organism: Haloferax mediterranei (strain ATCC 33500 / DSM 1411 / JCM 8866 / NBRC 14739 / NCIMB 2177 / R-4)

substrate_name: beta-D-glucose (in the presence of NADP(+), at 40 degrees Celsius and pH 8.8)


enzyme_display_name: galactose 1-dehydrogenase

organism: Mus musculus

substrate_name: D-Galactose 6-phosphate; NADP+

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

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

km_unit: mM

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

assay_conditions_summary: cofactor NADP+

enzyme: galactose 1-dehydrogenase

substrate: D-Galactose 6-phosphate; NADP+

status: unverified


enzyme_display_name: L-arabinose 1-dehydrogenase (NAD(P)(+))

organism: Azospirillum brasilense

substrate_name: L-arabinose (in the presence of NAD(+), at 30 degrees Celsius and pH 9.0)

source_db: uniprot

source_license: CC BY 4.0

assay_conditions_summary: pH 9

enzyme: L-arabinose 1-dehydrogenase (NAD(P)(+))

source: uniprot


enzyme_display_name: Glucose 1-dehydrogenase

organism: Saccharolobus solfataricus

substrate_name: D-glucose (in the presence of NAD(+), at 70 degrees Celsius and pH 8)

assay_conditions_summary: pH 8; cofactor NADP+

proof_lines: Saccharolobus solfataricus glucose dehydrogenase

enzyme: Glucose 1-dehydrogenase


organism: Thermotoga maritima

substrate_name: thio-NAD+

source_db: brenda

assay_conditions_summary: pH 7.4; 353.15 K; cofactor NADP+

substrate: thio-NAD+

source: brenda


organism: Taenia crassiceps

substrate_name: Unknown

km_display: Not reported

ki_unit: mM

proof_lines: Kis, variable substrate D-glucose 6-phosphate

proof_lines: Kii, variable substrate D-glucose 6-phosphate

substrate: Unknown


organism: Rattus norvegicus

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

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

proof_lines: pH 7.6, and temperature not specified in the publication, competitive inhibition with respect to NADP+

proof_lines: pH 7.6, and temperature not specified in the publication, competitive inhibition with respect to D-glucose 6-phosphate


organism: Aspergillus aculeatus

assay_conditions_summary: pH 7.5; cofactor NADP+

proof_lines:
pH 7.5
pH 7.5, versus NADP+
pH 7.5, versus D-glucose 6-phosphate


organism: Brugia malayi

proof_lines: versus D-glucose 6-phosphate, pH 8.0, 25°C


substrate_name: 2-Deoxy-D-glucose 6-phosphate

source_db: oed

kcat_over_km_origin: calculated

data_origin: experimental

substrate: 2-Deoxy-D-glucose 6-phosphate

source: oed


substrate_name: NAD+

assay_conditions_summary: pH 7.4; 353.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADP+

substrate: NADP+


substrate_name: thio-NADP+

substrate: thio-NADP+


substrate_name: glucose 6-phosphate

substrate: glucose 6-phosphate


organism: Plasmodium falciparum (isolate 3D7)

substrate_name: 6-phosphoglucono-gamma-lactone (at 25 degrees Celsius)


enzyme_display_name: Glucose-6-phosphate 1-dehydrogenase

organism: Gluconobacter oxydans (strain 621H)

proof_lines: kcat is 44.1 sec(-1). Can use NAD or NADP in vitro, but primarily functions in a NADP-dependent manner in vivo.

enzyme: Glucose-6-phosphate 1-dehydrogenase


proof_lines: pH 7.4, 25°C, recombinant wild-type AKR1C17


organism: Comamonas testosteroni

substrate_name: NADH

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature Y155F to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 7.5; cofactor NADH

proof_lines: mutant Y155F, pH 7.5, 25°C, steady-state kinetic study

substrate: NADH


proof_lines: mutant Y155F, pH 7.5, 25°C, product inhibition study


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature N86A with inferred residue-numbering offset -5 to reconstruct the assayed variant sequence.

proof_lines: mutant N86A, pH 7.5, 25°C, steady-state kinetic study


proof_lines: mutant N86A, pH 7.5, 25°C, product inhibition study


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K159A with inferred residue-numbering offset +9 to reconstruct the assayed variant sequence.

