substrate_name: testosterone (at 37 degrees Celsius)

column_label: Table 2 row Testosterone; KM (uM) = 30; Vmax = 238 mU/mg; corresponding ketosteroid = 4-Androstene-3,17-dione.

raw_value_unit_evidence: KM column reports 30 uM.

row_label: Testosterone

substrate: testosterone (at 37 degrees Celsius)


enzyme_display_name: Dehydrogenase/reductase SDR family member 11

organism: Homo sapiens

substrate_name: 5-alpha-androstane-3-alpha,17-beta-diol (at 37 degrees Celsius)

source_db: uniprot

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

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

data_origin: experimental

source: uniprot


substrate_name: isolithocholic acid (at 37 degrees Celsius)

verification_status: verified

assay_conditions_summary: cofactor NADP+

column_label: Table 2 row Isolithocholic acid; KM (uM) = 0.4; Vmax = 28 mU/mg; corresponding ketosteroid = Dehydrolithocholic acid.

raw_value_unit_evidence: KM column reports 0.4 uM.

row_label: Isolithocholic acid

table_label: Table 2. Substrate specificity for hydroxysteroids.

enzyme: Dehydrogenase/reductase SDR family member 11

status: verified


substrate_name: 1-phenyl-1,2-propanedione (at 37 degrees Celsius)

assay_conditions_summary: cofactor NADPH

column_label: Table 3 row 1-Phenyl-1,2-propanedione; KM (uM) = 60; Vmax = 69 mU/mg; Vmax/KM = 1.2 mU/mg/uM.

raw_value_unit_evidence: KM column reports 60 uM.

table_label: Table 3. Substrate specificity for nonsteroidal carbonyl compounds.


substrate_name: 2,3-hexanedione (at 37 degrees Celsius)

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

column_label: Table 3 row 2,3-Hexanedione; KM (uM) = 620; Vmax = 331 mU/mg; Vmax/KM = 0.53 mU/mg/uM.

raw_value_unit_evidence: KM column reports 620 uM.

substrate: 2,3-hexanedione (at 37 degrees Celsius)


enzyme_display_name: 17beta-estradiol 17-dehydrogenase

organism: Rattus norvegicus

source_db: oed

kcat_over_km_origin: calculated

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

column_label: Table 1 row 2-Cyclohexen-1-ol, Rat 17HSD5 columns. Current quotient 0.008285714285714287 lies in the printed-efficiency precision interval [0.0075, 0.009166666666666667].

normalized_value_unit_evidence: Current stored-precision tuple: Km 7.0 mM; kcat 0.058 s^-1; same-row quotient 0.008285714285714287 s^-1 mM^-1. The independently printed efficiency normalizes to 0.008333333333333333 s^-1 mM^-1 and remains separately preserved.

raw_value_unit_evidence: Table 1 rat 17HSD5 cells for 2-Cyclohexen-1-ol: Km 7,000 uM; kcat 3.5 min^-1; independently printed kcat/Km 0.0005 min^-1 uM^-1.

table_label: Table 1. Substrate specificity for non-steroidal substrates

enzyme: 17beta-estradiol 17-dehydrogenase

source: oed


substrate_name: Dimethylglyoxal

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

column_label: PMID 16788056 Table 1. Substrate specificity for non-steroidal substrates in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5; row 2,3-Butanedione / Rat 17HSD5 (Table 1, Reduction); Rat 17HSD5 column group, sub-columns Km, kcat and kcat/Km; printed cells Km 126 uM, kcat 16 min^-1, kcat/Km 0.13 min^-1 uM^-1. The exported kcat/Km is recorded as the quotient of this same row's own two printed cells as stored (0.267 s^-1 / 0.126 mM = 2.119047619047619 s^-1 mM^-1), not as the paper's two-decimal printed kcat/Km cell (0.13 min^-1 uM^-1), which agrees with that quotient at the printed cell's precision.

normalized_value_unit_evidence: metric: Km; normalized value: 0.126 mM; metric: kcat; normalized value: 0.267 s^-1; metric: kcat/Km; normalized value: 2.119047619047619 s^-1 mM^-1; assay condition: pH 7.4; rat 17HSD5 column group; NADP(H) coenzyme per the Table 1 footnote; reduction reaction; wild-type recombinant enzyme; no mutation

raw_value_unit_evidence: Table row as printed: Km 126 uM; kcat 16 min^-1; kcat/Km 0.13 min^-1 uM^-1 (Rat 17HSD5 column group).

substrate: Dimethylglyoxal


column_label: Table 2 row 17b-Estradiol, Rat 17HSD5 columns. Current quotient 29.785714285714285 lies in the printed-efficiency precision interval [29.166666666666668, 30.833333333333332].

normalized_value_unit_evidence: Current stored-precision tuple: Km 0.014 mM; kcat 0.417 s^-1; same-row quotient 29.785714285714285 s^-1 mM^-1. The independently printed efficiency normalizes to 30.0 s^-1 mM^-1 and remains separately preserved.

raw_value_unit_evidence: Table 2 rat 17HSD5 cells for 17b-Estradiol: Km 14 uM; kcat 25 min^-1; independently printed kcat/Km 1.8 min^-1 uM^-1.

table_label: Table 2. Substrate specificity for steroids


substrate_name: Isatin

verification_status: corrected

column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 2, substrate `Isatin`, Rat 17HSD5 column group: Km = 2.1 uM (normalized 0.0021000000000000003 mM); kcat = 11 min-1 (normalized 0.18333333333333332 s^-1); kcat/Km = 5.2 min-1 uM-1 (normalized 86.66666666666667 s^-1 mM^-1).

table_label: Table 1 (journal page 1058) 'Substrate specificity for non-steroidal substrates in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5', decoded plain-numeral transcription

substrate: Isatin

status: corrected


substrate_name: NAD+

verification_status: unverified

proof_lines:
NAD+
preferred coenzyme
pH 7.4

substrate: NAD+

status: unverified


substrate_name: NADH

proof_lines:
NAD+
preferred coenzyme
TBER1

substrate: NADH


substrate_name: NADPH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH

substrate: NADPH


substrate_name: p-Nitrobenzaldehyde

column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 7, substrate `4-Nitrobenzaldehyde`, Rat 17HSD5 column group: Km = 11 uM (normalized 0.011 mM); kcat = 7.9 min-1 (normalized 0.13166666666666668 s^-1); kcat/Km = 0.72 min-1 uM-1 (normalized 12.0 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 7.9 min-1 / 60 = 0.13166666666666668 s^-1; the catalog holds 0.132 s^(-1). Km: printed cell 11 uM / 1000 = 0.011 mM; the catalog holds 0.011 mM. kcat/Km: the paper prints the cell 0.72 min-1 uM-1, which is 0.72 x 1000 / 60 = 12.0 s^-1 mM^-1; the catalog holds 12.000000000000002 s^(-1)*mM^(-1).

substrate: p-Nitrobenzaldehyde


column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Oxidation, printed row 2, substrate `S-Indan-1-ol`, Rat 17HSD5 column group: Km = 3080 uM (normalized 3.08 mM); kcat = 6.8 min-1 (normalized 0.11333333333333333 s^-1); kcat/Km = 0.002 min-1 uM-1 (normalized 0.03333333333333334 s^-1 mM^-1).


column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Oxidation, printed row 3, substrate `trans-Benzene dihydrodiol`, Rat 17HSD5 column group: Km = 2300 uM (normalized 2.3000000000000003 mM); kcat = 4.1 min-1 (normalized 0.06833333333333333 s^-1); kcat/Km = 0.002 min-1 uM-1 (normalized 0.03333333333333334 s^-1 mM^-1).


substrate_name: 2,3-heptanedione (at 37 degrees Celsius)

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

assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 3; row alpha-Dicarbonyl compounds / 2,3-Heptanedione; Km column

normalized_value_unit_evidence: Km=0.201 mM converted from 201 uM

raw_value_unit_evidence: Table 3 alpha-Dicarbonyl compounds / 2,3-Heptanedione Km 201 uM

table_label: Table 3


substrate_name: 3,4-hexanedione (at 37 degrees Celsius)

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

column_label: Table 3; row alpha-Dicarbonyl compounds / 3,4-Hexanedione; Km column

normalized_value_unit_evidence: Km=0.42 mM converted from 420 uM

raw_value_unit_evidence: Table 3 alpha-Dicarbonyl compounds / 3,4-Hexanedione Km 420 uM

substrate: 3,4-hexanedione (at 37 degrees Celsius)


substrate_name: alpha-tetralone (at 37 degrees Celsius)

column_label: Table 3; row Alicyclic ketones / alpha-Tetralone; Km column

normalized_value_unit_evidence: Km=0.178 mM converted from 178 uM

raw_value_unit_evidence: Table 3 Alicyclic ketones / alpha-Tetralone Km 178 uM

row_label: Alicyclic ketones / alpha-Tetralone

substrate: alpha-tetralone (at 37 degrees Celsius)


substrate_name: loxoprofen (at 37 degrees Celsius)

column_label: Table 3; row Alicyclic ketones / Loxoprofen; Km column

normalized_value_unit_evidence: Km=0.74 mM converted from 740 uM

raw_value_unit_evidence: Table 3 Alicyclic ketones / Loxoprofen Km 740 uM

row_label: Alicyclic ketones / Loxoprofen

substrate: loxoprofen (at 37 degrees Celsius)


proof_lines: NADPH coenzyme DHRS11


substrate_name: estrone (at 37 degrees Celsius)

