044 min(-1) for testosterone oxydation (PubMed:10998348). kcat is 13 min(-1) for 9-cis-retinal as substrate (PubMed:21851338). kcat is 4.18 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction (PubMed:10998348). kcat is 0.3

enzyme: Aldo-keto reductase family 1 member C3


enzyme_display_name: Aldo-keto reductase family 1 member B10

proof_lines: kcat is 640 min(-1) for glyceraldehyde as substrate (PubMed:12732097). kcat is 185 min(-1) for pyridine-3-aldehyde as substrate (PubMed:12732097). kcat is 116 min(-1) for acrolein as substrate. kcat is 103 min(-1) for 3-methyl-2-butenal as

enzyme: Aldo-keto reductase family 1 member B10


substrate_name: all-trans-retinal


substrate_name: androstanediol

assay_conditions_summary: pH 8.9; cofactor NADP+

column_label: PMC Table 4, panel Androstanediol -> androsterone, row Adiol alone, column Km, uM reports 1 +/- 0.03.

raw_value_unit_evidence: Km raw_value=1 +/- 0.03 raw_unit=uM

row_label: Androstanediol -> androsterone; Adiol alone

table_label: Table 4. Summary of II Brain activity with androgens

substrate: androstanediol


proof_lines: kcat is 11000 min(-1) for pyridine-3-carbaldehyde as substrate. kcat is 2500 min(-1) for D,L-glyceraldehyde as substrate.


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

substrate_name: tetramyristoyl cardiolipin

proof_lines: kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA (PubMed:28888424). kcat is 706 min(-1) for allopregnanolone (PubMed:28888424).

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2

substrate: tetramyristoyl cardiolipin


substrate_name: tetralinoleoyl cardiolipin

substrate: tetralinoleoyl cardiolipin


organism: Klebsiella aerogenes

substrate_name: NAD+

assay_conditions_summary: pH 11; 298.15 K; cofactor NAD+

proof_lines:
pH 11
at pH 11.0 and 25°C

substrate: NAD+


proof_lines:
pH 11
pH 7
at pH 11.0 and 25°C


organism: Arabidopsis thaliana

proof_lines: kcat is 0.33 sec(-1) towards sorbitol for the reaction with sorbitol as substrate. kcat is 0.39 sec(-1) towards NAD(+) for the reaction with sorbitol as substrate.


enzyme_display_name: malate dehydrogenase (NADP+)

organism: Cicer arietinum

substrate_name: NADPH

enzyme: malate dehydrogenase (NADP+)

substrate: NADPH


substrate_name: NADP+

substrate: NADP+


substrate_name: oxaloacetate

substrate: oxaloacetate


substrate_name: (S)-malate

substrate: (S)-malate


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


smiles: CC(C)CCC=O


organism: Danio rerio

substrate_name: cortisone

proof_lines: 28°C, pH not specified in the publication

substrate: cortisone


enzyme_display_name: (S,S)-butanediol dehydrogenase

organism: Klebsiella pneumoniae

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

smiles: CC(C(C)O)O

enzyme: (S,S)-butanediol dehydrogenase


proof_lines: pH 8.0, 25°C, recombinant wild-type enzyme


enzyme_display_name: glyoxylate reductase (NADP(+))

substrate_name: glyoxylate

source_db: oed

smiles: O=CC(=O)O

enzyme: glyoxylate reductase (NADP(+))

substrate: glyoxylate

source: oed


organism: Malus domestica


assay_conditions_summary: pH 7.8; 298.15 K; cofactor NADPH


assay_conditions_summary: pH 7.3; 298.15 K; cofactor NADPH


substrate_name: Succinic semialdehyde

smiles: O=CCCC(=O)O

substrate: Succinic semialdehyde


enzyme_display_name: hydroxypyruvate reductase

enzyme: hydroxypyruvate reductase


substrate_name: Hydroxypyruvate

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

substrate: Hydroxypyruvate


substrate_name: phenylpyruvate

substrate: phenylpyruvate


organism: Spinacia oleracea

substrate_name: NADPH; Oxaloacetate; H+

km_display: Not reported

assay_conditions_summary: cofactor NADPH

column_label: Table 4, Oxaloacetate block, thioredoxin m, amount 2 ug row, S0.5/Vmax/h columns.

raw_value_unit_evidence: Table 4: S0.5 51 uM; Vmax 4.8 umol NADPH min^-1 mg enzyme^-1; Hill coefficient 1.18.

row_label: Oxaloacetate; thioredoxin m; amount 2 ug

substrate: NADPH; Oxaloacetate; H+


substrate_name: Oxaloacetate; NADPH; H+

column_label: Table 4, Oxaloacetate block, thioredoxin m, amount 5 ug row, S0.5/Vmax/h columns.

raw_value_unit_evidence: Table 4: S0.5 83 uM; Vmax 6.9 umol NADPH min^-1 mg enzyme^-1; Hill coefficient 1.45.

row_label: Oxaloacetate; thioredoxin m; amount 5 ug

substrate: Oxaloacetate; NADPH; H+


substrate_name: NADPH; H+; Oxaloacetate

column_label: Table 4, Oxaloacetate block, thioredoxin f, amount 2 ug row, S0.5/Vmax/h columns.

raw_value_unit_evidence: Table 4: S0.5 65 uM; Vmax 6 umol NADPH min^-1 mg enzyme^-1; Hill coefficient 1.73.

row_label: Oxaloacetate; thioredoxin f; amount 2 ug

substrate: NADPH; H+; Oxaloacetate


column_label: Table 4, NADPH block, thioredoxin f, amount 2 ug row, S0.5/Vmax/h columns.

raw_value_unit_evidence: Table 4: S0.5 54 uM; Vmax 5.9 umol NADPH min^-1 mg enzyme^-1; Hill coefficient 1.75.

row_label: NADPH; thioredoxin f; amount 2 ug


enzyme_display_name: lactaldehyde reductase

organism: Rattus norvegicus

substrate_name: acetaldehyde

smiles: CC=O

enzyme: lactaldehyde reductase

substrate: acetaldehyde


substrate_name: ethanol

smiles: CCO

substrate: ethanol


substrate_name: DL-lactaldehyde

smiles: CC(C=O)O

substrate: DL-lactaldehyde


enzyme_display_name: isopropanol dehydrogenase (NADP+)

organism: Trichomonas vaginalis

substrate_name: Butanone

smiles: CCC(=O)C

enzyme: isopropanol dehydrogenase (NADP+)

substrate: Butanone


substrate_name: acetone

smiles: CC(=O)C

substrate: acetone


smiles: CCC(=O)CC


smiles: CC(C)O


smiles: CCC(C)O


smiles: CCC(CC)O


assay_conditions_summary: pH 7; 310.15 K; cofactor NADP+


smiles: CCCC(C)O


smiles: CCCO


substrate_name: NADPH

assay_conditions_summary: pH 9; 310.15 K; cofactor NADPH

substrate: NADPH


smiles: CC(C)CCCO


smiles: CC(C)CCCC(C)O


enzyme_display_name: glyoxylate reductase (NADP+)

organism: Neurospora crassa

enzyme: glyoxylate reductase (NADP+)


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


organism: Methylotuvimicrobium alcaliphilum

assay_conditions_summary: pH 7; 310.15 K; cofactor NADH

proof_lines: cosubsubstrate 3-hydroxypyruvate, 37°C, pH 7


assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

proof_lines:
cosubstrate NADH, pH 7, 37°C
cosubstrate NADPH, pH 7, 37°C


organism: Methylococcus capsulatus


proof_lines:
cosubstrate NADPH, pH 7, 37°C
cosubstrate NADH, pH 7, 37°C


enzyme_display_name: methylglyoxal reductase (NADH)

organism: Capra hircus

enzyme: methylglyoxal reductase (NADH)


substrate_name: Phenylglyoxal

substrate: Phenylglyoxal


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


organism: Bacillus licheniformis

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


smiles: CC(C(C)O)O


substrate_name: diacetyl

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

substrate: diacetyl


organism: Bos taurus

proof_lines: value increases with NaCl concentrations higher than 10 mM


substrate_name: D-glycerate

assay_conditions_summary: pH 9

proof_lines: D-glycerate oxidation, 50 mM, NaCl, pH 9

substrate: D-glycerate


substrate_name: NAD+; Lactaldehyde

assay_conditions_summary: cofactor NAD+

substrate: NAD+; Lactaldehyde


substrate_name: NAD+

substrate: NAD+


organism: Methylosinus trichosporium

substrate_name: glyoxylate

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

proof_lines:
cosubstrate NADPH, pH 7, 30°C
cosubstrate NADH, pH 7, 30°C

substrate: glyoxylate


proof_lines: cosubsubstrate 3-hydroxypyruvate, 30°C, pH 7


assay_conditions_summary: pH 7; 303.15 K; cofactor NADH


organism: Acetobacter aceti

substrate_name: glycolate

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

assay_conditions_summary: pH 9; 318.15 K; cofactor NADP+

proof_lines: with NAD+ as cosubstrate, at pH 9.0 and 45°C

proof_lines: with NADP+ as cosubstrate, at pH 9.0 and 45°C

substrate: glycolate


assay_conditions_summary: pH 4; 318.15 K; cofactor NADPH

proof_lines: with NADH as cosubstrate, at pH 4.0 and 45°C

proof_lines: with NADPH as cosubstrate, at pH 4.0 and 45°C


organism: Pyrococcus horikoshii OT3

assay_conditions_summary: pH 7.5; cofactor NADPH

proof_lines: with hydroxypyruvate as substrate, pH 7.5


assay_conditions_summary: pH 7.5; cofactor NADH


organism: Zea mays

substrate_name: 3-Hydroxypyruvate; H+; NADPH

substrate: 3-Hydroxypyruvate; H+; NADPH


substrate_name: Hydroxypyruvate

proof_lines: ammonium sulfate fractionated leaf extracts, 45-60% fraction

substrate: Hydroxypyruvate


organism: Euglena gracilis

assay_conditions_summary: cofactor NADP+


organism: Aspergillus fumigatus

assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication


substrate_name: n-butanol

smiles: CCCCO

substrate: n-butanol


substrate_name: NADP+

substrate: NADP+


assay_conditions_summary: pH 9; cofactor NAD+


organism: Aeropyrum pernix

assay_conditions_summary: pH 10; 323.15 K; cofactor NADP+

proof_lines: pH 10.0, 50°C, with cofactor NAD+, recombinant enzyme

proof_lines: pH 10.0, 50°C, with cofactor NADP+, recombinant enzyme


substrate_name: (S)-malate

proof_lines: pH and temperature not specified in the publication

substrate: (S)-malate


organism: Hordeum vulgare

proof_lines: enzyme activity of wild-type in 40-60% precipitate fractions after ammonium sulfate fractionation


proof_lines: enzyme activity of LaPr 88/29 mutant which lacks NADH-prefering hydroxypyruvate reductase in 40-60% precipitate fractions after ammonium sulfate fractionation


organism: Pseudomonas putida


organism: Thermus thermophilus


substrate_name: oxaloacetate

proof_lines:
enzyme from intermembrane space
enzyme from mitochondrial matrix

substrate: oxaloacetate


organism: Mycobacterium sp.