proof_lines: mutant K159A, pH 7.5, 25°C, product inhibition study


proof_lines: mutant K159A, pH 7.5, 25°C, steady-state kinetic study


substrate_name: androstandione

substrate: androstandione


organism: Pseudomonas sp

sequence: QVIAITGSASGIGAA

wild_type_sequence: QVIAITGSASGIGAA


enzyme_display_name: Aldo-keto reductase family 1 member C4

organism: Homo sapiens

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

enzyme: Aldo-keto reductase family 1 member C4


enzyme_display_name: Aldo-keto reductase family 1 member C2

proof_lines: kcat is 19.88 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:10998348). kcat is 1.98 min(-1) for the reduction of 17beta-hydroxy-5alpha-androstan-3-one (PubMed:19218247). kcat is 1.39 min(-1) for the reduction of

enzyme: Aldo-keto reductase family 1 member C2


enzyme_display_name: Aldo-keto reductase family 1 member C1

proof_lines: kcat is 0.29 min(-1) for the reduction of progesterone (PubMed:10998348). kcat is 1.1 min(-1) for the reduction of 3beta-hydroxy-5beta-pregnane-20-one (PubMed:10998348). kcat is 1.2 min(-1) for the oxidation of (20S)-hydroxypregn-4-en-3-one

enzyme: Aldo-keto reductase family 1 member C1


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

organism: Drosophila melanogaster

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

assay_conditions_summary: pH 9.3; cofactor CoA

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


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_display_name: 2-hydroxy-3-oxopropionate reductase

organism: Escherichia coli

substrate_name: NADH; 2-Hydroxy-3-oxopropanoate; H+

assay_conditions_summary: cofactor NADH

enzyme: 2-hydroxy-3-oxopropionate reductase

substrate: NADH; 2-Hydroxy-3-oxopropanoate; H+


substrate_name: NAD+; D-Glycerate

assay_conditions_summary: cofactor NAD+

substrate: NAD+; D-Glycerate


organism: Haemophilus influenzae

substrate_name: D-Glycerate; NAD+

substrate: D-Glycerate; NAD+


enzyme_display_name: 4-hydroxybutyrate dehydrogenase

substrate_name: 3-hydroxypropane sulfonate

sequence_source: multiple

assay_conditions_summary: pH 8.8; 310.15 K; buffer 100 mM Tris-HCl; cofactor NADH

proof_lines: in 100 mM Tris-HCl buffer (pH 8.8), at 37°C

proof_lines: kcat is 332 sec(-1) with 3-sulfolactaldehyde as substrate. kcat is 548 sec(-1) with NADH as substrate.

source_databases_merged: brenda uniprot

enzyme: 4-hydroxybutyrate dehydrogenase

substrate: 3-hydroxypropane sulfonate


enzyme_display_name: estradiol 17beta-dehydrogenase

enzyme: estradiol 17beta-dehydrogenase


substrate_name: Estrone; H+; NADPH

verification_status: verified

assay_conditions_summary: cofactor NADPH

column_label: Official OUP Table 1 row '17beta-HSD12', column 'Km (uM)': 3.5 +/- 0.5; Vmax column: 56 +/- 7

raw_value_unit_evidence: Table 1 row 17beta-HSD12: Km raw_value=3.5 +/- 0.5 uM; Vmax=56 +/- 7 nmol product/h/10^6 cells

table_label: OUP full text Table 1. Kinetic parameters of human types 1, 7, and 12 17beta-HSD

substrate: Estrone; H+; NADPH

status: verified


substrate_name: H+; NADPH; Estrone

column_label: Official OUP Table 1 row '17beta-HSD1', column 'Km (uM)': 0.2 +/- 0.05; Vmax column: 110 +/- 15

raw_value_unit_evidence: Table 1 row 17beta-HSD1: Km raw_value=0.2 +/- 0.05 uM; Vmax=110 +/- 15 nmol product/h/10^6 cells

substrate: H+; NADPH; Estrone


column_label: Official OUP Table 1 row '17beta-HSD7', column 'Km (uM)': 4.0 +/- 0.3; Vmax column: 83 +/- 9

raw_value_unit_evidence: Table 1 row 17beta-HSD7: Km raw_value=4.0 +/- 0.3 uM; Vmax=83 +/- 9 nmol product/h/10^6 cells


organism: Mus musculus

substrate_name: Estradiol-17beta; NAD+

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

substrate: Estradiol-17beta; NAD+


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_name: NAD+; Estradiol-17beta

substrate: NAD+; Estradiol-17beta


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

substrate_name: Unknown

proof_lines: The kinetic parameters were determined using microsomes from transfected cells.