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 1; row 17-Ketosteroids / Estrone; Km column

normalized_value_unit_evidence: Km=0.0007 mM converted from 0.7 uM

raw_value_unit_evidence: Table 1 17-Ketosteroids / Estrone Km 0.7 uM

row_label: 17-Ketosteroids / Estrone

table_label: Table 1

substrate: estrone (at 37 degrees Celsius)


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


substrate_name: dehydroepiandrosterone (DHEA) (at 37 degrees Celsius)


substrate_name: DHEA sulfate (at 37 degrees Celsius)

substrate: DHEA sulfate (at 37 degrees Celsius)


substrate_name: dehydrolithocholic acid (at 37 degrees Celsius)


substrate_name: 20-alpha-hydroxyprogesterone (at 37 degrees Celsius)


substrate_name: taurodehydrocholic acid (at 37 degrees Celsius)


substrate_name: dehydrocholic acid (at 37 degrees Celsius)


substrate_name: 5-beta-dihydrotestosterone (DHT) (at 37 degrees Celsius)


enzyme_display_name: mannitol 2-dehydrogenase

organism: Pseudomonas fluorescens

substrate_name: meso-erythritol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N300S to reconstruct the assayed variant sequence.

mutation_type: substitution

enzyme: mannitol 2-dehydrogenase

substrate: meso-erythritol


substrate_name: D-Arabitol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature H303A to reconstruct the assayed variant sequence.

column_label: Table 2; row label H303A; substrate D-Arabitol; checked column(s): kcat, km, kcat_over_km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm

table_label: Table 2

substrate: D-Arabitol


sequence_variant_note: Resolved canonical sequence from uniprotkb:O08355 and applied mutation signature H303A/R373A/K381A to reconstruct the assayed variant sequence.

column_label: Table 2; row label H303A/R373A/K381A; substrate D-Arabitol; checked column(s): kcat, km, kcat_over_km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K381A with inferred residue-numbering offset +3 to reconstruct the assayed variant sequence.

column_label: Table 2; row label K381A; substrate D-Arabitol; checked column(s): kcat_over_km, km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N191A with inferred residue-numbering offset +4 to reconstruct the assayed variant sequence.

column_label: Table 2; row label N191A; substrate D-Arabitol; checked column(s): km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N300A to reconstruct the assayed variant sequence.

column_label: Table 2; row label N300A; substrate D-Arabitol; checked column(s): kcat_over_km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprotkb:O08355 and applied mutation signature N300D to reconstruct the assayed variant sequence.

column_label: Table 2; row label N300D; substrate D-Arabitol; checked column(s): kcat, km, kcat_over_km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


column_label: Table 2; row label N300S; substrate D-Arabitol; checked column(s): kcat, km, kcat_over_km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R373A with inferred residue-numbering offset -12 to reconstruct the assayed variant sequence.

column_label: Table 2; row label R373A; substrate D-Arabitol; checked column(s): km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


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 CoA

proof_lines:
17beta-HSD10
Drosophila melanogaster
hydroxyacyl-CoA dehydrogenase

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


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

assay_conditions_summary: pH 9.3; cofactor CoA


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


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)

assay_conditions_summary: pH 6.4; cofactor NADH


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


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

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


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)


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: 17-beta-hydroxysteroid dehydrogenase type 2

substrate_name: estradiol

assay_conditions_summary: pH 7.4; cofactor NAD+

column_label: Table I, row Estradiol -> Estrone; NAD+, column K_m (uM).

normalized_value_unit_evidence: Km=0.00021 mM converted from 0.21 uM.

raw_value_unit_evidence: Table I reports Estradiol -> Estrone; NAD+ Km=0.21 +/- 0.04 uM.

row_label: Estradiol -> Estrone; NAD+

table_label: Table I: Characterization in vitro of human 17beta-HSD type 2 expressed in transfected 293 cells

substrate: estradiol


substrate_name: testosterone

column_label: Table I, row Testosterone -> Androstenedione; NAD+, column K_m (uM).

normalized_value_unit_evidence: Km=0.00039 mM converted from 0.39 uM.

raw_value_unit_evidence: Table I reports Testosterone -> Androstenedione; NAD+ Km=0.39 +/- 0.09 uM.

row_label: Testosterone -> Androstenedione; NAD+

enzyme: 17-beta-hydroxysteroid dehydrogenase type 2

substrate: testosterone


substrate_name: dihydrotestosterone

column_label: Table III row Dihydrotestosterone / cofactor NAD / Km app column = 0.25 +/- 0.11 uM.

row_label: Dihydrotestosterone row; cofactor NAD

table_label: Table III. Kinetic constants of substrates in the oxidation reaction with purified reconstituted His6-tagged 17beta-HSD2

substrate: dihydrotestosterone


column_label: Table III row 20alpha-Dihydroprogesterone P / cofactor NAD / Km app column = 0.53 +/- 0.22 uM.

row_label: 20alpha-Dihydroprogesterone P row; cofactor NAD


substrate_name: androstenedione

assay_conditions_summary: pH 7.4; cofactor NADH

column_label: Table I, row Androstenedione -> Testosterone; NADH, column K_m (uM).

normalized_value_unit_evidence: Km=0.00263 mM converted from 2.63 uM.

raw_value_unit_evidence: Table I reports Androstenedione -> Testosterone; NADH Km=2.63 +/- 0.20 uM.

row_label: Androstenedione -> Testosterone; NADH

substrate: androstenedione


substrate_name: estrone

column_label: Table I, row Estrone -> Estradiol; NADH, column K_m (uM).

normalized_value_unit_evidence: Km=0.00078 mM converted from 0.78 uM.

raw_value_unit_evidence: Table I reports Estrone -> Estradiol; NADH Km=0.78 +/- 0.08 uM.

row_label: Estrone -> Estradiol; NADH

substrate: estrone


assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADP+

column_label: Table 2, row 17beta-Estradiol, columns Km, kcat, kcat/Km; unit header row: Km uM; kcat min^-1; kcat/Km uM^-1 min^-1

normalized_value_unit_evidence: Km normalized_value=0.0091 normalized_unit=mM; kcat normalized_value=0.008333333333333333333333333333 normalized_unit=s^-1; kcat_over_km normalized_value=1 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Table 2 (Oxidative reactions), row 17beta-Estradiol: Km 9.1 +/- 1.2 uM; kcat 0.5 +/- 0.1 min^-1; kcat/Km 0.06 uM^-1 min^-1


substrate_name: 5alpha-androstane 3alpha,17beta-diol

column_label: Table 2, row 3alpha,17beta-Androstandiol, columns Km, kcat, kcat/Km; unit header row: Km uM; kcat min^-1; kcat/Km uM^-1 min^-1

normalized_value_unit_evidence: Km normalized_value=0.0192 normalized_unit=mM; kcat normalized_value=0.05 normalized_unit=s^-1; kcat_over_km normalized_value=2.666666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Table 2 (Oxidative reactions), row 3alpha,17beta-Androstandiol: Km 19.2 +/- 2.3 uM; kcat 3.0 +/- 0.3 min^-1; kcat/Km 0.16 uM^-1 min^-1

substrate: 5alpha-androstane 3alpha,17beta-diol


substrate_name: androsterone

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

column_label: Table 2, row Androsterone, columns Km, kcat, kcat/Km; unit header row: Km uM; kcat min^-1; kcat/Km uM^-1 min^-1

normalized_value_unit_evidence: Km normalized_value=0.0028 normalized_unit=mM; kcat normalized_value=0.02833333333333333333333333333 normalized_unit=s^-1; kcat_over_km normalized_value=10.16666666666666666666666667 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Table 2 (Reductive reactions), row Androsterone: Km 2.8 +/- 0.2 uM; kcat 1.7 +/- 0.1 min^-1; kcat/Km 0.61 uM^-1 min^-1

row_label: Androsterone

substrate: androsterone


column_label: Table 2, row Delta4-Androstenedione, columns Km, kcat, kcat/Km; unit header row: Km uM; kcat min^-1; kcat/Km uM^-1 min^-1

normalized_value_unit_evidence: Km normalized_value=0.0019 normalized_unit=mM; kcat normalized_value=0.01833333333333333333333333333 normalized_unit=s^-1; kcat_over_km normalized_value=10 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Table 2 (Reductive reactions), row Delta4-Androstenedione: Km 1.9 +/- 0.2 uM; kcat 1.1 +/- 0.1 min^-1; kcat/Km 0.60 uM^-1 min^-1


column_label: Table 2, row Testosterone, columns Km, kcat, kcat/Km; unit header row: Km uM; kcat min^-1; kcat/Km uM^-1 min^-1

normalized_value_unit_evidence: Km normalized_value=0.0071 normalized_unit=mM; kcat normalized_value=0.01 normalized_unit=s^-1; kcat_over_km normalized_value=1.5 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Table 2 (Oxidative reactions), row Testosterone: Km 7.1 +/- 1.5 uM; kcat 0.6 +/- 0.1 min^-1; kcat/Km 0.09 uM^-1 min^-1