substrate_name: (R,S)-acetoin

assay_conditions_summary: pH 7; 303.15 K; cofactor NAD+

substrate: (R,S)-acetoin


organism: Bacillus subtilis


organism: Methanothermobacter thermautotrophicus

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


organism: Pseudomonas aeruginosa


organism: Populus gelrica


substrate_name: 3-Hydroxypyruvate; H+; NADH

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

assay_conditions_summary: cofactor NADH

substrate: 3-Hydroxypyruvate; H+; NADH


organism: Spinacia oleracea


organism: Pyrococcus horikoshii

assay_conditions_summary: pH 8; 323.15 K; cofactor NADPH

proof_lines: with NADPH as cosubstrate, at pH 8.0 and 50°C

proof_lines: with NADH as cosubstrate, at pH 8.0 and 50°C

proof_lines: in the presence of NADH, at pH 8.0 and 50°C


organism: Sinorhizobium meliloti

substrate_name: pyruvate

substrate: pyruvate


organism: Clostridium autoethanogenum

substrate_name: acetone

substrate: acetone


organism: Escherichia coli

substrate_name: H+; Oxaloacetate; NADH

substrate: H+; Oxaloacetate; NADH


organism: Bos taurus


assay_conditions_summary: pH 6; cofactor NADPH


organism: Pyrococcus yayanosii

assay_conditions_summary: pH 8; cofactor NADPH


organism: Pyrococcus furiosus


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.8; cofactor NADPH

column_label: PDF Table 1 columns Varied substrate=NADPH^1; Fixed substrate=Glyoxylate; Km uM=2.2 +/- 0.3; kcat s^-1=9.3 +/- 0.1; kcat/Km s^-1 mM^-1=4370 +/- 446

normalized_value_unit_evidence: Km 0.0022 mM; kcat 9.3 s^-1; expected kcat/Km 4227.2727 s^-1 mM^-1 from rounded kcat/Km while paper labeled kcat/Km is 4370 +/- 446 s^-1 mM^-1

row_label: AtGLYR1; varied NADPH^1; fixed Glyoxylate

table_label: Table 1


substrate_name: Succinic semialdehyde

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

column_label: PDF Table 1 columns Varied substrate=SSA^1; Fixed substrate=NADPH; Km uM=870 +/- 40; kcat s^-1=10.1 +/- 0.4; kcat/Km s^-1 mM^-1=11.6 +/- 2.2

normalized_value_unit_evidence: Km 0.87 mM; kcat 10.1 s^-1; kcat/Km 11.6092 s^-1 mM^-1 from rounded kcat/Km and paper labeled 11.6 +/- 2.2 s^-1 mM^-1

row_label: AtGLYR1; varied SSA^1; fixed NADPH

substrate: Succinic semialdehyde


proof_lines: isoform GLYR2, with succinic semialdehyde as cosubstrate, at pH 7.8 and 25°C

proof_lines: isoform GLYR2, with glyoxylate as cosubstrate, at pH 7.8 and 25°C


column_label: PDF Table 1 columns Varied substrate=SSA^2; Fixed substrate=NADPH; Km uM=8960 +/- 710; kcat s^-1=17.0 +/- 2.2; kcat/Km s^-1 mM^-1=1.9 +/- 0.3

normalized_value_unit_evidence: Km 8.96 mM; kcat 17.0 s^-1; kcat/Km 1.8973 s^-1 mM^-1 from rounded kcat/Km and paper labeled 1.9 +/- 0.3 s^-1 mM^-1

row_label: AtGLYR2; varied SSA^2; fixed NADPH


column_label: PDF Table 1 columns Varied substrate=Glyoxylate; Fixed substrate=NADPH; Km uM=19.3 +/- 4.0; kcat s^-1=18.4 +/- 10.0; kcat/Km s^-1 mM^-1=906 +/- 353

normalized_value_unit_evidence: Km 0.0193 mM; kcat 18.4 s^-1; expected kcat/Km 953.3679 s^-1 mM^-1 from rounded kcat/Km while paper labeled kcat/Km is 906 +/- 353 s^-1 mM^-1

row_label: AtGLYR2; varied Glyoxylate; fixed NADPH


column_label: PDF Table 1 columns Varied substrate=Glyoxylate; Fixed substrate=NADPH; Km uM=23.2 +/- 3.2; kcat s^-1=28.4 +/- 2.8; kcat/Km s^-1 mM^-1=1259 +/- 188

row_label: AtGLYR1; varied Glyoxylate; fixed NADPH


column_label: PDF Table 1 columns Varied substrate=Glyoxylate^1; Fixed substrate=NADPH; Km uM=4.5 +/- 0.9

normalized_value_unit_evidence: Km 0.0045 mM; row required only Km

row_label: AtGLYR1; varied Glyoxylate^1; fixed NADPH


organism: Saccharomyces cerevisiae


organism: Corynebacterium glutamicum

assay_conditions_summary: pH 10.5; cofactor NAD+


substrate_name: NADH

assay_conditions_summary: pH 6; cofactor NADH

substrate: NADH


enzyme_display_name: Glyoxylate/hydroxypyruvate reductase A

organism: Escherichia coli (strain K12)

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 5 row YcdW / Glyoxylate, column Km (mM), raw value 0.6; table header gives Km (mM)

normalized_value_unit_evidence: Paper Km 0.6 mM is already in mM and matches expected Km 0.6 mM.

raw_value_unit_evidence: Table 5 row YcdW / Glyoxylate, column Km (mM), raw value 0.6 (0.6 mM); substrate row aligns with expected label 'glyoxylate (at 25 degrees Celsius and pH 7)'.

row_label: YcdW | Glyoxylate

table_label: Table 5. Kinetic parameters of YcdW and YiaE enzymes

enzyme: Glyoxylate/hydroxypyruvate reductase A


column_label: Table 5 row YcdW / Hydroxypyruvate, column Km (mM), raw value 1; table header gives Km (mM)

normalized_value_unit_evidence: Paper Km 1 mM is already in mM and matches expected Km 1 mM.

raw_value_unit_evidence: Table 5 row YcdW / Hydroxypyruvate, column Km (mM), raw value 1 (1 mM); substrate row aligns with expected label 'hydroxypyruvate (at 25 degrees Celsius and pH 7)'.

row_label: YcdW | Hydroxypyruvate


enzyme_display_name: Glyoxylate/hydroxypyruvate reductase B

substrate_name: hydroxypyruvate (at pH 7.5)

column_label: Table 5 row YiaE / Hydroxypyruvate, column Km (mM), raw value 0.7; table header gives Km (mM)

normalized_value_unit_evidence: Paper Km 0.7 mM is already in mM and matches expected Km 0.7 mM.

raw_value_unit_evidence: Table 5 row YiaE / Hydroxypyruvate, column Km (mM), raw value 0.7 (0.7 mM); substrate row aligns with expected label 'hydroxypyruvate (at pH 7.5)'.

row_label: YiaE | Hydroxypyruvate

enzyme: Glyoxylate/hydroxypyruvate reductase B

substrate: hydroxypyruvate (at pH 7.5)


substrate_name: glyoxylate (at pH 7.5)

column_label: Table 5 row YiaE / Glyoxylate, column Km (mM), raw value 6.6; table header gives Km (mM)

normalized_value_unit_evidence: Paper Km 6.6 mM is already in mM and matches expected Km 6.6 mM.

raw_value_unit_evidence: Table 5 row YiaE / Glyoxylate, column Km (mM), raw value 6.6 (6.6 mM); substrate row aligns with expected label 'glyoxylate (at pH 7.5)'.

row_label: YiaE | Glyoxylate

substrate: glyoxylate (at pH 7.5)


enzyme_display_name: UniProt Q92LZ4

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q92LZ4

source: skid


assay_conditions_summary: pH 7.5; 298.15 K; cofactor NADPH


substrate_name: glyoxylate

substrate: glyoxylate


substrate_name: phenylpyruvate

substrate: phenylpyruvate


enzyme_display_name: UniProt Q92T34

enzyme: UniProt Q92T34


organism: Homo sapiens

substrate_name: prostaglandin H2

proof_lines: kcat is 0.044 min(-1) for testosterone oxydation (PubMed:10998348). kcat is 13 min(-1) for 9-cis-retinal as substrate (PubMed:21851338). kcat is 4.18 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction (PubMed:10998348). kcat is 0.3

substrate: prostaglandin H2


substrate_name: glyoxylate (at 25 degrees Celsius and pH 7)

column_label: Table 5 row YcdW / Glyoxylate, column Km (mM), reports 0.6.

normalized_value_unit_evidence: Km 0.6 mM is already normalized and matches target 0.6 mM.

raw_value_unit_evidence: Table 5 row YcdW / Glyoxylate, column Km (mM), raw value 0.6 mM.


substrate_name: hydroxypyruvate (at 25 degrees Celsius and pH 7)

column_label: Table 5 row YcdW / Hydroxypyruvate, column Km (mM), reports 1.

normalized_value_unit_evidence: Km 1.0 mM is already normalized and matches target 1.0 mM.

raw_value_unit_evidence: Table 5 row YcdW / Hydroxypyruvate, column Km (mM), raw value 1 mM.


assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Table 5 row YiaE / Hydroxypyruvate, column Km (mM), reports 0.7.

normalized_value_unit_evidence: Km 0.7 mM is already normalized and matches target 0.7 mM.

raw_value_unit_evidence: Table 5 row YiaE / Hydroxypyruvate, column Km (mM), raw value 0.7 mM.


column_label: Table 5 row YiaE / Glyoxylate, column Km (mM), reports 6.6.

normalized_value_unit_evidence: Km 6.6 mM is already normalized and matches target 6.6 mM.

raw_value_unit_evidence: Table 5 row YiaE / Glyoxylate, column Km (mM), raw value 6.6 mM.


proof_lines: kcat is 1.99 min(-1) for 17beta-hydroxy-5alpha-androstan-3-one reduction. kcat is 1.79 min(-1) for 5alpha-androstan-3,17-dione reduction. kcat is 2.1 min(-1) for 5alpha-androstane-3alpha,17beta-diol oxydation. kcat is 1.39.1 min(-1) for 3al


proof_lines: pH 7.5, 37°C, recombinant enzyme, with NADPH

proof_lines: pH 7.5, 37°C, recombinant enzyme, with NADH


substrate_name: Hydroxypyruvate

substrate: Hydroxypyruvate


assay_conditions_summary: pH 7.5; cofactor NADH


assay_conditions_summary: cofactor CoA

proof_lines: kcat is 458 min(-1) for DL-3-hydroxybutyryl-CoA (PubMed:28888424). kcat is 706 min(-1) for allopregnanolone (PubMed:28888424).


organism: Hyphomicrobium methylovorum GM2

proof_lines:
native enzyme
purified recombinant enzyme


enzyme_display_name: Aldo-keto reductase family 1 member C1

assay_conditions_summary: pH 7; buffer 100 mM potassium phosphate; cofactor NADPH

column_label: PDF Table 2 row DhtS has AKR1C1 Km=5.2 +/- 0.8 uM; 5.2 uM normalizes to 0.0052 mM

raw_value_unit_evidence: Km raw_value=5.2 raw_unit=uM; S.D.=0.8 uM

row_label: DhtS; enzyme AKR1C1

table_label: Table 2 Kinetic parameters for the reduction of Dht, DhtG, and DhtS catalyzed by AKR1C isoforms

enzyme: Aldo-keto reductase family 1 member C1


enzyme_display_name: UniProt Q9SLN8

organism: Nicotiana tabacum

substrate_name: (R)-pulegone

enzyme: UniProt Q9SLN8

substrate: (R)-pulegone


enzyme_display_name: Aldo-keto reductase family 1 member A1

substrate_name: S-nitroso-glutathione

proof_lines: kcat is 959 min(-1) for S-nitroso-CoA as substrate (PubMed:30538128). kcat is 604 min(-1) for D-glucuronate as substrate (PubMed:30538128). kcat is 306 min(-1) for D,L-glyceraldehyde as substrate (PubMed:30538128). kcat is 948 min(-1) for S

enzyme: Aldo-keto reductase family 1 member A1

substrate: S-nitroso-glutathione


substrate_name: S-nitroso-CoA

proof_lines: kcat is 627 min(-1) for S-nitroso-CoA as substrate (PubMed:25512491). kcat is 471 min(-1) for S-nitroso-glutathione as substrate (PubMed:31649033).

substrate: S-nitroso-CoA


enzyme_display_name: D-mannonate oxidoreductase

organism: Thermotoga maritima (strain ATCC 43589 / DSM 3109 / JCM 10099 / NBRC 100826 / MSB8)

substrate_name: D-mannonate

proof_lines: kcat is 4.2 sec(-1) with D-mannonate as substrate.