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

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


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase 13

enzyme: 17-beta-hydroxysteroid dehydrogenase 13


enzyme_display_name: Dehydrogenase/reductase SDR family member 11

substrate_name: 5-alpha-androstan-3-beta-ol-17-one (at 37 degrees Celsius)


proof_lines: Vmax was measured using transfected cell lysates.

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6


substrate: NAD (in the presence of (3S)-3-hydroxybutanoyl-CoA, at pH 9.3 and 25 degrees Celsius)


enzyme_display_name: 3-keto-steroid reductase/17-beta-hydroxysteroid dehydrogenase 7

substrate: Unknown


substrate_name: NADP+; Testosterone

substrate: NADP+; Testosterone


substrate_name: Testosterone; NADP+

substrate: Testosterone; NADP+


substrate_name: NADPH; H+; Androst-4-ene-3,17-dione

substrate: NADPH; H+; Androst-4-ene-3,17-dione


proof_lines: isoform 17beta-hydroxysteroid dehydrogenase type 3, pH 7.4, 37°C

proof_lines: isoform 3beta-hydroxysteriod dehydrogenase, pH 7.4, 37°C

proof_lines: isoform 17beta-hydroxysteroid dehydrogenase type 3 , pH 7.4, 37°C


enzyme_display_name: Aldo-keto reductase family 1 member B15

substrate_name: 3-alpha,17-beta-androstandiol (tested with isoform 1 in the oxidative reaction)

assay_conditions_summary: cofactor CoA

proof_lines: kcat is 1.7 min(-1) using isoform 1 for the reduction of androsterone. kcat is 1.1 min(-1) using isoform 1 for the reduction of delta-4-androstenedione. kcat is 1.0 min(-1) using isoform 1 for the reduction of estrone. kcat is 0.5 min(-1) u

enzyme: Aldo-keto reductase family 1 member B15


enzyme_display_name: pyridoxine 4-dehydrogenase

organism: Schizosaccharomyces pombe

substrate_name: Pyridoxal; H+; NADPH

enzyme: pyridoxine 4-dehydrogenase

substrate: Pyridoxal; H+; NADPH


enzyme_display_name: All-trans-retinol dehydrogenase [NAD(+)] ADH7

substrate_name: 12-OH-dodecanoic acid (with 0.1 M sodium phosphate at pH 7.5)


enzyme_display_name: mannitol 2-dehydrogenase

organism: Pseudomonas fluorescens

substrate_name: NADH; H+; D-Fructose

enzyme: mannitol 2-dehydrogenase

substrate: NADH; H+; D-Fructose


organism: Aspergillus fumigatus

substrate_name: D-Mannitol; NAD+

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NAD+

proof_lines:
pH 7.1, 25°C, reduction of fructose
pH 7.1, 25°C, oxidation of mannitol

source_databases_merged: sabio_rk brenda uniprot

substrate: D-Mannitol; NAD+


enzyme_display_name: Mannitol dehydrogenase DSF1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

enzyme: Mannitol dehydrogenase DSF1


enzyme_display_name: isocitrate dehydrogenase (NAD+)

organism: Phycomyces blakesleeanus

substrate_name: NAD+; Isocitrate

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

enzyme: isocitrate dehydrogenase (NAD+)

substrate: NAD+; Isocitrate


enzyme_display_name: isocitrate dehydrogenase (NADP+)

organism: Streptococcus suis

substrate_name: Isocitrate; NADP+

enzyme: isocitrate dehydrogenase (NADP+)

substrate: Isocitrate; NADP+


enzyme_display_name: glucose 1-dehydrogenase

organism: Bos taurus

substrate_name: NAD+; beta-D-Glucose

enzyme: glucose 1-dehydrogenase

substrate: NAD+; beta-D-Glucose


organism: Sus scrofa

substrate_name: beta-D-Glucose; NAD+

substrate: beta-D-Glucose; NAD+


organism: Gallus gallus

substrate_name: NADP+; Estradiol-17beta

substrate: NADP+; Estradiol-17beta


enzyme_display_name: 3-hydroxypropionate dehydrogenase

organism: Bacillus cereus

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

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

enzyme: 3-hydroxypropionate dehydrogenase


proof_lines: pH 8.5, 37°C, KM-value for 3-hydroxyisobutyrate is approximately 20fold lower