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

substrate_name: 10-OH-decanoic acid (with 0.1 M sodium phosphate at pH 7.5)

smiles: C(CCCCC(=O)O)CCCCO

column_label: Table 1, row 10-OH-Decanoic acid, column Km (mM).

raw_value_unit_evidence: Table 1 reports 10-OH-Decanoic acid Km=0.1 mM.

row_label: 10-OH-Decanoic acid

table_label: Table 1: Kinetic constants of human class IV ADH with gamma-hydroxyfatty acids and products of lipid peroxidation


substrate_name: hexanol (with 0.1 M sodium phosphate at pH 7.5)

smiles: CCCCCCO

column_label: Table 1, row Hexanol, column Km (mM).

raw_value_unit_evidence: Table 1 reports Hexanol Km=0.14 mM.

row_label: Hexanol

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


substrate_name: hexanal (with 0.1 M sodium phosphate at pH 7.5)

smiles: CCCCCC=O

column_label: Table 1, row Hexanal, column Km (mM).

raw_value_unit_evidence: Table 1 reports Hexanal Km=0.02 mM.

row_label: Hexanal


substrate_name: 2-hexenol (with 0.1 M sodium phosphate at pH 7.5)

smiles: CCCC=CCO

column_label: Table 1, row 2-Hexenol, column Km (mM).

raw_value_unit_evidence: Table 1 reports 2-Hexenol Km=0.017 mM.


substrate_name: 2-hexenal (with 0.1 M sodium phosphate at pH 7.5)

smiles: CCCC=CC=O

column_label: Table 1, row 2-Hexenal, column Km (mM).

raw_value_unit_evidence: Table 1 reports 2-Hexenal Km=0.025 mM.


substrate_name: 4-hydroxynonenal (with 0.1 M sodium phosphate at pH 7.5)

smiles: CCCCCC(C=CC=O)O

column_label: Table 1, row 4-Hydroxynonenal, column Km (mM).

raw_value_unit_evidence: Table 1 reports 4-Hydroxynonenal Km=0.038 mM.


enzyme_display_name: pyridoxine 4-dehydrogenase

organism: Schizosaccharomyces pombe

proof_lines: Schizosaccharomyces pombe pyridoxal reductase

enzyme: pyridoxine 4-dehydrogenase


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH


substrate_name: p-Nitrobenzaldehyde


substrate_name: Pyridoxal

substrate: Pyridoxal


substrate_name: all-trans-retinol

column_label: PMC full-text HTML for PMID 16787387; Table 1 'Kinetic constants of purified AKR, MDR and SDR enzymes with retinoids'; row All-trans-Retinol / Km (uM); ADH4 column=0.3+/-0.03.

raw_value_unit_evidence: PMID 16787387 Table 1 reports ADH4 / All-trans-Retinol: Km=0.3+/-0.03 uM and kcat=190+/-6 min^-1.

row_label: All-trans-Retinol; ADH4 column

substrate: all-trans-retinol


assay_conditions_summary: pH 7.5; cofactor NAD+

column_label: Table 1 row 3,4-Didehydroretinol, ADH4 Km column: 28 +/- 7 uM.

raw_value_unit_evidence: Km raw_value=28 +/- 7 uM raw_unit=uM

row_label: 3,4-Didehydroretinol / ADH4 Km

table_label: Table 1, Kinetic constants of human alcohol dehydrogenases with retinoids


substrate_name: all-trans-retinal

column_label: PMC full-text HTML for PMID 16787387; Table 1 'Kinetic constants of purified AKR, MDR and SDR enzymes with retinoids'; row All-trans-Retinaldehyde / Km (uM); ADH4 column=0.8+/-0.1.

raw_value_unit_evidence: PMID 16787387 Table 1 reports ADH4 / All-trans-Retinaldehyde: Km=0.8+/-0.1 uM and kcat=300+/-10 min^-1.

row_label: All-trans-Retinaldehyde; ADH4 column

substrate: all-trans-retinal


assay_conditions_summary: pH 7.5; cofactor NADH

column_label: Table 1 row 3,4-Didehydroretinal, ADH4 Km column: 26 +/- 6 uM.

raw_value_unit_evidence: Km raw_value=26 +/- 6 uM raw_unit=uM

row_label: 3,4-Didehydroretinal / ADH4 Km


enzyme_display_name: 4-hydroxybutyrate dehydrogenase

organism: Clostridium kluyveri

source_db: brenda

sequence_source: multiple

column_label: The official abstract states that in the reverse direction the Km values were 670 +/- 80 uM and 55 +/- 16 mM for NAD and 4-hydroxybutanoate, respectively.

raw_value_unit_evidence: Km raw_value=55 +/- 16 raw_unit=mM

table_label: Official ScienceDirect abstract kinetic summary for purified 4-hydroxybutanoate dehydrogenase

source_databases_merged: brenda uniprot

enzyme: 4-hydroxybutyrate dehydrogenase

source: brenda


substrate_name: NADH

assay_conditions_summary: pH 6.1; cofactor NADH

column_label: The official abstract states Km values for NADH and succinic semialdehyde were 150 +/- 20 uM and 560 +/- 80 uM, respectively.

raw_value_unit_evidence: Km raw_value=150 +/- 20 raw_unit=uM

row_label: NADH

substrate: NADH


substrate_name: succinate semialdehyde

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

raw_value_unit_evidence: Km raw_value=560 +/- 80 raw_unit=uM

row_label: succinic semialdehyde

substrate: succinate semialdehyde


substrate_name: NAD+

assay_conditions_summary: pH 9.4; cofactor NAD+

raw_value_unit_evidence: Km raw_value=670 +/- 80 raw_unit=uM

row_label: NAD

substrate: NAD+


organism: Aspergillus fumigatus

substrate_name: D-arabinitol

column_label: Table label: Table 1: AfM2DH substrate rows. Row: AfM2DH | D-Arabinitol. Enzyme column group: AfM2DH. Columns read: kcat (s^-1) cell 162, Km (mM) cell 163, kcat/Km (s^-1 mM^-1) cell 0.99. metric: kcat; raw value: 162; raw unit: s^-1; normalized value: 162.0 s^(-1); metric: Km; raw value: 163; raw unit: mM; normalized value: 163.0 mM; metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 0.9938650306748467 s^-1 mM^-1; assay condition: polyol oxidation at pH 10.0; companion Table 2 measurements at 25 C. Export row conditions: pH 10.0; 298.15 K.

normalized_value_unit_evidence: AfM2DH row D-Arabinitol of Table 1: kcat 162 s^-1 = 162.0 s^(-1) (no conversion needed); Km 163 mM = 163.0 mM (already in the export unit mM); kcat/Km 0.9938650306748467 s^-1 mM^-1 is the quotient of this row's own cells, 162 s^-1 / 163 mM = 0.9938650306748467 s^-1 mM^-1. The paper also prints a rounded kcat/Km cell for this row, 0.99 +/- 0.08 s^-1 mM^-1; the quotient rounds to that printed cell at the printed cell's own precision (two decimal places), so the two agree and the disagreement is printed precision only.

raw_value_unit_evidence: Table 1: AfM2DH substrate rows | row: D-Arabinitol, polyol oxidation at pH 10.0: kcat `162 +/- 5 s^-1`; Km `163 +/- 13 mM`; kcat/Km `0.99 +/- 0.08 s^-1 mM^-1`. | AfM2DH cells read: kcat = 162 s^-1; Km = 163 mM; kcat/Km = 0.99 s^-1 mM^-1

row_label: AfM2DH | D-Arabinitol

table_label: Table 1: AfM2DH substrate rows

substrate: D-arabinitol


substrate_name: D-fructose

substrate: D-fructose


substrate_name: D-mannitol

substrate: D-mannitol


substrate_name: D-Xylulose

column_label: Table label: Table 1: AfM2DH substrate rows. Row: AfM2DH | D-Xylulose. Enzyme column group: AfM2DH. Columns read: kcat (s^-1) cell 64, open-chain-corrected Km (mM) cell 1.7, corrected kcat/Km (s^-1 mM^-1) cell 39. metric: kcat; raw value: 64; raw unit: s^-1; normalized value: 64.0 s^(-1); metric: Km; raw value: 1.7; raw unit: mM; normalized value: 1.7 mM; metric: kcat/Km; raw value: 39 +/- 2; raw unit: s^-1 mM^-1; normalized value: 39 s^-1 mM^-1; explicit printed primary cell; assay condition: ketose reduction at pH 7.1, Km and kcat/Km corrected for the available open-chain form of the carbonyl substrate; companion Table 2 measurements at 25 C and pH 7.1. Export row conditions: pH 7.1; 298.15 K.