enzyme: D-mannonate oxidoreductase

substrate: D-mannonate


enzyme_display_name: UniProt Q48436

organism: Klebsiella pneumoniae

enzyme: UniProt Q48436


organism: Paecilomyces sp. 'thermophila'

proof_lines: pH 7.5, 50°C, recombinant enzyme, with NADPH


organism: Rattus norvegicus

substrate_name: mevaldate

proof_lines: kcat is 3.0 sec(-1) for D,L glyceraldehyde as substrate (PubMed:22820017). kcat is 3.0 sec(-1) for methylglyoxal as substrate (PubMed:22820017). kcat is 3.4 sec(-1) for 3-deoxyglucosone as substrate (PubMed:22820017). kcat is 3.1 sec(-1) fo

substrate: mevaldate


organism: Delftia acidovorans

proof_lines:
with 0.15 mM NADPH
with 0.15 mM NADH


enzyme_display_name: Aldo-keto reductase family 1 member B1

proof_lines: kcat is 15 min(-1) for all-trans-retinal as substrate. kcat is 30 min(-1) for 9-cis-retinal as substrate. kcat is 94 min(-1) for 13-cis-retinal as substrate (PubMed:12732097). kcat is 11 min(-1) for acrolein as substrate. kcat is 31 min(-1)

enzyme: Aldo-keto reductase family 1 member B1


organism: Spinacia oleracea

proof_lines:
cofactor NADPH
cofactor NADH


organism: Streptomyces exfoliatus

substrate_name: cortisone

proof_lines:
NADH
free enzyme
immobilized enzyme

substrate: cortisone


enzyme_display_name: UniProt F8AEA4

enzyme: UniProt F8AEA4


enzyme_display_name: UniProt Q8U3Y2

enzyme: UniProt Q8U3Y2


enzyme_display_name: Hydroxypyruvate reductase

organism: Blautia hydrogenotrophica (strain DSM 10507 / JCM 14656 / S5a33)

substrate_name: hydroxypyruvate

enzyme: Hydroxypyruvate reductase

substrate: hydroxypyruvate


enzyme_display_name: alcohol dehydrogenase [NAD(P)(+)]

organism: Pyrococcus horikoshii

substrate_name: propanal

smiles: CCC=O

enzyme: alcohol dehydrogenase [NAD(P)(+)]

substrate: propanal


substrate_name: Butanal

smiles: CCCC=O

substrate: Butanal


substrate_name: NAD+

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADH

assay_conditions_summary: pH 5.5; 303.15 K; cofactor NADH

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 5.5; 303.15 K; cofactor NADPH

substrate: NADPH


substrate_name: pentanal

smiles: CCCCC=O

substrate: pentanal


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

organism: Drosophila melanogaster

substrate_name: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)

assay_conditions_summary: pH 6.4; cofactor NADH

column_label: Table 3; Drosophila species columns; row Acetoacetyl-CoA/NADH; Km column

normalized_value_unit_evidence: Km=0.0337 mM converted from 33.7 uM

raw_value_unit_evidence: Table 3 Drosophila Acetoacetyl-CoA/NADH Km 33.7 +/- 8 ×10^-6 M

row_label: Acetoacetyl-CoA/NADH

table_label: Table 3

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


substrate_name: (3S)-3-hydroxybutanoyl-CoA (beta-hydroxybutyryl-CoA) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

assay_conditions_summary: pH 9.3; cofactor CoA

column_label: Table 3; Drosophila species columns; row β-Hydroxybutyryl-CoA/NAD+; Km column

normalized_value_unit_evidence: Km=0.101 mM converted from 101 uM

raw_value_unit_evidence: Table 3 Drosophila β-Hydroxybutyryl-CoA/NAD+ Km 101 +/- 8 ×10^-6 M

row_label: β-Hydroxybutyryl-CoA/NAD+


substrate_name: androsterone (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

assay_conditions_summary: pH 9.3; cofactor NAD+

column_label: Table 3; Drosophila species columns; row Androsterone/NAD+; Km column

normalized_value_unit_evidence: Km=0.0373 mM converted from 37.3 uM

raw_value_unit_evidence: Table 3 Drosophila Androsterone/NAD+ Km 37.3 +/- 2 ×10^-6 M

row_label: Androsterone/NAD+


substrate_name: 17beta-hydroxy-5alpha-androstan-3-one (5-alpha-dihydrotestosterone) (in the presence of 0.2 mM NADH, at pH 6.4 and 25 degrees Celsius)

column_label: Table 3; Drosophila species columns; row 5α-Dihydrotestosterone/NADH; Km column

normalized_value_unit_evidence: Km=0.0123 mM converted from 12.3 uM

raw_value_unit_evidence: Table 3 Drosophila 5α-Dihydrotestosterone/NADH Km 12.3 +/- 1 ×10^-6 M


substrate_name: 17-beta-estradiol (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

column_label: Table 3; Drosophila species columns; row 17β-Oestradiol/NAD+; Km column

normalized_value_unit_evidence: Km=0.0111 mM converted from 11.1 uM

raw_value_unit_evidence: Table 3 Drosophila 17β-Oestradiol/NAD+ Km 11.1 +/- 2.3 ×10^-6 M


substrate_name: 5alpha-pregnan-20beta-ol-3-one (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

column_label: Table 3; Drosophila species columns; row 5α-Pregnan-20β-ol-3-one; Km column

normalized_value_unit_evidence: Km=0.009 mM converted from 9 uM

raw_value_unit_evidence: Table 3 Drosophila 5α-Pregnan-20β-ol-3-one Km 9 +/- 2 ×10^-6 M


substrate_name: 3beta,7beta-dihydroxy-5beta-cholan-24-oate (also known as isoursodeoxycholate or 7beta-hydroxyisolithocholate) (in the presence of 1 mM NAD, at pH 9.3 and 25 degrees Celsius)

column_label: Table 3; Drosophila species columns; row Isoursodeoxycholic acid; Km column

normalized_value_unit_evidence: Km=0.003 mM converted from 3 uM

raw_value_unit_evidence: Table 3 Drosophila Isoursodeoxycholic acid Km 3 +/- 0.3 ×10^-6 M

row_label: Isoursodeoxycholic acid


substrate_name: NADH (in the presence of acetoacetyl-CoA, at pH 7.0 and 25 degrees Celsius)

assay_conditions_summary: pH 7; cofactor NADH


substrate_name: NAD (in the presence of aldosterone, at pH 9.3 and 25 degrees Celsius)


enzyme_display_name: Dehydrogenase/reductase SDR family member 9

substrate_name: allopregnanolone

assay_conditions_summary: pH 7.4; cofactor NAD+

column_label: Table II; K_m (uM) block; Allopregnanolone row; raw K_m value 5.0 +/- 0.7 uM.

raw_value_unit_evidence: Table II reports 3-alpha-HSD steroid-substrate K_m for allopregnanolone = 5.0 +/- 0.7 uM.

row_label: Table II steroid-substrate K_m block; Allopregnanolone row

table_label: PMID 11294878, Table II: Kinetic constants for steroid substrates

substrate: allopregnanolone


column_label: Table II; K_m (uM) block; 3-alpha-Androstanediol row; raw K_m value 7.5 +/- 0.4 uM.

raw_value_unit_evidence: Table II reports 3-alpha-HSD steroid-substrate K_m for 3-alpha-androstanediol = 7.5 +/- 0.4 uM.

row_label: Table II steroid-substrate K_m block; 3-alpha-Androstanediol row

enzyme: Dehydrogenase/reductase SDR family member 9


substrate_name: dehydroepiandrosterone

column_label: Table II; K_m (uM) block; Dehydroepiandrosterone row; raw K_m value 14.0 +/- 1.0 uM.

raw_value_unit_evidence: Table II reports 3-alpha-HSD steroid-substrate K_m for dehydroepiandrosterone = 14.0 +/- 1.0 uM.

row_label: Table II steroid-substrate K_m block; Dehydroepiandrosterone row

substrate: dehydroepiandrosterone


substrate_name: androsterone

column_label: Table II; K_m (uM) block; Androsterone row; raw K_m value 24.0 +/- 1.0 uM.

raw_value_unit_evidence: Table II reports 3-alpha-HSD steroid-substrate K_m for androsterone = 24.0 +/- 1.0 uM.

row_label: Table II steroid-substrate K_m block; Androsterone row

substrate: androsterone


substrate_name: dihydrotestosterone

assay_conditions_summary: pH 7.4; cofactor NADH

column_label: Table II; K_m (uM) block; Dihydrotestosterone row; raw K_m value 12.0 +/- 0.4 uM.

raw_value_unit_evidence: Table II reports 3-alpha-HSD steroid-substrate K_m for dihydrotestosterone = 12.0 +/- 0.4 uM.

row_label: Table II steroid-substrate K_m block; Dihydrotestosterone row

substrate: dihydrotestosterone


enzyme_display_name: glycerol dehydrogenase (NADP(+))

organism: Trichoderma reesei

substrate_name: Acetoin

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

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

column_label: Table 1. Specificities and kinetic properties of the histidine-tagged and purified GLD1 and GLD2; GLD1 row Acetoin; kcat 11 s^-1, Km 122 mM, efficacy 90 s^-1 M^-1 from one GLD1 row.

normalized_value_unit_evidence: Printed kcat 11 s^-1 and Km 122 mM are already in catalog units. Current stored quotient is 0.09016393442622951 s^-1*mM^-1; printed efficacy 90 s^-1 M^-1 normalizes to 0.09 s^-1*mM^-1 and agrees at the printed precision.

raw_value_unit_evidence: Table 1, GLD1, Acetoin: Vmax 300 nkat mg^-1 (kcat 11 s^-1); Km 122 mM; enzyme efficacy 90 s^-1 M^-1.

row_label: GLD1 | Acetoin

enzyme: glycerol dehydrogenase (NADP(+))

substrate: Acetoin


substrate_name: D-Glucose

column_label: Table 1. Specificities and kinetic properties of the histidine-tagged and purified GLD1 and GLD2; GLD1 row D-Glucose; kcat 6.8 s^-1, Km 470 mM, efficacy 14 s^-1 M^-1 from one GLD1 row.

normalized_value_unit_evidence: Printed kcat 6.8 s^-1 and Km 470 mM are already in catalog units. Current stored quotient is 0.01446808510638298 s^-1*mM^-1; printed efficacy 14 s^-1 M^-1 normalizes to 0.014 s^-1*mM^-1 and agrees at the printed precision.

raw_value_unit_evidence: Table 1, GLD1, D-Glucose: Vmax 190 nkat mg^-1 (kcat 6.8 s^-1); Km 470 mM; enzyme efficacy 14 s^-1 M^-1.

row_label: GLD1 | D-Glucose

substrate: D-Glucose


substrate_name: Dihydroxyacetone

smiles: O=C(CO)CO

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; Table 1 row GLD1 / Dihydroxyacetone; column(s) Vmax kcat value in parentheses (s^-1); Km (mM); kcat/Km from Table 1 kcat and Km cells

normalized_value_unit_evidence: kcat normalized_value=1.4 normalized_unit=s^-1; Km normalized_value=5.8 normalized_unit=mM; kcat/Km normalized_value=0.24137931034482757 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=1.4 raw_unit=s^-1; Km raw_value=5.8 raw_unit=mM; kcat/Km raw_value=1.4/5.8 raw_unit=s^-1*mM^-1

row_label: GLD1 / Dihydroxyacetone

substrate: Dihydroxyacetone


substrate_name: Dimethylglyoxal

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

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; Table 1 row GLD1 / Diacetyl; dimethylglyoxal is the source synonym; column(s) Vmax kcat value in parentheses (s^-1); Km (mM); kcat/Km from Table 1 kcat and Km cells

normalized_value_unit_evidence: kcat normalized_value=12 normalized_unit=s^-1; Km normalized_value=0.9 normalized_unit=mM; kcat/Km normalized_value=13.333333333333332 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=12 raw_unit=s^-1; Km raw_value=0.9 raw_unit=mM; kcat/Km raw_value=12/0.9 raw_unit=s^-1*mM^-1

row_label: GLD1 / Diacetyl (dimethylglyoxal synonym)

substrate: Dimethylglyoxal


substrate_name: D-Ribose

column_label: Table 1. Specificities and kinetic properties of the histidine-tagged and purified GLD1 and GLD2; GLD1 row D-Ribose; kcat 5.8 s^-1, Km 122 mM, efficacy 48 s^-1 M^-1 from one GLD1 row.