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NADP+

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+

substrate: NAD+


enzyme_display_name: allyl-alcohol dehydrogenase

assay_conditions_summary: cofactor NADP+

enzyme: allyl-alcohol dehydrogenase


substrate_name: allyl-alcohol

smiles: C=CCO

substrate: allyl-alcohol


organism: Candida albicans

assay_conditions_summary: pH 9.5; 295.15 K; cofactor CoA


substrate_name: L-serine

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

substrate: L-serine


substrate_name: NAD+; 3-Hydroxypropanoate

substrate: NAD+; 3-Hydroxypropanoate


enzyme_display_name: lactaldehyde reductase (NADPH)

substrate_name: H+; Lactaldehyde; NADPH

enzyme: lactaldehyde reductase (NADPH)

substrate: H+; Lactaldehyde; NADPH


substrate_name: L-lactaldehyde

smiles: CC(C=O)O

substrate: L-lactaldehyde


enzyme_display_name: ribitol 2-dehydrogenase

organism: Gluconobacter oxydans

substrate_name: NADH

assay_conditions_summary: pH 9.5; 298.15 K; cofactor NADH

enzyme: ribitol 2-dehydrogenase

substrate: NADH


assay_conditions_summary: pH 9.5; 298.15 K; cofactor NAD+


substrate_name: D-ribulose

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

substrate: D-ribulose


substrate_name: ribitol

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

substrate: ribitol


organism: Pseudomonas putida

smiles: CC(=CCO)Cl


substrate_name: benzyl alcohol

substrate: benzyl alcohol


substrate_name: 3-aminobenzyl alcohol

substrate: 3-aminobenzyl alcohol


substrate_name: (R)-(+)-perillyl alcohol

substrate: (R)-(+)-perillyl alcohol


substrate_name: cinnamyl alcohol

substrate: cinnamyl alcohol


smiles: CC(=CCO)C


smiles: CC=CCO


proof_lines:
with 3-methyl-2-buten-1-ol
with benzyl alcohol


smiles: CC(C)CCO


smiles: CCCCO


smiles: CC(=C)CCO


organism: Sphingomonas sp.

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+


substrate_name: D-ribitol

substrate: D-ribitol


organism: Nicotiana tabacum

substrate_name: (S)-pulegone

proof_lines:
recombinant enzyme, pH 7.0, 35°C
native enzyme, pH 7.0, 35°C

substrate: (S)-pulegone


organism: Homo sapiens

substrate_name: NAD

substrate: NAD


substrate_name: NADPH

substrate: NADPH


substrate_name: NADP

substrate: NADP


substrate_name: all-trans-retinol

substrate: all-trans-retinol


substrate_name: allopregnanolone

substrate: allopregnanolone


substrate_name: androsterone

substrate: androsterone


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


organism: Providencia alcalifaciens

substrate_name: NAD+

assay_conditions_summary: pH 10; 308.15 K; cofactor NAD+

substrate: NAD+


substrate_name: all-trans-retinal

substrate: all-trans-retinal


substrate_name: D,L-glyceraldehyde

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

substrate: D,L-glyceraldehyde


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


smiles: CCCC=CC=O


smiles: CCCCCC(C=CC=O)O


smiles: CCCCCC=CC(=O)C


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


substrate_name: farnesal

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

substrate: farnesal


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

substrate_name: acetoacetyl-CoA (in the presence of 0.2 mM NADH, at pH 7.0 and 25 degrees Celsius)

assay_conditions_summary: pH 7; cofactor NADH

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


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


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


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


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


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


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


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Rattus norvegicus


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


substrate_name: testosterone

substrate: testosterone


substrate_name: estradiol

substrate: estradiol


substrate_name: NAD


substrate_name: NADP


organism: Agathobaculum desmolans

substrate_name: cortisone

proof_lines: pH and temperature not specified in the publication

substrate: cortisone


substrate_name: androsterone (tested with isoform 1 in the reductive reaction)


substrate_name: delta-4-androstenedione (tested with isoform 1 in the reductive reaction)