normalized_value_unit_evidence: kcat raw 64 s^-1 -> 64.0 s^(-1); Km raw 1.7 mM -> 1.7 mM; explicit printed kcat/Km raw 39 +/- 2 s^-1 mM^-1 -> 39 s^-1 mM^-1. Conversion: 39 s^-1 mM^-1 requires no unit conversion. The normalized ratio is taken directly from the printed primary cell, not recomputed from kcat and Km.

raw_value_unit_evidence: Table 1: AfM2DH substrate rows | row: D-Xylulose, ketose reduction at pH 7.1: kcat `64 +/- 1 s^-1`; open-chain-corrected Km `1.7 +/- 0.1 mM`; corrected kcat/Km `39 +/- 2 s^-1 mM^-1`. | AfM2DH cells read: kcat = 64 s^-1; open-chain-corrected Km = 1.7 mM; corrected kcat/Km = 39 s^-1 mM^-1

row_label: AfM2DH | D-Xylulose

substrate: D-Xylulose


substrate_name: L-Sorbitol

proof_lines:
AfM2DH
D-mannitol oxidation
D-fructose reduction

substrate: L-Sorbitol


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O08355 and applied mutation signature N191A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 10; 298.15 K; buffer a three-component MES/Tris/glycine; cofactor NAD+

column_label: Table 1 (Kinetic parameters for site-directed mutants of PfM2DH), enzyme column N191A: row kcatO (s^-1) = 2.78; row KNAD+ (uM) = 310; row kcatO/KNAD+ (M^-1 s^-1) = 8968.

normalized_value_unit_evidence: Km: printed Table 1 KNAD+ cell 310 uM; 310 / 1000 = 0.31 mM; the exported value is 0.31 mM. kcat: printed Table 1 kcatO cell 2.78 s^-1; the row head prints s^-1, so no unit conversion applies and the exported value is 2.78 s^(-1). kcat/Km: printed Table 1 kcatO/KNAD+ cell 8968 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 8.968 s^-1 mM^-1. Quotient disclosure for this column: 2.78 / 0.31 = 8.96774193548387 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the four significant figures Table 1 prints for it.

raw_value_unit_evidence: Table 1, enzyme column N191A: kcatO = 2.78 s^-1; KNAD+ = 310 uM; printed kcatO/KNAD+ = 8968 M^-1 s^-1.

row_label: Table 1, N191A column, coenzyme rows of the mannitol-oxidation block (kcatO, KNAD+, kcatO/KNAD+)

table_label: Table 1: Kinetic parameters for site-directed mutants of PfM2DH (Biochem. J. 2010, volume 425, pages 455-463); one kinetic parameter per printed row and one enzyme per printed column; the coenzyme rows print KNAD+ and KNADH in uM, kcatO and kcatR in s^-1 and kcatO/KNAD+ and kcatR/KNADH in M^-1 s^-1


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O08355 and applied mutation signature N191A/N300A to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for site-directed mutants of PfM2DH), enzyme column N191A/N300A: row kcatO (s^-1) = 0.04; row KNAD+ (uM) = 314; row kcatO/KNAD+ (M^-1 s^-1) = 127.4.

normalized_value_unit_evidence: Km: printed Table 1 KNAD+ cell 314 uM; 314 / 1000 = 0.314 mM; the exported value is 0.314 mM. kcat: printed Table 1 kcatO cell 0.04 s^-1; the row head prints s^-1, so no unit conversion applies and the exported value is 0.04 s^(-1). kcat/Km: printed Table 1 kcatO/KNAD+ cell 127.4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 0.1274 s^-1 mM^-1. Quotient disclosure for this column: 0.04 / 0.314 = 0.12738853503184713 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the four significant figures Table 1 prints for it.

raw_value_unit_evidence: Table 1, enzyme column N191A/N300A: kcatO = 0.04 s^-1; KNAD+ = 314 uM; printed kcatO/KNAD+ = 127.4 M^-1 s^-1.

row_label: Table 1, N191A/N300A column, coenzyme rows of the mannitol-oxidation block (kcatO, KNAD+, kcatO/KNAD+)


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:O08355 and applied mutation signature N191L to reconstruct the assayed variant sequence.

column_label: Table 1 (Kinetic parameters for site-directed mutants of PfM2DH), enzyme column N191L: row kcatO (s^-1) = 0.55; row KNAD+ (uM) = 55; row kcatO/KNAD+ (M^-1 s^-1) = 9964.

normalized_value_unit_evidence: Km: printed Table 1 KNAD+ cell 55 uM; 55 / 1000 = 0.055 mM; the export stores 0.055 mM. kcat: printed Table 1 kcatO cell 0.55 s^-1; the row head prints s^-1, so no unit conversion applies; the export stores 0.55 s^(-1). kcat/Km: printed Table 1 kcatO/KNAD+ cell 9964 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 9964 / 1000 = 9.964 s^(-1)*mM^(-1). The export stores 10.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column N191L: kcatO = 0.55 s^-1; KNAD+ = 55 uM; printed kcatO/KNAD+ = 9964 M^-1 s^-1.

row_label: Table 1, N191L column, coenzyme rows of the mannitol-oxidation block (kcatO, KNAD+, kcatO/KNAD+)


column_label: Table 1 (Kinetic parameters for site-directed mutants of PfM2DH), enzyme column Wild-type: row kcatO (s^-1) = 40.0; row KNAD+ (uM) = 93; row kcatO/KNAD+ (M^-1 s^-1) = 4.0 x 10^5.

normalized_value_unit_evidence: Km: printed Table 1 KNAD+ cell 93 uM; 93 / 1000 = 0.093 mM; the export stores 0.093 mM. kcat: printed Table 1 kcatO cell 40.0 s^-1; the row head prints s^-1, so no unit conversion applies; the export stores 40.0 s^(-1). kcat/Km: printed Table 1 kcatO/KNAD+ cell 4.0 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 4.0 x 10^5 / 1000 = 400 s^(-1)*mM^(-1). The export stores 430.10752688172045 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column Wild-type: kcatO = 40.0 s^-1; KNAD+ = 93 uM; printed kcatO/KNAD+ = 4.0 x 10^5 M^-1 s^-1.

row_label: Table 1, Wild-type column, coenzyme rows of the mannitol-oxidation block (kcatO, KNAD+, kcatO/KNAD+)


assay_conditions_summary: pH 7.1; 298.15 K; buffer a three-component MES/Tris/glycine; cofactor NADH

column_label: Table 1 (Kinetic parameters for site-directed mutants of PfM2DH), enzyme column N191A: row kcatR (s^-1) = 0.56; row KNADH (uM) = 17; row kcatR/KNADH (M^-1 s^-1) = 3.2 x 10^4.

normalized_value_unit_evidence: Km: printed Table 1 KNADH cell 17 uM; 17 / 1000 = 0.017 mM; the export stores 0.017 mM. kcat: printed Table 1 kcatR cell 0.56 s^-1; the row head prints s^-1, so no unit conversion applies; the export stores 0.56 s^(-1). kcat/Km: printed Table 1 kcatR/KNADH cell 3.2 x 10^4 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 3.2 x 10^4 / 1000 = 32 s^(-1)*mM^(-1). The export stores 32.94117647058824 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 1, enzyme column N191A: kcatR = 0.56 s^-1; KNADH = 17 uM; printed kcatR/KNADH = 3.2 x 10^4 M^-1 s^-1.

row_label: Table 1, N191A column, coenzyme rows of the fructose-reduction block (kcatR, KNADH, kcatR/KNADH)


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N191A/N300A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NADH


column_label: Table 1 (Kinetic parameters for site-directed mutants of PfM2DH), enzyme column N191L: row kcatR (s^-1) = 0.55; row KNADH (uM) = 3.3; row kcatR/KNADH (M^-1 s^-1) = 1.7 x 10^5.

normalized_value_unit_evidence: Km: printed Table 1 KNADH cell 3.3 uM; 3.3 / 1000 = 0.0033 mM; the exported value is 0.0033 mM. kcat: printed Table 1 kcatR cell 0.55 s^-1; the row head prints s^-1, so no unit conversion applies and the exported value is 0.55 s^(-1). kcat/Km: printed Table 1 kcatR/KNADH cell 1.7 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 170 s^-1 mM^-1. Quotient disclosure for this column: 0.55 / 0.0033 = 166.66666666666669 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the two significant figures Table 1 prints for it.

raw_value_unit_evidence: Table 1, enzyme column N191L: kcatR = 0.55 s^-1; KNADH = 3.3 uM; printed kcatR/KNADH = 1.7 x 10^5 M^-1 s^-1.

row_label: Table 1, N191L column, coenzyme rows of the fructose-reduction block (kcatR, KNADH, kcatR/KNADH)


column_label: Table 1 (Kinetic parameters for site-directed mutants of PfM2DH), enzyme column Wild-type: row kcatR (s^-1) = 61; row KNADH (uM) = 67; row kcatR/KNADH (M^-1 s^-1) = 9.1 x 10^5.