normalized_value_unit_evidence: Printed kcat 5.8 s^-1 and Km 122 mM are already in catalog units. Current stored quotient is 0.047540983606557376 s^-1*mM^-1; printed efficacy 48 s^-1 M^-1 normalizes to 0.048 s^-1*mM^-1 and agrees at the printed precision.

raw_value_unit_evidence: Table 1, GLD1, D-Ribose: Vmax 160 nkat mg^-1 (kcat 5.8 s^-1); Km 122 mM; enzyme efficacy 48 s^-1 M^-1.

row_label: GLD1 | D-Ribose

substrate: D-Ribose


substrate_name: D-Xylose

column_label: Table 1. Specificities and kinetic properties of the histidine-tagged and purified GLD1 and GLD2; GLD1 row D-Xylose; kcat 16 s^-1, Km 334 mM, efficacy 48 s^-1 M^-1 from one GLD1 row.

normalized_value_unit_evidence: Printed kcat 16 s^-1 and Km 334 mM are already in catalog units. Current stored quotient is 0.04790419161676647 s^-1*mM^-1; printed efficacy 48 s^-1 M^-1 normalizes to 0.048 s^-1*mM^-1 and agrees at the printed precision.

raw_value_unit_evidence: Table 1, GLD1, D-Xylose: Vmax 450 nkat mg^-1 (kcat 16 s^-1); Km 334 mM; enzyme efficacy 48 s^-1 M^-1.

row_label: GLD1 | D-Xylose

substrate: D-Xylose


substrate_name: Glyoxal

smiles: O=CC=O

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; Table 1 row GLD1 / Glyoxal; column(s) Vmax kcat value in parentheses (s^-1); Km (mM); kcat/Km from Table 1 kcat and Km cells

normalized_value_unit_evidence: kcat normalized_value=14 normalized_unit=s^-1; Km normalized_value=2.4 normalized_unit=mM; kcat/Km normalized_value=5.833333333333334 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=14 raw_unit=s^-1; Km raw_value=2.4 raw_unit=mM; kcat/Km raw_value=14/2.4 raw_unit=s^-1*mM^-1

row_label: GLD1 / Glyoxal

substrate: Glyoxal


substrate_name: L-Glyceraldehyde

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD1 / L-Glyceraldehyde

normalized_value_unit_evidence: Per-metric normalized values and units are preserved in paper_metric_evidence.

raw_value_unit_evidence: Per-metric raw values and units are preserved in paper_metric_evidence; captured_primary_segment preserves the exact source transcription.

row_label: GLD1 / L-Glyceraldehyde

substrate: L-Glyceraldehyde


substrate_name: NADPH


substrate_name: methylglyoxal

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; Table 1 row GLD1 / Methylglyoxal; column(s) Vmax kcat value in parentheses (s^-1); Km (mM); kcat/Km from Table 1 kcat and Km cells

normalized_value_unit_evidence: kcat normalized_value=15 normalized_unit=s^-1; Km normalized_value=0.4 normalized_unit=mM; kcat/Km normalized_value=37.5 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=15 raw_unit=s^-1; Km raw_value=0.4 raw_unit=mM; kcat/Km raw_value=15/0.4 raw_unit=s^-1*mM^-1

row_label: GLD1 / Methylglyoxal

substrate: methylglyoxal


organism: Clostridium beijerinckii

smiles: CCC(C)O


substrate_name: isopropanol

smiles: CC(C)O

proof_lines:
2-propanol-producing C. beijerinckii
NADP(H) dependent
2-propanol

substrate: isopropanol


smiles: CCCC(C)O

proof_lines:
aldehydes
2-ketones
NADP(H) dependent


substrate_name: acetone

smiles: CC(=O)C

proof_lines:
acetone
butyraldehyde
common active site

substrate: acetone


smiles: CCC(=O)C

proof_lines:
2-ketones
aldehydes
NADP(H) dependent


assay_conditions_summary: cofactor NADPH

proof_lines:
NADP(H) dependent
low level of NAD(+)-linked activity

substrate: NADPH


enzyme_display_name: Retinol dehydrogenase 16

assay_conditions_summary: cofactor NAD+

column_label: Table I row Androstane-diol has Km 0.22 +/- 0.06 uM and Vmax 6.9 +/- 0.5 nmol/min/mg.

raw_value_unit_evidence: Table I reports Androstane-diol Km = 0.22 +/- 0.06 uM.

row_label: Androstane-diol

table_label: JBC 273(31) Table I, substrate kinetics of recombinant human RoDH-4

enzyme: Retinol dehydrogenase 16


assay_conditions_summary: pH 7.3; cofactor NADH

column_label: Table I; K_m (uM) block; Dihydrotestosterone row; raw Km value 0.80 uM.

raw_value_unit_evidence: Table I reports RoDH-4 steroid-substrate K_m for dihydrotestosterone = 0.80 uM.

row_label: RoDH-4 steroid substrate K_m block; Dihydrotestosterone row

table_label: PMID 9677409, Table I: Kinetic constants of RoDH-4 for steroid substrates


substrate_name: NAD

assay_conditions_summary: pH 7.3; cofactor NAD+

column_label: Table II; K_m (uM) block; NAD+ row; raw Km value 0.13 uM.

raw_value_unit_evidence: Table II reports RoDH-4 cofactor K_m for NAD+ = 0.13 uM.

row_label: RoDH-4 cofactor K_m block; NAD+ row

table_label: PMID 9677409, Table II: Apparent K_m values of RoDH-4 for cofactors

substrate: NAD


substrate_name: NADP

column_label: Table II; K_m (uM) block; NADP+ row; raw Km value 190 uM.

raw_value_unit_evidence: Table II reports RoDH-4 cofactor K_m for NADP+ = 190 uM.

row_label: RoDH-4 cofactor K_m block; NADP+ row

substrate: NADP


substrate_name: all-trans-retinol

substrate: all-trans-retinol


enzyme_display_name: Alcohol dehydrogenase 1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

smiles: CCCCCCCO

column_label: Table IV; K_m (mM) block; Sc I row; Heptyl column; raw Km value 7.8 mM.

raw_value_unit_evidence: Table IV reports Sc I K_m for Heptyl alcohol = 7.8 mM.

row_label: Sc I (wild-type Saccharomyces cerevisiae alcohol dehydrogenase I / P00330); K_m block; Heptyl column

table_label: PMID 8463307, Table IV: Kinetic constants for primary alcohols

enzyme: Alcohol dehydrogenase 1


smiles: CCCCCCCCO

column_label: Table IV; K_m (mM) block; Sc I row; Octyl column; raw Km value 5.3 mM.

raw_value_unit_evidence: Table IV reports Sc I K_m for Octyl alcohol = 5.3 mM.

row_label: Sc I (wild-type Saccharomyces cerevisiae alcohol dehydrogenase I / P00330); K_m block; Octyl column


smiles: CCCCCCCCCO

column_label: Table IV; K_m (mM) block; Sc I row; Nonyl column; raw Km value 1.7 mM.

raw_value_unit_evidence: Table IV reports Sc I K_m for Nonyl alcohol = 1.7 mM.

row_label: Sc I (wild-type Saccharomyces cerevisiae alcohol dehydrogenase I / P00330); K_m block; Nonyl column


substrate_name: isobutanol

smiles: CC(C)CO

column_label: Table V; K_m (mM) block; Sc I row; 2-Methyl-1-propanol column; raw Km value 25 mM.

raw_value_unit_evidence: Table V reports Sc I K_m for 2-methyl-1-propanol = 25 mM; 2-methyl-1-propanol is isobutanol.

row_label: Sc I (wild-type Saccharomyces cerevisiae alcohol dehydrogenase I / P00330); K_m block; 2-Methyl-1-propanol column

table_label: PMID 8463307, Table V: Kinetic constants for secondary and branched alcohols

substrate: isobutanol


organism: Thermococcus sibiricus

column_label: Table 2 row 2-Propanol gives Km 168 and kcat 0.53.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 0.53 s^-1; Km 168.0 mM; kcat/Km 0.0031547619047619046 s^-1 mM^-1. kcat/Km is derived from the same Table 2 2-Propanol row because the paper table reports kcat and Km but not a kcat/Km column.

table_label: Table 2. Apparent Km and Vmax values for TsAdh319


substrate_name: NADP+

assay_conditions_summary: pH 10.5; 333.15 K; cofactor NADP+

substrate: NADP+


assay_conditions_summary: pH 7.5; 333.15 K; cofactor NADPH

column_label: Table 2 row NADPH gives Km 0.020 and kcat 1.51.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 1.51 s^-1; Km 0.02 mM; kcat/Km 75.5 s^-1 mM^-1. kcat/Km is derived from the same Table 2 NADPH row because the paper table reports kcat and Km but not a kcat/Km column.

row_label: NADPH


substrate_name: Pyruvaldehyde

smiles: CC(=O)C=O

column_label: Table 2 row Pyruvaldehyde gives Km 17.75 and kcat 2.04.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 2.04 s^-1; Km 17.75 mM; kcat/Km 0.11492957746478873 s^-1 mM^-1. kcat/Km is derived from the same Table 2 Pyruvaldehyde row because the paper table reports kcat and Km but not a kcat/Km column.

row_label: Pyruvaldehyde

substrate: Pyruvaldehyde


column_label: Table 2 row D-Xylose gives Km 54.4 and kcat 0.70.

normalized_value_unit_evidence: Paper-normalized metrics: kcat 0.7 s^-1; Km 54.4 mM; kcat/Km 0.012867647058823529 s^-1 mM^-1. kcat/Km is derived from the same Table 2 D-Xylose row because the paper table reports kcat and Km but not a kcat/Km column.

row_label: D-Xylose


enzyme_display_name: (S,S)-butanediol dehydrogenase

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F212S to reconstruct the assayed variant sequence.

enzyme: (S,S)-butanediol dehydrogenase


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F212W to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature F212Y to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N146Q with inferred residue-numbering offset -10 to reconstruct the assayed variant sequence.


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Mus musculus

assay_conditions_summary: pH 9; buffer 0.25 ml CHES; cofactor NAD+

column_label: Official OUP Table 5; row 3alpha-Adiolb; column K0.5 (uM); raw value 1.4; normalized km 0.0014 mM

normalized_value_unit_evidence: K0.5=0.0014 mM for km field; raw 1.4 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row 3alpha-Adiolb; column K0.5 (uM); raw cell 1.4 uM.


substrate_name: androsterone

column_label: Official OUP Table 5; row Androsterone; column K0.5 (uM); raw value 1.3; normalized km 0.0013 mM

normalized_value_unit_evidence: K0.5=0.0013 mM for km field; raw 1.3 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row Androsterone; column K0.5 (uM); raw cell 1.3 uM.

row_label: Androsterone

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6

substrate: androsterone


column_label: Official OUP Table 5; row All-trans-retinol; column K0.5 (uM); raw value 3.2; normalized km 0.0032 mM

normalized_value_unit_evidence: K0.5=0.0032 mM for km field; raw 3.2 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row All-trans-retinol; column K0.5 (uM); raw cell 3.2 uM.

row_label: All-trans-retinol


substrate_name: estradiol

column_label: Official OUP Table 5; row Estradiol; column K0.5 (uM); raw value 1.5; normalized km 0.0015 mM

normalized_value_unit_evidence: K0.5=0.0015 mM for km field; raw 1.5 uM normalized by uM-to-mM conversion.

raw_value_unit_evidence: Table 5. Kinetic constants of 17betaHSD9 activity with steroid and retinoid substrates. row Estradiol; column K0.5 (uM); raw cell 1.5 uM.

row_label: Estradiol

substrate: estradiol


enzyme_display_name: Aldo-keto reductase family 1 member C3

organism: Bos taurus

substrate_name: prostaglandin D2

column_label: Table I row PGD2 gives PGFS Km 100 uM.

normalized_value_unit_evidence: Km=0.1 mM

raw_value_unit_evidence: Km=100 uM in PGFS Km column

row_label: PGFS / PGD2

table_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS

enzyme: Aldo-keto reductase family 1 member C3

substrate: prostaglandin D2


column_label: Table I row 9,10-Phenanthrenequinone gives PGFS Km 0.13 uM.