substrate_name: estrone (tested with isoform 1 in the reductive reaction)


substrate_name: acetoacetyl-CoA (tested with isoform 1 in the reductive reaction)


substrate_name: testosterone (tested with isoform 1 in the oxidative reaction)


substrate_name: 17-beta-estradiol (tested with isoform 1 in the oxidative reaction)


enzyme_display_name: Aldo-keto reductase family 1 member C1

substrate_name: (s)-tetralol

proof_lines: kcat is 0.29 min(-1) for the reduction of progesterone (PubMed:10998348). kcat is 1.1 min(-1) for the reduction of 3beta-hydroxy-5beta-pregnane-20-one (PubMed:10998348). kcat is 1.2 min(-1) for the oxidation of (20S)-hydroxypregn-4-en-3-one

enzyme: Aldo-keto reductase family 1 member C1

substrate: (s)-tetralol


enzyme_display_name: Aldo-keto reductase family 1 member C4

assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C4; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C4: Km 10.5 uM; kcat 2.1 min^-1; kcat/Km 200 min^-1 mM^-1.

enzyme: Aldo-keto reductase family 1 member C4


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


assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C4; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C4: Km 1.44 uM; kcat 1.79 min^-1; kcat/Km 1243 min^-1 mM^-1.


enzyme_display_name: Aldo-keto reductase family 1 member C3

enzyme: Aldo-keto reductase family 1 member C3


substrate_name: testosterone (oxidation)

substrate: testosterone (oxidation)


substrate_name: progesterone (reduction)

verification_status: corrected

column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Progesterone reduction / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Progesterone reduction / AKR1C1: Km 2.65 uM; kcat 0.29 min^-1; kcat/Km 109 min^-1 mM^-1.

row_label: Progesterone reduction / AKR1C1

substrate: progesterone (reduction)

status: corrected


column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3beta-Hydroxy-5beta-pregnan-20-one reduction / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3beta-Hydroxy-5beta-pregnan-20-one reduction / AKR1C1: Km 16.2 uM; kcat 1.10 min^-1; kcat/Km 68 min^-1 mM^-1.


column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxyprogesterone oxidation / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxyprogesterone oxidation / AKR1C1: Km 14.7 uM; kcat 1.20 min^-1; kcat/Km 82 min^-1 mM^-1.


column_label: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-DHT reduction / AKR1C1 (R); columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 2. Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-DHT reduction / AKR1C1 (R): Km 80.6 uM; kcat 0.66 min^-1; kcat/Km 8 min^-1 mM^-1.

row_label: 5alpha-DHT reduction / AKR1C1 (R)


column_label: Table 3. Kinetic parameters for 17-ketosteroid reduction and 17beta-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C1 (R); columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 3. Kinetic parameters for 17-ketosteroid reduction and 17beta-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C1 (R): Km 39.8 uM; kcat 0.044 min^-1; kcat/Km 1.1 min^-1 mM^-1.

row_label: Testosterone oxidation / AKR1C1 (R)


column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxy-5beta-pregnan-3-one oxidation / AKR1C1; columns Km (uM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

raw_value_unit_evidence: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxy-5beta-pregnan-3-one oxidation / AKR1C1: Km 19.4 uM; kcat 3.23 min^-1; kcat/Km 167 min^-1 mM^-1.


enzyme_display_name: Aldo-keto reductase family 1 member B1

substrate_name: acrolein

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


smiles: CC(=CC=O)C


smiles: CC=CC=CC=O


substrate_name: D,L-glyceraldehyde


substrate_name: glucose

substrate: glucose


substrate_name: all-trans-retinal


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


organism: Mus musculus

proof_lines: kcat is 1.3 sec(-1) for D,L-glyceraldehyde as substrate. kcat is 0.95 sec(-1) for D-xylose as substrate. kcat is 0.9 sec(-1) for D-glucose as substrate. kcat is 1.1 sec(-1) for D-galactose as substrate. kcat is 0.9 sec(-1) for D-glucuronate


enzyme_display_name: Aldo-keto reductase family 1 member A1

substrate_name: D,L glyceraldehyde

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

enzyme: Aldo-keto reductase family 1 member A1

substrate: D,L glyceraldehyde


substrate_name: D-glucuronic acid

substrate: D-glucuronic acid


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


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


substrate_name: D-glucurono-gamma-lactone

substrate: D-glucurono-gamma-lactone


substrate_name: D-xylose

substrate: D-xylose


substrate_name: D-glucose

substrate: D-glucose


substrate_name: D-glucuronate

substrate: D-glucuronate


enzyme_display_name: gluconate 5-dehydrogenase

substrate_name: NADPH

enzyme: gluconate 5-dehydrogenase

substrate: NADPH


substrate_name: NADP+

substrate: NADP+


substrate_name: D-gluconate

substrate: D-gluconate


substrate: acrolein


enzyme_display_name: Sorbitol dehydrogenase

substrate_name: xylitol (at pH 10.0)