normalized_value_unit_evidence: Km: printed Table 1 KNADH cell 67 uM; 67 / 1000 = 0.067 mM; the exported value is 0.067 mM. kcat: printed Table 1 kcatR cell 61 s^-1; the row head prints s^-1, so no unit conversion applies and the exported value is 61.0 s^(-1). kcat/Km: printed Table 1 kcatR/KNADH cell 9.1 x 10^5 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so the printed cell converts to 910 s^-1 mM^-1. Quotient disclosure for this column: 61 / 0.067 = 910.4477611940298 s^-1 mM^-1, which is the exported kcat_over_km; the printed efficiency cell is that same quotient carried to the two significant figures Table 1 prints for it.

raw_value_unit_evidence: Table 1, enzyme column Wild-type: kcatR = 61 s^-1; KNADH = 67 uM; printed kcatR/KNADH = 9.1 x 10^5 M^-1 s^-1.

row_label: Table 1, Wild-type column, coenzyme rows of the fructose-reduction block (kcatR, KNADH, kcatR/KNADH)


enzyme_display_name: Aldo-keto reductase family 1 member C3

organism: Bos taurus

substrate_name: prostaglandin D2

assay_conditions_summary: cofactor NADPH

column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / prostaglandin D2; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS prostaglandin D2 Km raw_value=100 raw_unit=uM

row_label: PGFS / prostaglandin D2

enzyme: Aldo-keto reductase family 1 member C3

substrate: prostaglandin D2


column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / 9,10-phenanthroquinone; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS 9,10-phenanthroquinone Km raw_value=0.13 raw_unit=uM

row_label: PGFS / 9,10-phenanthroquinone


substrate_name: menadione

column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / menadione; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS menadione Km raw_value=13 raw_unit=uM

row_label: PGFS / menadione

substrate: menadione


column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / 4-nitrobenzaldehyde; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS 4-nitrobenzaldehyde Km raw_value=8.3 raw_unit=uM

row_label: PGFS / 4-nitrobenzaldehyde


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Mus musculus

proof_lines:
adiol-class steroid substrates
3alphaHSD activity


substrate_name: androsterone

proof_lines:
androsterone
3alphaHSD activity

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6


proof_lines:
retinol dehydrogenases
SDR overlap


substrate_name: estradiol

proof_lines:
estradiol
17betaHSD activity

substrate: estradiol


substrate_name: D-Arabitol

sequence_variant_note: Resolved canonical sequence from uniprotkb:O08355 and applied mutation signature E133A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

column_label: Table 2; row label E133A; substrate D-Arabitol; checked column(s): kcat, km, kcat_over_km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm

substrate: D-Arabitol


sequence_variant_note: Resolved canonical sequence from uniprotkb:O08355 and applied mutation signature E133Q to reconstruct the assayed variant sequence.

column_label: Table 2; row label E133Q; substrate D-Arabitol; checked column(s): kcat, km, kcat_over_km; assay: oxidation of D-arabitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


column_label: Table 1; row label N300S; substrate D-mannitol; checked column(s): kcat, km, kcat_over_km; assay: oxidation of D-mannitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


column_label: Table 1; row label R373A; substrate D-mannitol; checked column(s): kcat, km, kcat_over_km; assay: oxidation of D-mannitol for 1 h; 100 uL 50 mM HEPES, 150 mM NaCl, pH 7.4, 1 mg/mL BSA, 1 mM NAD+, 90-900 nM pfMDH; substrate serial dilutions to 200 mM; NADH at 340 nm


column_label: Table 1; row WT; column kcat: raw 4.39 +/- 0.11 s^-1; normalized 4.39 s^-1; column KM: raw 5.98 +/- 0.67 mM; normalized 5.98 mM; column kcat/KM: raw 734.25 +/- 84.83 M^-1 s^-1; normalized 0.73425 s^-1 mM^-1.

row_label: WT

table_label: PMID 25752240, Table 1: Kinetic Constants for WT and Mutant pfMDH on d-Mannitol


substrate_name: meso-erythritol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E133A to reconstruct the assayed variant sequence.

substrate: meso-erythritol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature E133Q to reconstruct the assayed variant sequence.


km_display: Not reported


enzyme_display_name: (3R)-3-hydroxyacyl-CoA dehydrogenase

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

assay_conditions_summary: buffer 50 mM Hepes

column_label: Results prose tied to Fig. 5; substrate row estradiol/E2; metric label Km; raw unit uM; Fig. 5A Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.110 uM / 1000 = 0.000110 mM; required UniProt Km row value is 0.00011 mM.

raw_value_unit_evidence: Results prose / Fig. 5A: estradiol Km = 0.110 +/- 0.02 uM.

row_label: estradiol (E2), Fig. 5A

table_label: Results prose and Fig. 5

enzyme: (3R)-3-hydroxyacyl-CoA dehydrogenase


substrate_name: testosterone

column_label: Results prose tied to Fig. 5; substrate row testosterone/T; metric label Km; raw unit uM; Fig. 5B Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.422 uM / 1000 = 0.000422 mM; required UniProt Km row value is 0.000422 mM.

raw_value_unit_evidence: Results prose / Fig. 5B: testosterone Km = 0.422 +/- 0.063 uM.

row_label: testosterone (T), Fig. 5B

substrate: testosterone


substrate_name: estrone

assay_conditions_summary: buffer potassium phosphate; cofactor NADPH

column_label: Results prose tied to Fig. 5; substrate row estrone/E1; metric label Km; raw unit uM; Fig. 5D Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.368 uM / 1000 = 0.000368 mM; required UniProt Km row value is 0.000368 mM.

raw_value_unit_evidence: Results prose / Fig. 5D: estrone Km = 0.368 +/- 0.063 uM.

row_label: estrone (E1), Fig. 5D

substrate: estrone


substrate_name: dihydrotestosterone

column_label: Results prose tied to Fig. 5; substrate row dihydrotestosterone/DHT; metric label Km; raw unit uM; Fig. 5C Lineweaver-Burk plot calculated Km/Vmax by GraphPad.

normalized_value_unit_evidence: 0.360 uM / 1000 = 0.000360 mM; required UniProt Km row value is 0.00036 mM.

raw_value_unit_evidence: Results prose / Fig. 5C: dihydrotestosterone Km = 0.360 +/- 0.04 uM.

row_label: dihydrotestosterone (DHT), Fig. 5C

substrate: dihydrotestosterone


organism: Saccharomyces cerevisiae

substrate_name: NADPH

proof_lines:
NADPH
NADP
pyridoxal reductase

substrate: NADPH


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

proof_lines: NADP+ NADPH NAD

substrate: NADP+


substrate_name: pyridoxal

assay_conditions_summary: pH 6.3; cofactor NADPH

proof_lines: pyridoxal NADPH pyridoxine

substrate: pyridoxal


substrate_name: pyridoxol

proof_lines: pyridoxol pyridoxine NADP

substrate: pyridoxol


enzyme_display_name: 2-hydroxy-3-oxopropionate reductase

organism: Haemophilus influenzae

substrate_name: (R)-beta-hydroxybutyrate

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

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

enzyme: 2-hydroxy-3-oxopropionate reductase

substrate: (R)-beta-hydroxybutyrate


substrate_name: D-threonine

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

substrate: D-threonine


substrate_name: D-glycerate

substrate: D-glycerate


substrate_name: NAD

column_label: The official PubMed abstract states that the Km of NAD is 110 +/- 10 microM using estradiol as substrate.

raw_value_unit_evidence: Km raw_value=110 +/- 10 microM raw_unit=microM

row_label: Prose segment: human 17 beta-hydroxysteroid dehydrogenase 2 NAD Km

table_label: PubMed PMID 11940569 abstract

substrate: NAD


substrate_name: NADP

column_label: The official PubMed abstract states that the Km of NADP is 9600 +/- 100 microM using estradiol as substrate.

raw_value_unit_evidence: Km raw_value=9600 +/- 100 microM raw_unit=microM

row_label: Prose segment: human 17 beta-hydroxysteroid dehydrogenase 2 NADP Km

substrate: NADP


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


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


organism: Hyphomicrobium sp.

substrate_name: tartronate semialdehyde

substrate: tartronate semialdehyde


column_label: Table 2: Kinetic parameters of purified recombinant human and mouse 17HSD type 7; row E1 -> E2; Human 17HSD type 7 Km (uM) column = 3.25 +/- 0.38 uM.

normalized_value_unit_evidence: Km normalized_value=0.00325 normalized_unit=mM from 3.25 uM / 1000.

raw_value_unit_evidence: Table 2 row E1 -> E2, Human 17HSD type 7 Km column reports Km 3.25 +/- 0.38 uM.


column_label: Table 2: Kinetic parameters of purified recombinant human and mouse 17HSD type 7; row DHT -> 3betaA-diol; Human 17HSD type 7 Km (uM) column = 2.60 +/- 0.30 uM.