raw_value_unit_evidence: Km=0.13 uM in PGFS Km column

row_label: PGFS / 9,10-Phenanthrenequinone


substrate_name: menadione

column_label: Table I row Menadione gives PGFS Km 13 uM.

raw_value_unit_evidence: Km=13 uM in PGFS Km column

row_label: PGFS / Menadione

substrate: menadione


column_label: Table I row 4-Nitrobenzaldehyde gives PGFS Km 8.3 uM.

raw_value_unit_evidence: Km=8.3 uM in PGFS Km column

row_label: PGFS / 4-Nitrobenzaldehyde


enzyme_display_name: 3-hydroxypropionate dehydrogenase

organism: Candida albicans

smiles: O=C(O)CCO

column_label: Table 3 row 3-Hydroxy-propionate; kcat column = 30.97 s^-1; Km column = 5.37 mM; Keff column = 5.77 x 10^3 M^-1 s^-1

enzyme: 3-hydroxypropionate dehydrogenase


substrate_name: L-serine

column_label: Table 3 row l-Serine; kcat column = 9.41 s^-1; Km column = 46.7 mM; Keff column = 2.02 x 10^2 M^-1 s^-1

row_label: l-Serine

substrate: L-serine


column_label: Table 3 row (R)-beta-Hydroxyisobutyrate; kcat column = 1.31 s^-1; Km column = 0.58 mM; Keff column = 2.26 x 10^3 M^-1 s^-1

row_label: (R)-beta-Hydroxyisobutyrate


column_label: Table 3 row (S)-beta-Hydroxyisobutyrate; kcat column = 2.48 s^-1; Km column = 0.13 mM; Keff column = 1.91 x 10^4 M^-1 s^-1

row_label: (S)-beta-Hydroxyisobutyrate


smiles: CCCO

proof_lines:
alcohol dehydrogenase I
butanol
pentanol


smiles: CCCCO


smiles: CCCCCO


smiles: CCCCCCO


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: ethanol

substrate: ethanol


substrate_name: acetaldehyde

substrate: acetaldehyde


substrate_name: NADH

substrate: NADH


enzyme_display_name: Carbonyl reductase [NADPH] 1

organism: Homo sapiens

substrate_name: prostaglandin E1

enzyme: Carbonyl reductase [NADPH] 1

substrate: prostaglandin E1


substrate_name: phenylglyoxal

substrate: phenylglyoxal


enzyme_display_name: alcohol dehydrogenase

enzyme: alcohol dehydrogenase


smiles: CCO


smiles: CC=O


organism: Vitis vinifera

substrate_name: 2-keto-L-gulonate (in presence of NADPH)

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Table 2 columns Substrate, Coenzyme, Km (mM), Vmax (units/mg), Kcat (s^-1); row 2KLG / NADPH has Km 0.700 mM

raw_value_unit_evidence: Table 2 row 2KLG with coenzyme NADPH reports Km 0.700 mM, Vmax 7.544 units/mg, and Kcat 4.178 s^-1

row_label: 2KLG / NADPH

table_label: Table 2


substrate_name: hydroxypyruvate (in presence of NADPH)

column_label: Table 2 columns Substrate, Coenzyme, Km (mM), Vmax (units/mg), Kcat (s^-1); row Hydroxypyruvate / NADPH has Km 0.096 mM

raw_value_unit_evidence: Table 2 row Hydroxypyruvate with coenzyme NADPH reports Km 0.096 mM, Vmax 6.295 units/mg, and Kcat 6.973 s^-1; the NADH row reports no activity

row_label: Hydroxypyruvate / NADPH

substrate: hydroxypyruvate (in presence of NADPH)


substrate_name: glyoxylate (in presence of NADPH)

column_label: Table 2 columns Substrate, Coenzyme, Km (mM), Vmax (units/mg), Kcat (s^-1); row d-Glyoxylate / NADPH has Km 0.044 mM

raw_value_unit_evidence: Table 2 row d-Glyoxylate with coenzyme NADPH reports Km 0.044 mM, Vmax 13.820 units/mg, and Kcat 38.26 s^-1

row_label: d-Glyoxylate / NADPH

substrate: glyoxylate (in presence of NADPH)


substrate_name: pyruvate (in presence of NADPH)

substrate: pyruvate (in presence of NADPH)


enzyme_display_name: hydroxypyruvate reductase

organism: Methylococcus capsulatus

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

proof_lines:
hydroxypyruvate reductase
Methylococcus capsulatus
3-hydroxypyruvate

enzyme: hydroxypyruvate reductase


substrate_name: glyoxylate

smiles: O=CC(=O)O

proof_lines:
hydroxypyruvate reductase
Methylococcus capsulatus
glyoxylate

substrate: glyoxylate


assay_conditions_summary: pH 7; 310.15 K; cofactor NADH

proof_lines:
hydroxypyruvate reductase
Methylococcus capsulatus
NADH


substrate_name: NADPH

assay_conditions_summary: pH 7; 310.15 K; cofactor NADPH

proof_lines:
hydroxypyruvate reductase
Methylococcus capsulatus
NADPH

substrate: NADPH


organism: Acetivibrio thermocellus

assay_conditions_summary: pH 7; 328.15 K; cofactor NADH

proof_lines: NADH preferred for ALDH and ADH activities


assay_conditions_summary: pH 7; 328.15 K; cofactor NADPH


column_label: Table V has substrate columns Ethanol, Propanol, Butanol, Pentanol, Hexanol; the Isozyme I K_m row gives Propanol = 27 mM.

raw_value_unit_evidence: Km raw_value=27 raw_unit=mM

row_label: Isozyme I; K_m row

table_label: Table V, Kinetic constants for different alcohols


column_label: Table V has substrate columns Ethanol, Propanol, Butanol, Pentanol, Hexanol; the Isozyme I K_m row gives Butanol = 55 mM.

raw_value_unit_evidence: Km raw_value=55 raw_unit=mM


column_label: Table V has substrate columns Ethanol, Propanol, Butanol, Pentanol, Hexanol; the Isozyme I K_m row gives Pentanol = 37 mM.

raw_value_unit_evidence: Km raw_value=37 raw_unit=mM


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

column_label: Table 3 reports Menadione row, CBR1 V88 Km column = 42 +/- 23 uM (0.042 mM), not the queued 0.022 mM; CBR1 I88 is 55 +/- 21 uM (0.055 mM).

normalized_value_unit_evidence: Expected Km=0.022 mM, but primary Table 3 gives CBR1 V88 Km=0.042 mM; not accepted.

row_label: Menadione row / CBR1 V88 Km column

table_label: Table 3 / CBR1 V88 and CBR1 I88 kinetic constants for prototypical substrates


substrate_name: prostaglandin E2

column_label: Table 3 reports PGE2 row, CBR1 V88 Km column = 309 +/- 94 uM; normalized Km = 0.309 mM.

normalized_value_unit_evidence: Km=0.309 mM after converting 309 +/- 94 uM from uM to mM.

row_label: PGE2 row / CBR1 V88 Km column

substrate: prostaglandin E2


substrate_name: daunorubicin

column_label: Table 3 reports Daunorubicin row, CBR1 V88 Km column = 173 +/- 26 uM; normalized Km = 0.173 mM.

normalized_value_unit_evidence: Km=0.173 mM after converting 173 +/- 26 uM from uM to mM.

row_label: Daunorubicin row / CBR1 V88 Km column

substrate: daunorubicin


enzyme_display_name: malate dehydrogenase (NADP(+))

organism: Zea mays

substrate_name: L-Malate

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH

column_label: Table 3, row Malate, columns kcat (s^-1) and Km (mM) for corn or spinach as applicable; kcat/Km value is computed from those exact same-row cells.

raw_value_unit_evidence: Table 3 row Malate: kcat=2.9 s^-1; Km=75 mM; kcat/Km calculated from Table 3 cells 2.9 s^-1 / 75 mM.

row_label: Malate

enzyme: malate dehydrogenase (NADP(+))

substrate: L-Malate


substrate_name: NADP+

assay_conditions_summary: pH 8; 303.15 K; cofactor NADP+

column_label: Table 3, row NADP, columns kcat (s^-1) and Km (mM) for corn or spinach as applicable; kcat/Km value is computed from those exact same-row cells.

raw_value_unit_evidence: Table 3 row NADP: kcat=2.9 s^-1; Km=1.26 mM; kcat/Km calculated from Table 3 cells 2.9 s^-1 / 1.26 mM.

row_label: NADP

substrate: NADP+


column_label: Table 3, row NADPH, columns kcat (s^-1) and Km (mM) for corn or spinach as applicable; kcat/Km value is computed from those exact same-row cells.

raw_value_unit_evidence: Table 3 row NADPH: kcat=955 s^-1; Km=0.195 mM; kcat/Km calculated from Table 3 cells 955 s^-1 / 0.195 mM.

row_label: NADPH


substrate_name: oxaloacetate

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

column_label: Table 3, row Oxaloacetate, columns kcat (s^-1) and Km (mM) for corn or spinach as applicable; kcat/Km value is computed from those exact same-row cells.

raw_value_unit_evidence: Table 3 row Oxaloacetate: kcat=955 s^-1; Km=0.214 mM; kcat/Km calculated from Table 3 cells 955 s^-1 / 0.214 mM.

row_label: Oxaloacetate

substrate: oxaloacetate


enzyme_display_name: Tartrate dehydrogenase/decarboxylase

organism: Pseudomonas putida

substrate_name: D-malate

proof_lines:
D-malate
tartrate dehydrogenase
oxidative decarboxylation

enzyme: Tartrate dehydrogenase/decarboxylase

substrate: D-malate


substrate_name: (+)-tartrate

proof_lines:
(+)-tartrate
tartrate dehydrogenase
oxidation

substrate: (+)-tartrate


substrate_name: NAD(+) (for D-malate oxidation)

proof_lines:
NAD(+)-dependent
D-malate reaction
tartrate dehydrogenase

substrate: NAD(+) (for D-malate oxidation)


substrate_name: butanal

smiles: CCCC=O

assay_conditions_summary: cofactor NADH

substrate: butanal


smiles: CC(C)O


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


organism: Rattus norvegicus

substrate_name: menadione

proof_lines:
rat testis carbonyl reductase
same substrate specificity
susceptibility to inhibitors

substrate: menadione


enzyme_display_name: 5-keto-D-gluconate 5-reductase

organism: Escherichia coli (strain K12)

column_label: PMC Results prose for IdnO reports apparent Km values: 2 mM for gluconate and 0.5 mM for 5KG.

normalized_value_unit_evidence: Km normalized_value=0.5 mM.

raw_value_unit_evidence: IdnO apparent Km for 5KG is reported as 0.5 mM.

row_label: IdnO crude extract / 5-keto-D-gluconate (5KG)

table_label: PMC107343 Results prose, IdnO characterization paragraph

enzyme: 5-keto-D-gluconate 5-reductase


substrate_name: D-gluconate

normalized_value_unit_evidence: Km normalized_value=2.0 mM.

raw_value_unit_evidence: IdnO apparent Km for gluconate is reported as 2 mM.

row_label: IdnO crude extract / gluconate

substrate: D-gluconate


enzyme_display_name: glyoxylate reductase (NADP+)

organism: Saccharomyces cerevisiae

substrate_name: NADH

column_label: Abstract reports Michaelis constants for glyoxylate, hydroxypyruvate, NADPH, and NADH as 16 mM, 1.4 mM, 5.7 microM, and 0.43 mM, respectively.

raw_value_unit_evidence: Km raw_value=0.43 mM raw_unit=mM

row_label: Baker yeast glyoxylate reductase II / NADH

table_label: PubMed XML abstract PMID 6993451

enzyme: glyoxylate reductase (NADP+)

substrate: NADH


substrate_name: Hydroxypyruvate

raw_value_unit_evidence: Km raw_value=1.4 mM raw_unit=mM

row_label: Baker yeast glyoxylate reductase II / hydroxypyruvate

substrate: Hydroxypyruvate


assay_conditions_summary: pH 7.05; cofactor NADH

column_label: Scanned page 264, Table 2: row Butyraldehyde; column phi2'/phi0' (mM), defined as the Michaelis constant for the substrate; value 27.5 mM.