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

assay_conditions_summary: pH 10; cofactor NAD+

column_label: Table III; row label: xylitol; pH column: 10.0; metric: Km; raw value: 2.2 x 10^-4; raw unit: M; normalized value: 0.22; normalized unit: mM.

normalized_value_unit_evidence: Km 0.22 mM

raw_value_unit_evidence: Table III Km column reports 2.2 x 10^-4 M for xylitol at pH 10.0.

row_label: xylitol

table_label: Table III: Steady-State Kinetic Parameters for Human Liver Sorbitol Dehydrogenase

enzyme: Sorbitol dehydrogenase

substrate: xylitol (at pH 10.0)


substrate_name: L-threitol (at pH 10.0)

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

column_label: Table III; row label: L-threitol; pH column: 10.0; metric: Km; raw value: 2.7 x 10^-3; raw unit: M; normalized value: 2.7; normalized unit: mM.

normalized_value_unit_evidence: Km 2.7 mM

raw_value_unit_evidence: Table III Km column reports 2.7 x 10^-3 M for L-threitol at pH 10.0.

row_label: L-threitol

substrate: L-threitol (at pH 10.0)


substrate_name: (2R,3R)-2,3-butanediol (at pH 10.0)

smiles: CC(C(C)O)O

column_label: Table III; row label: (2R,3R)-2,3-butanediol; pH column: 10.0; metric: Km; raw value: 9.5 x 10^-3; raw unit: M; normalized value: 9.5; normalized unit: mM.

normalized_value_unit_evidence: Km 9.5 mM

raw_value_unit_evidence: Table III Km column reports 9.5 x 10^-3 M for (2R,3R)-2,3-butanediol at pH 10.0.

substrate: (2R,3R)-2,3-butanediol (at pH 10.0)


substrate_name: D-fructose (at pH 7.1)

assay_conditions_summary: pH 7.1; cofactor NADH

column_label: Table III; row label: D-fructose; pH column: 7.1; metric: Km; raw value: 0.14; raw unit: M; normalized value: 140; normalized unit: mM.

normalized_value_unit_evidence: Km 140 mM

raw_value_unit_evidence: Table III Km column reports 0.14 M for D-fructose at pH 7.1.

row_label: D-fructose

substrate: D-fructose (at pH 7.1)


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: androsterone

proof_lines: kcat is 7.6 min(-1) with androsterone as substrate. kcat is 4.3 min(-1) with 20beta-hydroxyprogesterone as substrate. kcat is 1.2 min(-1) with progesterone as substrate.

substrate: androsterone


substrate_name: progesterone

substrate: progesterone


enzyme_display_name: alcohol dehydrogenase [NAD(P)+]

organism: Saccharomyces cerevisiae

substrate_name: Butanal

smiles: CCCC=O

enzyme: alcohol dehydrogenase [NAD(P)+]