normalized_value_unit_evidence: Km normalized_value=0.00260 normalized_unit=mM from 2.60 uM / 1000.

raw_value_unit_evidence: Table 2 row DHT -> 3betaA-diol, Human 17HSD type 7 Km column reports Km 2.60 +/- 0.30 uM.

row_label: DHT -> 3betaA-diol


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

column_label: Table 3; row Testosterone oxidation / AKR1C3; columns Km (microM), kcat (min^-1), and kcat/Km (min^-1 mM^-1).

normalized_value_unit_evidence: Converted: kcat=0.049/60=0.0008167 s^-1; Km=0.0243 mM; kcat/Km=2.0/60=0.03333 s^-1 mM^-1. Export values 0.0008, 0.024, and 0.03333 match after unit conversion and rounding.

raw_value_unit_evidence: Table 3 reports testosterone oxidation / AKR1C3: Km=24.3 +/- 7.5 microM, kcat=0.049 min^-1, kcat/Km=2.0 min^-1 mM^-1.

row_label: Testosterone oxidation; AKR1C3


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)


substrate_name: NAD+

assay_conditions_summary: pH 10; 298.15 K; cofactor NAD+

proof_lines: The predicted enzymatic function of a NAD(+)-dependent M2DH was confirmed.

proof_lines: pH profiles for M2DH ... were recorded in the pH range 6.0-10.0

substrate: NAD+


substrate_name: NADH

proof_lines: performed a detailed steady-state kinetic characterization

substrate: NADH


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 1


enzyme_display_name: Very-long-chain 3-oxoacyl-CoA reductase

column_label: Table 1 lists 17beta-HSD12 with Km 3.5 +/- 0.5 microM and Vmax 56 +/- 7; table note says constants were determined with [14C]E1 substrate.

raw_value_unit_evidence: Km raw_value=3.5 +/- 0.5 raw_unit=microM

table_label: OUP full text Table 1

enzyme: Very-long-chain 3-oxoacyl-CoA reductase


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+


column_label: PMID 16788056 Table 2, steroid substrates; row 4-Androstene-3,17-dione; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 1.6 uM, kcat 2.0 min^-1, kcat/Km 1.3 min^-1 uM^-1.

raw_value_unit_evidence: Km 1.6 uM; kcat 2.0 min^-1; kcat/Km 1.3 min^-1 uM^-1

row_label: 4-Androstene-3,17-dione / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row Testosterone; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 21 uM, kcat 21 min^-1, kcat/Km 1.0 min^-1 uM^-1.

raw_value_unit_evidence: Km 21 uM; kcat 21 min^-1; kcat/Km 1.0 min^-1 uM^-1

row_label: Testosterone / Rat 17HSD5


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase 13

proof_lines:
HSD17B13
chronic liver disease
reduced enzymatic activity

enzyme: 17-beta-hydroxysteroid dehydrogenase 13


substrate_name: prostaglandin D2

column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / prostaglandin D2; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS prostaglandin D2 Km raw_value=100 raw_unit=uM

substrate: prostaglandin D2


column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / 9,10-phenanthroquinone; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS 9,10-phenanthroquinone Km raw_value=0.13 raw_unit=uM


substrate_name: menadione

column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / menadione; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS menadione Km raw_value=13 raw_unit=uM

substrate: menadione


column_label: Table I. Substrate specificity of bovine liver PGFSII and bovine lung PGFS; row PGFS / 4-nitrobenzaldehyde; column(s) PGFS Km (uM)

raw_value_unit_evidence: Table I PGFS 4-nitrobenzaldehyde Km raw_value=8.3 raw_unit=uM


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Y24A to reconstruct the assayed variant sequence.


substrate_name: androstenedione

substrate: androstenedione


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A24Y with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

proof_lines: A24 androstenedione epi-testosterone


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


column_label: Table 1 row AKR1C3 / Delta4-androstene-3,17-dione gives Km 6.6 +/- 2.4 microM, kcat 0.16 +/- 0.02 min^-1, and kcat/Km 24 min^-1 mM^-1.

normalized_value_unit_evidence: Km normalized_value=0.0066 mM; kcat normalized_value=0.0026666666666666666 s^-1; kcat/Km normalized_value=0.4 s^-1 mM^-1

raw_value_unit_evidence: Km raw_value=6.6 +/- 2.4 microM; kcat raw_value=0.16 +/- 0.02 min^-1; kcat/Km raw_value=24 min^-1 mM^-1

row_label: AKR1C3 / Delta4-androstene-3,17-dione

table_label: Official PMC full-text Table 1


enzyme_display_name: Pyridoxal reductase

organism: Schizosaccharomyces pombe (strain 972 / ATCC 24843)

enzyme: Pyridoxal reductase


enzyme_display_name: Mannitol dehydrogenase DSF1

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: mannitol

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

enzyme: Mannitol dehydrogenase DSF1

substrate: mannitol


substrate_name: D-mannitol

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

proof_lines: mutant N300D, pH 6.8, temperature not specified in the publication

proof_lines: mutant N300D, pH 10.0, temperature not specified in the publication

substrate: D-mannitol


proof_lines: mutant enzyme H303A/R73A/K381A, at pH 7.4 and 25°C


substrate_name: meso-erythritol

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

proof_lines: Km far above 1800 mM, mutant enzyme N191A, at pH 7.4 and 25°C

substrate: meso-erythritol


substrate_name: D-arabitol

substrate: D-arabitol


proof_lines: Km far above 1800 mM, mutant enzyme N300S, at pH 7.4 and 25°C


proof_lines: Km far above 1800 mM, mutant enzyme N300A, at pH 7.4 and 25°C


proof_lines: Km far above 1800 mM, mutant enzyme H303A, at pH 7.4 and 25°C


proof_lines:
mutant enzyme N191A, at pH 7.4 and 25°C
mutant N191A, pH 10.0, 25°C


substrate_name: D-Mannitol

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K295A to reconstruct the assayed variant sequence.

proof_lines: Pseudomonas fluorescens mannitol 2-dehydrogenase

substrate: D-Mannitol


proof_lines: Km far above 1800 mM, mutant enzyme E133Q, at pH 7.4 and 25°C


proof_lines: Km far above 1800 mM, mutant enzyme E133A, at pH 7.4 and 25°C


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

proof_lines: Km far above 1800 mM, wild type enzyme, at pH 7.4 and 25°C


proof_lines: wild-type, pH 7.1, temperature not specified in the publication


assay_conditions_summary: cofactor NADH


substrate_name: polyethylenimine-NH-succinyl-NADH

substrate: polyethylenimine-NH-succinyl-NADH


substrate_name: D-fructose

substrate: D-fructose


ki_unit: mM

assay_conditions_summary: cofactor NAD+


enzyme_display_name: omega-hydroxydecanoate dehydrogenase

organism: Sus scrofa

enzyme: omega-hydroxydecanoate dehydrogenase


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


smiles: C(CCCCO)CCCC(=O)[O-]


enzyme_display_name: mannitol 2-dehydrogenase


proof_lines: mutant N191D, pH 7.1, temperature not specified in the publication

proof_lines: mutant N191D, pH 10.0, temperature not specified in the publication


assay_conditions_summary: pH 10

proof_lines: mutant N191D/N300D, pH 10.0, temperature not specified in the publication


assay_conditions_summary: pH 6.8; cofactor NAD+


assay_conditions_summary: pH 7.1; cofactor NADH


assay_conditions_summary: pH 10; cofactor NADH


assay_conditions_summary: pH 10; cofactor NAD+


organism: Pseudomonas putida

substrate_name: NADPH

substrate: NADPH


substrate_name: D-glycerate

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

substrate: D-glycerate


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


organism: Cupriavidus necator

assay_conditions_summary: pH 9; 296.15 K; cofactor NAD+


substrate_name: Unknown

proof_lines: substrate 4-hydroxybutanoate, pH 9, 23°C

substrate: Unknown


enzyme_display_name: 17beta-estradiol 17-dehydrogenase

organism: Homo sapiens

substrate_name: equilin

column_label: Official ScienceDirect PDF text, Table II row Equilin, Km (10^-5 M) column gives 1.3; this is 0.013 mM.

raw_value_unit_evidence: Km raw_value=1.3 raw_unit=10^-5 M

row_label: Equilin

table_label: Table II. Estrone or estradiol derivatives

enzyme: 17beta-estradiol 17-dehydrogenase

substrate: equilin


column_label: Official ScienceDirect PDF text, Table IV row 1-Methylestradiol, Km (10^-5 M) column gives 1.5; this is 0.015 mM.

raw_value_unit_evidence: Km raw_value=1.5 raw_unit=10^-5 M

table_label: Table IV. Steroid derivatives of estrone or estradiol


substrate_name: equilenin

column_label: Official ScienceDirect PDF text, Table II row Equilenin, Km (10^-5 M) column gives 2.0; this is 0.02 mM.

raw_value_unit_evidence: Km raw_value=2.0 raw_unit=10^-5 M

row_label: Equilenin

substrate: equilenin


substrate_name: estradiol 3-methyl ether

column_label: Official ScienceDirect PDF text, Table II row Estradiol 3-methyl ether, Km (10^-5 M) column gives 3.0; this is 0.03 mM.