raw_value_unit_evidence: Table 2 substrate Michaelis constant phi2'/phi0' for butyraldehyde = 27.5 mM.

row_label: Butyraldehyde

table_label: Table 2. Kinetic coefficients for the reduction of aldehydes by NADH with yeast alcohol dehydrogenase at 25 degrees Celsius and pH 7.05


assay_conditions_summary: pH 7.05; cofactor NAD+

column_label: Scanned page 263, Table 1: row Propan-2-ol; column phi2/phi0 (mM), defined as the Michaelis constant for the substrate; value 256 mM.

raw_value_unit_evidence: Table 1 substrate Michaelis constant phi2/phi0 for propan-2-ol = 256 mM.

table_label: Table 1. Kinetic coefficients for the oxidation of alcohols by NAD+ with yeast alcohol dehydrogenase at 25 degrees Celsius and pH 7.05


organism: Delftia acidovorans

assay_conditions_summary: cofactor NADPH


organism: Spinacia oleracea

raw_value_unit_evidence: Table 3 row Malate: kcat=6.7 s^-1; Km=18 mM; kcat/Km calculated from Table 3 cells 6.7 s^-1 / 18 mM.


raw_value_unit_evidence: Table 3 row NADP: kcat=6 s^-1; Km=2 mM; kcat/Km calculated from Table 3 cells 6 s^-1 / 2 mM.


assay_conditions_summary: pH 6.5; cofactor NADPH

column_label: Abstract reports Km values for NADPH and NADH as 3 and 150 microM, respectively.

raw_value_unit_evidence: Km raw_value=3 microM raw_unit=microM

row_label: Spinach glyoxylate reductase / NADPH

table_label: PubMed XML abstract PMID 3548703


raw_value_unit_evidence: Km raw_value=150 microM raw_unit=microM

row_label: Spinach glyoxylate reductase / NADH


organism: Sorghum bicolor

assay_conditions_summary: pH 7.9; 303.15 K; cofactor NADPH

column_label: Table 1, WT MDH column: Km NADPH, Km OAA, kcat, and dimensionally distinct kcat/(Km OAA x Km NADP) cells.

normalized_value_unit_evidence: Km NADPH 50 uM = 0.05 mM; kcat 600 s^-1; typed same-measurement quotient kcat/Km NADPH = 12000 s^-1 mM^-1. The M^-2 s^-1 two-substrate cell is not exported as canonical kcat/Km.

raw_value_unit_evidence: Table 1 WT MDH: Km NADPH 50 uM. Table 1 WT MDH: kcat 600 s^-1. Distinct two-substrate cell: kcat/(Km OAA x Km NADP) 40000x10^7 M^-2 s^-1.

row_label: WT MDH

table_label: Table 1. Kinetic parameters of the WT, Delta N and D101N NADP-MDH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D101N with inferred residue-numbering offset +14 to reconstruct the assayed variant sequence.


organism: Streptomyces exfoliatus


enzyme_display_name: glyoxylate reductase (NADP(+))

organism: Arabidopsis thaliana

substrate_name: Glyoxylate

enzyme: glyoxylate reductase (NADP(+))

substrate: Glyoxylate


assay_conditions_summary: pH 7.6; 303.15 K; cofactor NADPH


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

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

assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: Primary PMC HTML Table 3 row IPMDH_Mj, beta-Isopropylmalate group, K_m (uM) column = 24 +/- 3.

normalized_value_unit_evidence: Normalized paper Km: 24 uM = 0.024 mM, matching export Km 0.024 mM.

raw_value_unit_evidence: Table 3 row IPMDH_Mj reports beta-Isopropylmalate K_m 24 +/- 3 uM and kcat/Km 8.8 x 10^4 M^-1 s^-1.

row_label: IPMDH_Mj row; beta-Isopropylmalate K_m column

table_label: Table 3. Kinetic parameters for IPMDH homologs


column_label: Primary PMC HTML Table 3 row IPMDH_Mj, d-Malate group, K_m (uM) column = 410 +/- 40.

normalized_value_unit_evidence: Normalized paper Km: 410 uM = 0.410 mM, matching export Km 0.41000000000000003 mM.

raw_value_unit_evidence: Table 3 row IPMDH_Mj reports d-Malate K_m 410 +/- 40 uM and kcat/Km 1.4 x 10^4 M^-1 s^-1.

row_label: IPMDH_Mj row; d-Malate K_m column


assay_conditions_summary: pH 7.3; cofactor NAD+

column_label: Table I row Androsterone, column Km (microM), reports 0.14 +/- 0.02.

raw_value_unit_evidence: Androsterone Km 0.14 +/- 0.02 microM

row_label: Androsterone

table_label: Table I. Kinetic constants of RoDH-4 for steroid substrates, PMID 9677409


organism: Mycobacterium sp.

substrate_name: (R,S)-acetoin

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

assay_conditions_summary: pH 7; 303.15 K; cofactor NADH

proof_lines: Identification and characterization of a mycobacterial NAD+-dependent alcohol dehydrogenase with superior reduction of diacetyl to (S)-acetoin

substrate: (R,S)-acetoin


enzyme_display_name: Aldo-keto reductase family 1 member A1

organism: Mus musculus

substrate_name: D-glucuronate

enzyme: Aldo-keto reductase family 1 member A1

substrate: D-glucuronate


organism: Escherichia coli

assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: Table 5 row YcdW / Glyoxylate, primary kcat/Km column: 1.2 x 10^5 s^-1 M^-1; the explicit metric normalizes to 120 s^-1 mM^-1 rather than the current 117.66666666666666 s^-1 mM^-1.

raw_value_unit_evidence: Table 5 row YcdW / Glyoxylate: Km 0.6 mM; kcat 70.6 s^-1; kcat/Km 1.2 x 10^5 s^-1 M^-1.

row_label: YcdW | Glyoxylate

table_label: Table 5. Kinetic parameters of YcdW and YiaE enzymes


organism: Homo sapiens

substrate_name: S-nitrosoglutathione

assay_conditions_summary: pH 6.8; cofactor NADPH

column_label: Table 2 row hCBR1 / GSNO, column Km (uM), gives 30.1 +/- 3.6

raw_value_unit_evidence: Km (uM) = 30.1 +/- 3.6 uM; article abstract/discussion round the same hCBR1 GSNO value to Km = 30 uM

row_label: hCBR1 / GSNO

substrate: S-nitrosoglutathione


assay_conditions_summary: pH 8; cofactor NAD+

column_label: Table II row Androsterone has Activity 3alpha-HSD, Product androstanedione, Km 0.1 uM, Rate 6, V/Km 60.

normalized_value_unit_evidence: 0.1 uM = 0.0001 mM; CatLog row stores 0.0002 mM.

raw_value_unit_evidence: Table II reports Androsterone Km = 0.1 uM.

row_label: Androsterone / 3alpha-HSD / androstanedione

table_label: JBC 272(52) Table II, steroid substrate kinetics for recombinant mouse CRAD


organism: Pyrococcus furiosus

assay_conditions_summary: pH 8; 323.15 K; cofactor NADH


proof_lines: YiaE hydroxypyruvate kcat/Km


organism: Pyrococcus yayanosii

column_label: Table 1 columns under PyaGRHPR NADH are kcat/KM (s^-1/mM), KM (uM), kcat (s^-1), and KI (uM); hydroxypyruvate row cells are 60 +/- 25, 410 +/- 110, 25 +/- 5, 760 +/- 200.

normalized_value_unit_evidence: KM 410 uM = 0.41 mM; kcat 25 s^-1; printed kcat/KM 60 s^-1/mM. Expected computed ratio 60.97560975609756 s^-1/mM is within table precision/rounding.

raw_value_unit_evidence: Table 1 PyaGRHPR hydroxypyruvate NADH: kcat/KM 60 +/- 25 s^-1/mM, KM 410 +/- 110 uM, kcat 25 +/- 5 s^-1, KI 760 +/- 200 uM.

row_label: PyaGRHPR / Hydroxypyruvate / NADH

table_label: Table 1, Kinetic parameters of PfuGRHPR, PhoGRHPR and PyaGRHPR


enzyme_display_name: L-2,3-butanediol dehydrogenase

organism: Corynebacterium glutamicum

substrate_name: (S)-acetoin (at pH 6.0)

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

assay_conditions_summary: pH 6

column_label: PMID 11577733, Table 2, row AC, column Br. saccharolyticum C-1012 / L-BDH: 0.44 mM; the preceding kinetic paragraph explicitly binds L-AC to pH 6.0.

normalized_value_unit_evidence: Km=0.44 mM for (S)-acetoin at pH 6.0.

raw_value_unit_evidence: The page-1877 kinetic paragraph assigns Km 0.44 mM to L-AC at pH 6.0; Table 2 row AC in the Br. saccharolyticum C-1012 L-BDH column independently prints 0.44 mM.

row_label: L-AC / AC

table_label: Kinetic-parameter paragraph (PDF page 2 / article page 1877) and Table 2, Comparison of BDHs Isolated from Several Sources (PDF page 3 / article page 1878)

enzyme: L-2,3-butanediol dehydrogenase

substrate: (S)-acetoin (at pH 6.0)


enzyme_display_name: malate dehydrogenase (NADP+)

organism: Sorghum sp.

substrate_name: NADPH

proof_lines: mutant enzyme C207A/E387Q, oxidized form

enzyme: malate dehydrogenase (NADP+)

substrate: NADPH


proof_lines: mutant enzyme C29S/C207A/E387Q, oxidized enzyme form

proof_lines: mutant enzyme C29S/C207A/E387Q, reduced form and mutant enzyme C29S/C207A/DELTAEV, reduced form


proof_lines: mutant enzyme C29S/C207A/DELTAEV, oxidized form


proof_lines: mutant enzyme C207A/DELTAEV, oxidized form


proof_lines: mutant enzyme C29S/DELTAEV, oxidized form

proof_lines: mutant enzyme C29S/DELTAEV, reduced form


proof_lines: mutant enzyme C207A/DELTAEV, reduced form


proof_lines:
mutant enzyme C29S/E387Q, reduced form
mutant enzyme C29S/E387Q, oxidized form


proof_lines: mutant enzyme C207A/DELTAEV, and mutant enzyme C29S/C207S/DELTAEV, reduced forms


proof_lines: mutant enzyme C29S/C207A/E387Q, reduced form

proof_lines: mutant enzyme C29S/C207A/E387Q, oxidized form


substrate_name: glyoxylate

proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170E

substrate: glyoxylate


proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant K170R


proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant N174A


assay_conditions_summary: pH 7.8; cofactor NADPH


proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant F231A


proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant D239A


proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant T95A


proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant wild-type enzyme

proof_lines: pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a double beam spectrophotometer


proof_lines: pH 7.8, temperature not specified in the publication, recombinant wild-type enzyme, value determined with the use of a microplate reader


proof_lines: pH 7.8, temperature not specified in the publication, value determined with the use of a microplate reader, recombinant mutant S121A


mutation_signature: recombinant truncated enzyme

mutation_type: truncation

proof_lines: pH 7.8, temperature not specified in the publication, recombinant truncated enzyme


organism: Mycobacterium tuberculosis

substrate_name: progesterone

assay_conditions_summary: pH 6; 303.15 K; cofactor NADH

substrate: progesterone


assay_conditions_summary: pH 6; 303.15 K; cofactor NAD+


substrate_name: androsterone

substrate: androsterone


proof_lines: pH 6.0, 30°C, reaction with NADH, mutant enzyme I6T/V47M/T69K


proof_lines: pH 6.0, 30°C, reaction with NAD+, mutant enzyme I6T/V47M/T69K


enzyme_display_name: 3-isopropylmalate dehydrogenase

organism: Thermus thermophilus (strain ATCC 27634 / DSM 579 / HB8)

substrate_name: 3-isopropylmalate (at pH 8 and 60 degrees Celsius)

enzyme: 3-isopropylmalate dehydrogenase


enzyme_display_name: ketol-acid reductoisomerase (NADP(+))

organism: Streptococcus pneumoniae

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D191G to reconstruct the assayed variant sequence.

enzyme: ketol-acid reductoisomerase (NADP(+))


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D191K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D83G with inferred residue-numbering offset -8 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E195A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E195K to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E195S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R49A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R49E to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R49G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S53A with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S53G with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S53K with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S53T with inferred residue-numbering offset -13 to reconstruct the assayed variant sequence.