substrate: Butanal


substrate_name: ethanol

smiles: CCO

substrate: ethanol


smiles: CCCCCCCCO


smiles: CCCCCCO


smiles: CCCCO


smiles: CCCCCO


organism: Acinetobacter calcoaceticus


smiles: CCCCCCCO


substrate_name: benzyl alcohol

substrate: benzyl alcohol


organism: Pyrococcus horikoshii

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+

proof_lines: substrates NAD+ and 1-butanol, pH 9.0, 30°C


substrate_name: NAD+

substrate: NAD+


assay_conditions_summary: pH 5.5; 303.15 K; cofactor NADH

proof_lines: substrates NADH and butanal, pH 5.5, 30°C


substrate_name: propanal

smiles: CCC=O

proof_lines: substrates NADH and propanal, pH 5.5, 30°C

substrate: propanal


substrate_name: pentanal

smiles: CCCCC=O

proof_lines: substrates NADH and pentanal, pH 5.5, 30°C

substrate: pentanal


substrate_name: NADH

substrate: NADH


assay_conditions_summary: pH 5.5; 303.15 K; cofactor NADPH

proof_lines: substrates NADPH and butanal, pH 5.5, 30°C

substrate: NADPH


organism: Thermococcus sibiricus

smiles: CC(C)O


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


assay_conditions_summary: pH 7.5; 333.15 K; cofactor NADPH

proof_lines: 60°C, pH 7.5, cosubstrate: pyruvaldehyde


substrate_name: Pyruvaldehyde

substrate: Pyruvaldehyde


smiles: CC(CCC(C)O)O


organism: Acetivibrio thermocellus

substrate_name: acetaldehyde

smiles: CC=O

assay_conditions_summary: pH 7; 328.15 K; cofactor NADPH

proof_lines: cosubstrate NADPH, moderately ethanol producing strain, pH 7.0, 55°C

proof_lines: cosubstrate NADH, moderately ethanol producing strain, pH 7.0, 55°C

substrate: acetaldehyde


assay_conditions_summary: pH 7; 328.15 K; cofactor NADH

proof_lines: moderately ethanol producing strain, pH 7.0, 55°C


substrate_name: NADPH


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


substrate_name: NADP+

assay_conditions_summary: pH 9; 303.15 K; cofactor NADP+

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

substrate: NADP+


substrate_name: Cyclohexanol

assay_conditions_summary: pH 9; 303.15 K; cofactor NADPH

substrate: Cyclohexanol


substrate_name: cyclohexanone

substrate: cyclohexanone


substrate_name: benzaldehyde

substrate: benzaldehyde


organism: Haloferax volcanii

assay_conditions_summary: pH 6; cofactor NADPH

proof_lines: pH 6.0, temperature not specified in the publication


assay_conditions_summary: pH 10; cofactor NADP+

proof_lines: pH 10.0, temperature not specified in the publication


assay_conditions_summary: pH 10


assay_conditions_summary: pH 6


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

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


assay_conditions_summary: pH 6; cofactor NADP+


substrate_name: acetoin

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


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).


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.


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+)

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


organism: Gluconacetobacter liquefaciens


substrate_name: D-gluconate

substrate: D-gluconate


organism: Halobacterium sp.

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

row_label: NADPH

table_label: Table 2: Kinetics of His-HsADH2


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.


substrate_name: ethanol

smiles: CCO

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

row_label: Ethanol

substrate: 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


assay_conditions_summary: pH 10.5; 333.15 K; cofactor NADP+

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


substrate_name: D-xylose

substrate: D-xylose


organism: Oryctolagus cuniculus

substrate_name: H+; D-Glyceraldehyde; NADPH

substrate: H+; D-Glyceraldehyde; NADPH


substrate: NADPH


organism: Haloarcula marismortui


enzyme_display_name: octanol dehydrogenase

organism: Saccharomyces cerevisiae

substrate_name: NAD+

enzyme: octanol dehydrogenase

substrate: NAD+


smiles: CCCCCCCCO


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

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.


substrate_name: NADP+

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

substrate: NADP+


organism: Lactobacillus delbrueckii

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


organism: Rattus norvegicus


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

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


substrate_name: menadione

substrate: menadione


substrate_name: 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


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH


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.


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_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)


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

substrate: S-nitroso-CoA


substrate_name: D,L-glyceraldehyde

substrate: D,L-glyceraldehyde


enzyme_display_name: ribitol 2-dehydrogenase

organism: Cereibacter sphaeroides

substrate_name: NAD+

assay_conditions_summary: pH 9; 303.15 K; cofactor NAD+


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


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

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


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.


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


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


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

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


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).

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

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

smiles: O=CC(=O)O

enzyme: glyoxylate reductase (NADP(+))

substrate: glyoxylate


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+

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

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


enzyme_display_name: Aldo-keto reductase family 1 member C3

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

enzyme: Aldo-keto reductase family 1 member C3

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.


enzyme_display_name: Aldo-keto reductase family 1 member C4

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

enzyme: Aldo-keto reductase family 1 member C4


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).

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


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: hydroxypyruvate reductase


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


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


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

enzyme: hydroxypyruvate reductase


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