raw_value_unit_evidence: Km raw_value=3.0 raw_unit=10^-5 M

row_label: Estradiol 3-methyl ether

substrate: estradiol 3-methyl ether


column_label: Official ScienceDirect PDF text, Table IV row 4-Methyl-1,3,5(10)-estratriene-1,17beta-diol, Km (10^-5 M) column gives 3.2; this is 0.032 mM.

raw_value_unit_evidence: Km raw_value=3.2 raw_unit=10^-5 M


substrate_name: NADH

substrate: NADH


substrate_name: malonic semialdehyde

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

substrate: malonic semialdehyde


organism: Oryctolagus cuniculus

substrate_name: estradiol

substrate: estradiol


substrate_name: NAD+

substrate: NAD+


substrate_name: NADP+

substrate: NADP+


substrate_name: dehydroepiandrosterone

substrate: dehydroepiandrosterone


substrate_name: estrone

substrate: estrone


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


proof_lines: pH 7.4, 37°C, recombinant wild-type enzyme


substrate_name: androstenedione

substrate: androstenedione


organism: Escherichia coli


substrate_name: L-Glycerate

substrate: L-Glycerate


enzyme_display_name: estradiol 17beta-dehydrogenase

substrate_name: NADPH; H+; Estrone

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

assay_conditions_summary: pH 7.4; 310.15 K; cofactor NADPH

proof_lines: pH 7.4, 37°C recombinant His-tagged enzyme

proof_lines: pH and temperature not specified in the publication

enzyme: estradiol 17beta-dehydrogenase

substrate: NADPH; H+; Estrone


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


proof_lines: 17beta-HSD14 variant S205, pH and temperature not specified in the publication

proof_lines: 17beta-HSD14 variant T205, pH and temperature not specified in the publication


substrate_name: benzene diohydrodiol

column_label: Table III columns Substrate/Identified product/r17beta-HSD kcat, row Benzene dihydrodiol -> Catechol.

raw_value_unit_evidence: Table III r17beta-HSD row Benzene dihydrodiol: kcat=26 min^-1.

row_label: Benzene dihydrodiol -> Catechol

table_label: Table III: Comparison of kinetic constants for steroids and xenobiotics among r17beta-HSD and native mouse liver 17beta-HSDs (ED1-ED3)

substrate: benzene diohydrodiol


substrate_name: testosterone

substrate: testosterone


column_label: Table III columns Substrate/Identified product/r17beta-HSD Km, row 5beta-Pregnan-20alpha-ol-3-one -> 5beta-Pregnane-3,20-dione.

raw_value_unit_evidence: Table III r17beta-HSD row 5beta-Pregnan-20alpha-ol-3-one: Km=1.1 uM.


substrate_name: benzene dihydrodiol

column_label: Table III columns Substrate/Identified product/r17beta-HSD Km, row Benzene dihydrodiol -> Catechol.

raw_value_unit_evidence: Table III r17beta-HSD row Benzene dihydrodiol: Km=56 uM.

substrate: benzene dihydrodiol


organism: Pseudomonas fluorescens

substrate_name: NAD(P)H

assay_conditions_summary: pH 7.1; 298.15 K; cofactor NADH

enzyme: mannitol 2-dehydrogenase

substrate: NAD(P)H


proof_lines:
mutant D69A/D69A
mutant D69A


proof_lines: type 12 17beta-hydroxysteroid dehydrogenase


assay_conditions_summary: pH 7.4; cofactor NADP+

proof_lines: cosubstrate NADP+, secretory endometrium


substrate_name: allopregnanolone

substrate: allopregnanolone


enzyme_display_name: isocitrate dehydrogenase (NADP+)

substrate_name: Unknown

enzyme: isocitrate dehydrogenase (NADP+)

substrate: Unknown


organism: Gallus gallus

assay_conditions_summary: cofactor NADP+


proof_lines:
in absence of bovine serum albumin
in presence of bovine serum albumin


assay_conditions_summary: pH 10; buffer 50 mM glycine/NaOH; cofactor NAD+

proof_lines:
recombinant protein
in 50 mM glycine/NaOH buffer at pH 10.0


substrate_name: NADH

assay_conditions_summary: pH 10; buffer 50 mM glycine/NaOH; cofactor NADH

substrate: NADH


enzyme_display_name: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)

proof_lines:
pH 8.0, 25°C
at pH 7.5 and 22°C


organism: Spinacia oleracea

enzyme: phosphogluconate dehydrogenase (NADP+-dependent, decarboxylating)


substrate_name: NADP+; 6-Phospho-D-gluconate

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

substrate: NADP+; 6-Phospho-D-gluconate


assay_conditions_summary: pH 8; cofactor NADP+


enzyme_display_name: glucose 1-dehydrogenase [NAD(P)+]

organism: Saccharolobus solfataricus

substrate_name: beta-D-glucose

assay_conditions_summary: pH 6.5; 343.15 K; cofactor NADP+

proof_lines: cosubstrate NADP+, 70°C, pH not specified in the publication

enzyme: glucose 1-dehydrogenase [NAD(P)+]

substrate: beta-D-glucose


organism: Burkholderia cepacia


organism: Bacillus subtilis

substrate_name: NAD+

assay_conditions_summary: pH 8; cofactor NAD+

proof_lines:
at pH 8.0 and 25°C
pH 8.0, 25°C
pH 7.8, 23°C

substrate: NAD+


assay_conditions_summary: pH 9.9; 303.15 K; cofactor NAD+

proof_lines: pH 7.5, 37°C, reaction with beta-D-glucose


substrate_name: beta-D-xylose

assay_conditions_summary: pH 9; buffer pH was 9; cofactor NADP+

column_label: Table 4; Xylose-NAD+ row; carbohydrate K_m (mM) column; raw value 68.0 mM.

raw_value_unit_evidence: Table 4 Xylose-NAD+ row reports carbohydrate K_m = 68.0 mM.

row_label: Xylose-NAD+ row

table_label: PMID 3827812, Table 4: Apparent Km values for substrates and coenzymes of glucose dehydrogenase from Sulfolobus solfataricus

substrate: beta-D-xylose


organism: Ovis aries

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

assay_conditions_summary: pH 8


enzyme_display_name: D-galactose 1-dehydrogenase

assay_conditions_summary: cofactor NAD+

proof_lines: beta-galactosidase-galactose dehydrogenase fusion enzymes

enzyme: D-galactose 1-dehydrogenase


substrate_name: L-arabinose

substrate: L-arabinose


substrate_name: 2-deoxyglucose 6-phosphate

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

substrate: 2-deoxyglucose 6-phosphate


organism: Priestia megaterium


substrate_name: NADP+

proof_lines: isoenzymes I and II, with glucose 6-phosphate

substrate: NADP+


organism: Aquifex aeolicus

substrate_name: D-glucose 6-phosphate

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

assay_conditions_summary: 343.15 K; cofactor NADP+

substrate: D-glucose 6-phosphate


organism: Oncorhynchus mykiss


organism: Camelus dromedarius

proof_lines: at pH 8.0 temperature not specified in the publication


organism: Hordeum vulgare

assay_conditions_summary: 298.15 K; cofactor NADPH

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

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


sequence_variant_note: Resolved canonical sequence from manual_pmid_uniprot_reviewed_match and applied mutation signature P409R to reconstruct the assayed variant sequence.

column_label: Table 4, row Human P409R mutant, column Km for glucose 6-phosphate (umol/l), cell 286. Mutation support: abstract and Results report 1226 C>G predicting Pro409Arg/P409R, confirmed in exon 10; Methods state mutagenesis introduced G>C/P409R into human G6PD cDNA.

normalized_value_unit_evidence: Expected export Km 0.286 mM; Table 4 central Km for glucose 6-phosphate 286 umol/l = 0.286 mM.

raw_value_unit_evidence: Table 4 row Human P409R mutant: Km for glucose 6-phosphate = 286 umol/l.

row_label: Human P409R mutant

table_label: Table 4: Biochemical characterization of G6PD


organism: Equus caballus


substrate_name: dehydroepiandrosterone

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

substrate: dehydroepiandrosterone


organism: Bos taurus

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines: isoform G6PD1, at pH 8.0, temperature not specified in the publication

proof_lines: isoform G6PD2, at pH 8.0, temperature not specified in the publication


organism: Homo sapiens

substrate_name: estrone

sequence_variant_note: Resolved canonical sequence from manual_identity_resolution_uniprot_P14061_pmid_24348564 and applied mutation signature C10S with inferred residue-numbering offset +1 to reconstruct the assayed variant sequence.

substrate: estrone


organism: Pseudomonas sp.