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


organism: Zea mays

substrate_name: oxaloacetate

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

proof_lines:
cosubstrate NADPH
cosubstrate NADH

substrate: oxaloacetate


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


assay_conditions_summary: cofactor NADH


substrate_name: (S)-malate

proof_lines:
cosubstrate NAD+
cosubstrate NADP+

substrate: (S)-malate


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


proof_lines:
wild-type enzyme D201A
wild-type enzyme


assay_conditions_summary: cofactor NADPH


organism: Streptomyces coelicolor

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


organism: Streptomyces lividans


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


substrate_name: pyruvate

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

substrate: pyruvate


enzyme_display_name: aryl-alcohol dehydrogenase

organism: Streptomyces sp.

substrate_name: cinnamyl alcohol

enzyme: aryl-alcohol dehydrogenase

substrate: cinnamyl alcohol


substrate_name: coniferyl alcohol

substrate: coniferyl alcohol


substrate_name: coniferyl aldehyde

substrate: coniferyl aldehyde


assay_conditions_summary: pH 8; 303.15 K; cofactor NAD+


enzyme_display_name: aryl-alcohol dehydrogenase (NADP+)

organism: Solanum tuberosum

substrate_name: p-fluorobenzaldehyde

enzyme: aryl-alcohol dehydrogenase (NADP+)

substrate: p-fluorobenzaldehyde


substrate_name: o-fluorobenzaldehyde

substrate: o-fluorobenzaldehyde


substrate_name: p-methylbenzaldehyde

substrate: p-methylbenzaldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: p-chlorobenzaldehyde

substrate: p-chlorobenzaldehyde


substrate_name: m-fluorobenzaldehyde

substrate: m-fluorobenzaldehyde


substrate_name: m-hydroxybenzaldehyde

substrate: m-hydroxybenzaldehyde


substrate_name: benzyl alcohol

substrate: benzyl alcohol


enzyme_display_name: homoisocitrate dehydrogenase

organism: Thermococcus kodakarensis

substrate_name: homoisocitrate

assay_conditions_summary: pH 8; 333.15 K; cofactor NAD+

proof_lines: mutant enzyme S80A, with NAD+ as cosubstrate, at pH 8.0 and 60°C

enzyme: homoisocitrate dehydrogenase

substrate: homoisocitrate


proof_lines: mutant enzyme T71V, with NAD+ as cosubstrate, at pH 8.0 and 60°C


assay_conditions_summary: pH 8; 333.15 K; cofactor NADP+

proof_lines: wild type enzyme, with NADP+ as cosubstrate, at pH 8.0 and 60°C

proof_lines: wild type enzyme, with NAD+ as cosubstrate, at pH 8.0 and 60°C


proof_lines: wild type enzyme, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C


proof_lines: mutant enzyme L81P, with NAD+ as cosubstrate, at pH 8.0 and 60°C


proof_lines: mutant enzyme L83R, with NAD+ as cosubstrate, at pH 8.0 and 60°C


proof_lines: mutant enzyme I82N, with NAD+ as cosubstrate, at pH 8.0 and 60°C


proof_lines: mutant enzyme L83R, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C

proof_lines: mutant enzyme L83R, with isocitrate as cosubstrate, at pH 8.0 and 60°C


proof_lines: mutant enzyme T71V, with isocitrate as cosubstrate, at pH 8.0 and 60°C

proof_lines: mutant enzyme T71V, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C

proof_lines: mutant enzyme T71V, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C


proof_lines: mutant enzyme L81P, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C

proof_lines: mutant enzyme L81P, with isocitrate as cosubstrate, at pH 8.0 and 60°C

proof_lines: mutant enzyme L81P, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C


proof_lines: mutant enzyme I82N, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C

proof_lines: mutant enzyme I82N, with isocitrate as cosubstrate, at pH 8.0 and 60°C


proof_lines: mutant enzyme S80A, with isocitrate as cosubstrate, at pH 8.0 and 60°C

proof_lines: mutant enzyme S80A, with homoisocitrate as cosubstrate, at pH 8.0 and 60°C

proof_lines: mutant enzyme S80A, with 3-isopropylmalate as cosubstrate, at pH 8.0 and 60°C


organism: Acinetobacter calcoaceticus

substrate_name: 4-Hydroxybenzyl alcohol

substrate: 4-Hydroxybenzyl alcohol


substrate_name: perillyl alcohol

substrate: perillyl alcohol


substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


substrate_name: 4-Isopropylbenzyl alcohol

substrate: 4-Isopropylbenzyl alcohol


substrate_name: 3-Methoxybenzyl alcohol

substrate: 3-Methoxybenzyl alcohol


substrate_name: 3,4-dimethoxybenzyl alcohol

substrate: 3,4-dimethoxybenzyl alcohol


substrate_name: 2-hydroxybenzyl alcohol

substrate: 2-hydroxybenzyl alcohol


substrate_name: 2-Methoxybenzyl alcohol

substrate: 2-Methoxybenzyl alcohol


substrate_name: NADPH

substrate: NADPH


substrate_name: p-Hydroxybenzaldehyde

substrate: p-Hydroxybenzaldehyde


substrate_name: m-chlorobenzaldehyde

substrate: m-chlorobenzaldehyde


substrate_name: m-bromobenzaldehyde

substrate: m-bromobenzaldehyde


substrate_name: NADP+

substrate: NADP+


substrate_name: o-chlorobenzaldehyde

substrate: o-chlorobenzaldehyde


substrate_name: m-nitrobenzaldehyde

substrate: m-nitrobenzaldehyde


substrate_name: cinnamic aldehyde

substrate: cinnamic aldehyde


substrate_name: p-bromobenzaldehyde

substrate: p-bromobenzaldehyde


substrate_name: o-bromobenzaldehyde

substrate: o-bromobenzaldehyde


organism: Deinococcus radiodurans

proof_lines: pH 7.8, 25°C, recombinant wild-type enzyme


substrate_name: homoisocitrate

mutation_type: deletion

substrate: homoisocitrate


substrate_name: isocitrate

substrate: isocitrate


substrate_name: isopropylmalate

substrate: isopropylmalate


substrate_name: (2R,3S)-3-propylmalic acid

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

substrate: (2R,3S)-3-propylmalic acid


organism: Neurospora crassa


substrate_name: 4-methoxybenzyl alcohol

substrate: 4-methoxybenzyl alcohol


substrate_name: acetaldehyde

substrate: acetaldehyde


organism: Saccharomyces cerevisiae

proof_lines: pH 6.1, temperature not specified in the publication


substrate_name: Heptanal

smiles: CCCCCCC=O

substrate: Heptanal


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


organism: Brassica napus subsp. rapifera

substrate_name: NADH

substrate: NADH


substrate_name: NADPH

substrate: NADPH


substrate_name: coniferyl aldehyde

substrate: coniferyl aldehyde


substrate_name: coniferyl alcohol

substrate: coniferyl alcohol


substrate_name: D-malate

sequence_source: uniprot

column_label: Table 2. Kinetic properties of TK0280; D-malate / NAD+ row; kcat=0.099 +/- 0.006 s^-1; Ksubstrate=4500 +/- 800 uM; kcat/Ksubstrate=2.2 x 10^1 M^-1 s^-1.

row_label: D-malate / NAD+ wild-type

table_label: Table 2. Kinetic properties of TK0280

substrate: D-malate


substrate_name: NAD+

column_label: Table 2. Kinetic properties of TK0280; HIC / NAD+ row; kcat=17 +/- 1 s^-1; KNAD(P)=36 +/- 9 uM; kcat/KNAD(P)=4.7 x 10^5 M^-1 s^-1.

row_label: HIC / NAD+ wild-type

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5JFV8;refseq:WP_011249235.1;rcsb:5HN3,5HN4,5HN5,5HN6 and applied mutation signature T71V to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic properties of mutant enzymes; For IC / T71V; kcat=0.22 +/- 0.01 s^-1; Ksubstrate=500 +/- 90 uM; kcat/Ksubstrate=4.4 x 10^2 M^-1 s^-1.

row_label: For IC / T71V


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5JFV8;refseq:WP_011249235.1;rcsb:5HN3,5HN4,5HN5,5HN6 and applied mutation signature S80A to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic properties of mutant enzymes; For IC / S80A; kcat=0.71 +/- 0.2 s^-1; Ksubstrate=300 +/- 40 uM; kcat/Ksubstrate=2.4 x 10^3 M^-1 s^-1.

row_label: For IC / S80A


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5JFV8;refseq:WP_011249235.1;rcsb:5HN3,5HN4,5HN5,5HN6 and applied mutation signature I82N to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic properties of mutant enzymes; For IC / I82N; kcat=1.0 +/- 0.1 s^-1; Ksubstrate=2200 +/- 400 uM; kcat/Ksubstrate=4.5 x 10^2 M^-1 s^-1.

row_label: For IC / I82N


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5JFV8;refseq:WP_011249235.1;rcsb:5HN3,5HN4,5HN5,5HN6 and applied mutation signature L81P to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic properties of mutant enzymes; For IC / L81P; kcat=1.1 +/- 0.1 s^-1; Ksubstrate=1200 +/- 200 uM; kcat/Ksubstrate=9.2 x 10^2 M^-1 s^-1.

row_label: For IC / L81P


column_label: Table 4. Kinetic properties of mutant enzymes; For IPM / L81P; kcat=1.5 +/- 0.1 s^-1; Ksubstrate=680 +/- 120 uM; kcat/Ksubstrate=2.2 x 10^3 M^-1 s^-1.

row_label: For IPM / L81P


column_label: Table 4. Kinetic properties of mutant enzymes; For IPM / S80A; kcat=2.3 +/- 0.1 s^-1; Ksubstrate=50 +/- 6 uM; kcat/Ksubstrate=4.6 x 10^4 M^-1 s^-1.

row_label: For IPM / S80A


column_label: Table 2. Kinetic properties of TK0280; IPM / NAD+ row; kcat=4.8 +/- 0.2 s^-1; Ksubstrate=310 +/- 60 uM; kcat/Ksubstrate=1.5 x 10^4 M^-1 s^-1.

row_label: IPM / NAD+ wild-type


column_label: Table 4. Kinetic properties of mutant enzymes; For HIC / T71V; kcat=4.8 +/- 0.3 s^-1; Ksubstrate=940 +/- 160 uM; kcat/Ksubstrate=5.1 x 10^3 M^-1 s^-1.

row_label: For HIC / T71V


column_label: Table 2. Kinetic properties of TK0280; IC / NAD+ row; kcat=5.0 +/- 0.2 s^-1; Ksubstrate=14 +/- 3 uM; kcat/Ksubstrate=3.6 x 10^5 M^-1 s^-1.

row_label: IC / NAD+ wild-type


sequence_variant_note: Resolved canonical sequence from uniprotkb:Q5JFV8;refseq:WP_011249235.1;rcsb:5HN3,5HN4,5HN5,5HN6 and applied mutation signature L83R to reconstruct the assayed variant sequence.

column_label: Table 4. Kinetic properties of mutant enzymes; For IC / L83R; kcat=6.6 +/- 0.2 s^-1; Ksubstrate=580 +/- 90 uM; kcat/Ksubstrate=1.1 x 10^4 M^-1 s^-1.

row_label: For IC / L83R


organism: Yokenella sp. WZY002

substrate_name: benzyl alcohol

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

assay_conditions_summary: pH 6.5; cofactor NADP+

column_label: Table 5 row Benzyl alcohol / NADP+ (0.4 mM); columns Apparent Km (mM), Kcat (s^-1), Kcat/Km (s^-1 mM^-1)

row_label: Benzyl alcohol / NADP+ (0.4 mM)

table_label: PMCID PMC3993188 Table 5

substrate: benzyl alcohol


substrate_name: crotonyl alcohol

smiles: CC=CCO

assay_conditions_summary: pH 8; cofactor NADP+

column_label: Table 5 row Crotyl alcohol / NADP+ (0.4 mM); columns Apparent Km (mM), Kcat (s^-1), Kcat/Km (s^-1 mM^-1)

row_label: Crotyl alcohol / NADP+ (0.4 mM)

substrate: crotonyl alcohol


substrate_name: NADP+

column_label: Table 5 row NADP+ / Crotyl alcohol (40 mM); columns Apparent Km (mM), Kcat (s^-1), Kcat/Km (s^-1 mM^-1)

row_label: NADP+ / Crotyl alcohol (40 mM)

substrate: NADP+


substrate_name: benzaldehyde

assay_conditions_summary: pH 6.5; cofactor NADPH

column_label: Table 5 row Benzaldehyde / NADPH (0.4 mM); columns Apparent Km (mM), Kcat (s^-1), Kcat/Km (s^-1 mM^-1)

row_label: Benzaldehyde / NADPH (0.4 mM)

substrate: benzaldehyde


substrate_name: crotonaldehyde

smiles: CC=CC=O

assay_conditions_summary: pH 8; cofactor NADPH

column_label: Table 5 row Crotonaldehyde / NADPH (0.4 mM); columns Apparent Km (mM), Kcat (s^-1), Kcat/Km (s^-1 mM^-1)

row_label: Crotonaldehyde / NADPH (0.4 mM)

substrate: crotonaldehyde


enzyme_display_name: dimethylmalate dehydrogenase

organism: Pseudomonas fluorescens

enzyme: dimethylmalate dehydrogenase


organism: Pseudomonas sp.


enzyme_display_name: hydroxymethylglutaryl-CoA reductase

organism: Mycobacterium sp.

substrate_name: CoA

assay_conditions_summary: cofactor CoA

enzyme: hydroxymethylglutaryl-CoA reductase

substrate: CoA


substrate_name: DL-mevalonate

smiles: CC(CCO)(CC(=O)O)O

substrate: DL-mevalonate


organism: Thermus thermophilus

proof_lines:
purified enzyme, pH 8.0, 60°C
pH 7.8, 60°C


organism: synthetic construct

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

proof_lines:
acIPMDH-ML, pH 8.0, 25°C
ancIPMDH-IQ, pH 8.0, 25°C
acIPMDH-ML, pH 8.0, 40°C


substrate_name: isocitrate

substrate: isocitrate


proof_lines: pH 7.5, 60°C, recombinant wild-type enzyme


organism: Saccharum officinarum

substrate_name: sinapyl alcohol

substrate: sinapyl alcohol


organism: Cupriavidus necator

smiles: CCCCCCC(C)O

proof_lines:
isoform SDR B3, at pH 10.0 and 40°C
isoform SDR A5, at pH 10.0 and 40°C


organism: Mycobacterium tuberculosis

substrate_name: p-aminobenzyl alcohol

substrate: p-aminobenzyl alcohol


smiles: CC(=CCO)C


organism: Phanerodontia chrysosporium

assay_conditions_summary: pH 6.1; cofactor NADH

column_label: Table 2. Kinetic parameters of the recombinant Aad1p from Phanerochaete chrysosporium; row Coenzymes / NADH; columns KM (uM); Kcat (min^-1); kcat/KM (uM^-1 min^-1); raw row cells: NADH | KM 220 +/- 130 uM | Kcat 120 +/- 40 min^-1 | kcat/KM 0.6 +/- 0.5 uM^-1 min^-1 | Ki ni uM

normalized_value_unit_evidence: kcat normalized_value=2.0 normalized_unit=s^-1; Km normalized_value=0.22 normalized_unit=mM; kcat/Km normalized_value=9.090909090909092 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=120 +/- 40 raw_unit=min^-1; Km raw_value=220 +/- 130 raw_unit=uM; kcat/Km raw_value=0.6 +/- 0.5 raw_unit=uM^-1*min^-1; Ki raw_value=ni raw_unit=uM

row_label: Coenzymes / NADH


substrate_name: 3,4-dimethoxybenzyl alcohol

assay_conditions_summary: pH 6.1; cofactor NADP+

column_label: Table 2. Kinetic parameters of the recombinant Aad1p from Phanerochaete chrysosporium; row Oxidation / 3,4-Dimethoxybenzyl alcohol; columns KM (uM); Kcat (min^-1); kcat/KM (uM^-1 min^-1); raw row cells: 3,4-Dimethoxybenzyl alcohol | KM 370 +/- 50 uM | Kcat 153 +/- 6 min^-1 | kcat/KM 0.41 +/- 0.07 uM^-1 min^-1 | Ki 165000 +/- 31000 uM

normalized_value_unit_evidence: kcat normalized_value=2.55 normalized_unit=s^-1; Km normalized_value=0.37 normalized_unit=mM; kcat/Km normalized_value=6.891891891891891 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=153 +/- 6 raw_unit=min^-1; Km raw_value=370 +/- 50 raw_unit=uM; kcat/Km raw_value=0.41 +/- 0.07 raw_unit=uM^-1*min^-1; Ki raw_value=165000 +/- 31000 raw_unit=uM

row_label: Oxidation / 3,4-Dimethoxybenzyl alcohol

substrate: 3,4-dimethoxybenzyl alcohol


column_label: Table 2. Kinetic parameters of the recombinant Aad1p from Phanerochaete chrysosporium; row Coenzymes / NADP+; columns KM (uM); Kcat (min^-1); kcat/KM (uM^-1 min^-1); raw row cells: NADP+ | KM 38 +/- 7 uM | Kcat 154 +/- 7 min^-1 | kcat/KM 4.1 +/- 0.9 uM^-1 min^-1 | Ki ni uM

normalized_value_unit_evidence: kcat normalized_value=2.56 normalized_unit=s^-1; Km normalized_value=0.038 normalized_unit=mM; kcat/Km normalized_value=67.36842105263158 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=154 +/- 7 raw_unit=min^-1; Km raw_value=38 +/- 7 raw_unit=uM; kcat/Km raw_value=4.1 +/- 0.9 raw_unit=uM^-1*min^-1; Ki raw_value=ni raw_unit=uM

row_label: Coenzymes / NADP+


assay_conditions_summary: pH 6.1; cofactor NADPH

column_label: Table 2. Kinetic parameters of the recombinant Aad1p from Phanerochaete chrysosporium; row Reduction / 5-(Hydroxymethyl)-2-furaldehyde; columns KM (uM); Kcat (min^-1); kcat/KM (uM^-1 min^-1); raw row cells: 5-(Hydroxymethyl)-2-furaldehyde | KM 270 +/- 40 uM | Kcat 176 +/- 6 min^-1 | kcat/KM 0.65 +/- 0.12 uM^-1 min^-1 | Ki 136000 +/- 28000 uM

normalized_value_unit_evidence: kcat normalized_value=2.93 normalized_unit=s^-1; Km normalized_value=0.27 normalized_unit=mM; kcat/Km normalized_value=10.851851851851851 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=176 +/- 6 raw_unit=min^-1; Km raw_value=270 +/- 40 raw_unit=uM; kcat/Km raw_value=0.65 +/- 0.12 raw_unit=uM^-1*min^-1; Ki raw_value=136000 +/- 28000 raw_unit=uM


column_label: Table 2. Kinetic parameters of the recombinant Aad1p from Phanerochaete chrysosporium; row Reduction / 4-Hydroxy-3-methoxybenzaldehyde; columns KM (uM); Kcat (min^-1); kcat/KM (uM^-1 min^-1); raw row cells: 4-Hydroxy-3-methoxybenzaldehyde | KM 1400 +/- 600 uM | Kcat 200 +/- 50 min^-1 | kcat/KM 0.14 +/- 0.10 uM^-1 min^-1 | Ki 5100 +/- 2300 uM

normalized_value_unit_evidence: kcat normalized_value=3.33 normalized_unit=s^-1; Km normalized_value=1.4 normalized_unit=mM; kcat/Km normalized_value=2.3785714285714286 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=200 +/- 50 raw_unit=min^-1; Km raw_value=1400 +/- 600 raw_unit=uM; kcat/Km raw_value=0.14 +/- 0.10 raw_unit=uM^-1*min^-1; Ki raw_value=5100 +/- 2300 raw_unit=uM


column_label: Table 2. Kinetic parameters of the recombinant Aad1p from Phanerochaete chrysosporium; row Reduction / 3-Hydroxy-4-methoxybenzaldehyde; columns KM (uM); Kcat (min^-1); kcat/KM (uM^-1 min^-1); raw row cells: 3-Hydroxy-4-methoxybenzaldehyde | KM 1400 +/- 900 uM | Kcat 230 +/- 110 min^-1 | kcat/KM 0.16 +/- 0.18 uM^-1 min^-1 | Ki 2300 +/- 1800 uM

normalized_value_unit_evidence: kcat normalized_value=3.83 normalized_unit=s^-1; Km normalized_value=1.4 normalized_unit=mM; kcat/Km normalized_value=2.7357142857142858 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=230 +/- 110 raw_unit=min^-1; Km raw_value=1400 +/- 900 raw_unit=uM; kcat/Km raw_value=0.16 +/- 0.18 raw_unit=uM^-1*min^-1; Ki raw_value=2300 +/- 1800 raw_unit=uM


substrate_name: 4-hydroxy-3-methoxy-benzyl alcohol

column_label: Table 2. Kinetic parameters of the recombinant Aad1p from Phanerochaete chrysosporium; row Oxidation / 4-Hydroxy-3-methoxybenzyl alcohol; columns KM (uM); Kcat (min^-1); kcat/KM (uM^-1 min^-1); raw row cells: 4-Hydroxy-3-methoxybenzyl alcohol | KM 25000 +/- 7000 uM | Kcat 260 +/- 60 min^-1 | kcat/KM 0.010 +/- 0.005 uM^-1 min^-1 | Ki ni uM

normalized_value_unit_evidence: kcat normalized_value=4.33 normalized_unit=s^-1; Km normalized_value=25.0 normalized_unit=mM; kcat/Km normalized_value=0.1732 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=260 +/- 60 raw_unit=min^-1; Km raw_value=25000 +/- 7000 raw_unit=uM; kcat/Km raw_value=0.010 +/- 0.005 raw_unit=uM^-1*min^-1; Ki raw_value=ni raw_unit=uM

substrate: 4-hydroxy-3-methoxy-benzyl alcohol


column_label: Europe PMC fullTextXML Table 2; row 4-Methoxybenzaldehyde; KM, Kcat, and kcat/KM columns. Table label: Kinetic parameters of the recombinant Aad1p from Phanerochaete chrysosporium.

normalized_value_unit_evidence: normalized Table 2 values: KM=0.09 mM; kcat=8.17 s^-1; printed kcat/KM=90 s^-1 mM^-1; exported kcat/Km=90.66666666666667 s^-1 mM^-1.

raw_value_unit_evidence: Table 2 row 4-Methoxybenzaldehyde; KM=90 uM; Kcat=490 min^-1; kcat/KM=5.4 uM^-1 min^-1.

table_label: Table 2


column_label: Table 2. Kinetic parameters of the recombinant Aad1p from Phanerochaete chrysosporium; row Reduction / 3,5-Dimethoxybenzaldehyde; columns KM (uM); Kcat (min^-1); kcat/KM (uM^-1 min^-1); raw row cells: 3,5-Dimethoxybenzaldehyde | KM 22 +/- 4 uM | Kcat 590 +/- 30 min^-1 | kcat/KM 27 +/- 6 uM^-1 min^-1 | Ki 2100 +/- 600 uM

normalized_value_unit_evidence: kcat normalized_value=9.83 normalized_unit=s^-1; Km normalized_value=0.022 normalized_unit=mM; kcat/Km normalized_value=446.81818181818187 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=590 +/- 30 raw_unit=min^-1; Km raw_value=22 +/- 4 raw_unit=uM; kcat/Km raw_value=27 +/- 6 raw_unit=uM^-1*min^-1; Ki raw_value=2100 +/- 600 raw_unit=uM

row_label: Reduction / 3,5-Dimethoxybenzaldehyde