substrate_name: D-mannitol

substrate: D-mannitol


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

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


organism: Saccharomyces cerevisiae


organism: Cereibacter sphaeroides

substrate_name: D-arabitol

substrate: D-arabitol


enzyme_display_name: isocitrate dehydrogenase (NAD+)

organism: Rhodomicrobium vannielii

substrate_name: Isocitrate; NAD+

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

enzyme: isocitrate dehydrogenase (NAD+)

substrate: Isocitrate; NAD+


organism: Hydrogenobacter thermophilus

substrate_name: NAD+; Isocitrate

substrate: NAD+; Isocitrate


organism: Escherichia coli


organism: Bifidobacterium longum


organism: Ostreococcus tauri

proof_lines: pH 7.6, temperature not specified in the publication, His6-tagged recombinant wild-type enzyme


organism: Phaeodactylum tricornutum

proof_lines: kcat is 180.5 sec(-1) for NAD(+) with Mn(2+) as cofactor. kcat is 79.0 sec(-1) for NAD(+) with Mg(2+) as cofactor.


enzyme_display_name: Isocitrate dehydrogenase [NAD] subunit alpha, mitochondrial

sequence_variant_note: Mutation context was captured, but conflicting substitutions targeted the same residue position.

assay_conditions_summary: cofactor ATP

proof_lines: kcat is 26.7 sec(-1) for the heterotetramer with isocitrate as substrate. kcat is 14.6 sec(-1) for the heterodimer composed of IDH3A and IDH3B subunits with isocitrate as substrate. kcat is 9.72 sec(-1) for the heterodimer composed of IDH3A


organism: Sus scrofa

substrate_name: Isocitrate; NADP+

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

assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADP+

source_databases_merged: sabio_rk skid uniprot

substrate: Isocitrate; NADP+


organism: Rattus norvegicus


substrate_name: NADP+; Isocitrate

substrate: NADP+; Isocitrate


organism: Pisum sativum


organism: Bacillus subtilis


organism: Halobacterium volcanii


organism: Aspergillus nidulans

substrate_name: D-Isocitrate; NADP+

substrate: D-Isocitrate; NADP+


organism: Thermus thermophilus

substrate_name: Homoisocitrate; NAD+

substrate: Homoisocitrate; NAD+


organism: Mycobacterium tuberculosis


organism: Saccharopolyspora erythraea

substrate_name: DL-isocitrate

substrate: DL-isocitrate


organism: Synechocystis sp.

substrate_name: D,L-isocitrate

proof_lines:
Mn2+-dependent reaction
Mg2+-dependent reaction

substrate: D,L-isocitrate


organism: Chlamydomonas reinhardtii


organism: Caldococcus noboribetus


organism: Mycolicibacterium phlei


enzyme_display_name: UniProt O29610

organism: Archaeoglobus fulgidus

source_db: skid

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

proof_lines: kcat is 254.6 sec(-1) with isocitrate as substrate (at 60 degrees Celsius) (PubMed:17401542). kcat is 219.3 sec(-1) with NADP(+) as substrate (at 60 degrees Celsius) (PubMed:17401542).

source_databases_merged: skid uniprot

enzyme: UniProt O29610

source: skid


enzyme_display_name: UniProt Q4E4L7

organism: Trypanosoma cruzi

source_license: CC BY-NC-ND 4.0

enzyme: UniProt Q4E4L7


enzyme_display_name: Isocitrate dehydrogenase [NADP], mitochondrial

organism: Homo sapiens

substrate_name: Unknown

substrate: Unknown


enzyme_display_name: Isocitrate dehydrogenase [NADP] 2

organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: D,L-isocitrate (in the presence of Mg(2+))

enzyme: Isocitrate dehydrogenase [NADP] 2


enzyme_display_name: Isocitrate dehydrogenase [NADP]

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

enzyme: Isocitrate dehydrogenase [NADP]


organism: Nostoc sp. (strain PCC 7120 / SAG 25.82 / UTEX 2576)

substrate_name: D,L-isocitrate (in the presence of Mn(2+))


organism: Enterococcus faecalis

substrate_name: 6-Phospho-D-gluconate; NADP+

substrate: 6-Phospho-D-gluconate; NADP+


organism: Lactococcus lactis subsp. cremoris


substrate_name: NADP+; 6-Phospho-D-gluconate

proof_lines: human erythrocyte 6-phosphogluconate dehydrogenase

proof_lines: alternative substrate 2-deoxy 6-phosphogluconate

substrate: NADP+; 6-Phospho-D-gluconate


organism: Rattus norvegicus

proof_lines:
6-phosphogluconate dehydrogenase
rat liver
kidney cortex


organism: Dicentrarchus labrax


organism: Ovis aries

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

assay_conditions_summary: pH 8; 293.15 K; cofactor NADP+


organism: Corynebacterium glutamicum

assay_conditions_summary: cofactor NADP+


organism: Haemophilus influenzae


organism: Saccharomyces cerevisiae


organism: Spinacia oleracea


organism: Klebsiella pneumoniae


organism: Escherichia coli


organism: Synechocystis sp.


organism: Moorella thermoacetica

proof_lines: 6-phosphogluconate dehydrogenase from Moorella thermoacetica


organism: Thermotoga maritima

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NADP+

column_label: Table 1 (Kinetics parameters of Tm6PGDH and its mutants.), body row 'Wide-type'; column 'Km (mM)' under coenzyme NADP+ = 0.005; column 'kcat (s^-1)' under coenzyme NADP+ = 17.6; column 'kcat/Km (mM^-1*s^-1)' under coenzyme NADP+ = 3520.

normalized_value_unit_evidence: Km: printed Table 1 cell 0.005 mM; the column head prints mM, so no conversion is applied and the exported value is 0.005 mM. kcat: printed Table 1 cell 17.6 s^-1; the column head prints s^-1 and no conversion is applied, and the exported value is 47.9 s^(-1). kcat/Km: printed Table 1 cell 3520 mM^-1*s^-1; 1 mM^-1*s^-1 is 1 s^-1 mM^-1, so the printed cell converts unchanged to 3520.0 s^(-1)*mM^(-1), and this export row carries no ratio field.

raw_value_unit_evidence: Table 1, body row 'Wide-type', coenzyme NADP+ columns: Km = 0.005 mM; kcat = 17.6 s^-1; printed kcat/Km = 3520 mM^-1*s^-1.

row_label: Table 1, body row 'Wide-type', coenzyme NADP+ cell group

table_label: Table 1: Kinetics parameters of Tm6PGDH and its mutants. (Scientific Reports 2016, volume 6, article 36311)


organism: Trypanosoma brucei


organism: Ctenopharyngodon idella


enzyme_display_name: L-gulonate 3-dehydrogenase

organism: Oryctolagus cuniculus

substrate_name: NAD+; L-Gulonate

enzyme: L-gulonate 3-dehydrogenase

substrate: NAD+; L-Gulonate


organism: Homo sapiens


organism: Drosophila melanogaster

assay_conditions_summary: pH 8.2; cofactor NAD+

proof_lines:
cofactor NAD+, pH 8.2
cofactor NAD+


enzyme_display_name: glucose 1-dehydrogenase

substrate_name: beta-D-Glucose; NAD+

enzyme: glucose 1-dehydrogenase

substrate: beta-D-Glucose; NAD+


organism: Mus musculus


organism: Columba sp.


organism: Gallus gallus


organism: Bacillus megaterium

substrate_name: D-Glucose; NAD+

proof_lines: kcat is 190 sec(-1) with D-glucose as substrate and NAD(+) as the cosubstrate (PubMed:1629157). kcat is 120 sec(-1) with D-glucose as substrate and NADP(+) as the cosubstrate (PubMed:1629157).

substrate: D-Glucose; NAD+


proof_lines: kcat is 190 sec(-1) with D-glucose as substrate and NAD(+) as the cosubstrate (PubMed:1629157). kcat is 140 sec(-1) with D-glucose as substrate and NADP(+) as the cosubstrate (PubMed:1629157).


substrate_name: NAD+; D-Glucose

proof_lines: kcat is 430 sec(-1) with D-glucose as substrate and NAD(+) as the cosubstrate (PubMed:1629157). kcat is 802 sec(-1) with D-glucose as substrate and NADP(+) as the cosubstrate (PubMed:1629157).

substrate: NAD+; D-Glucose


proof_lines: kcat is 420 sec(-1) with D-glucose as substrate and NAD(+) as the cosubstrate (PubMed:1629157). kcat is 462 sec(-1) with D-glucose as substrate and NADP(+) as the cosubstrate (PubMed:1629157).


organism: Rattus norvegicus

substrate_name: NADP+; Glucose 6-phosphate

substrate: NADP+; Glucose 6-phosphate


organism: Sulfolobus solfataricus

substrate_name: D-Glucose; NADP+

substrate: D-Glucose; NADP+


organism: Bacillus subtilis


enzyme_display_name: Glucose 1-dehydrogenase

organism: Thermoproteus tenax (strain ATCC 35583 / DSM 2078 / JCM 9277 / NBRC 100435 / Kra 1)

substrate_name: glucose (in the presence of NADP(+), at 70 degrees Celsius and pH 7)

assay_conditions_summary: pH 7

enzyme: Glucose 1-dehydrogenase


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

substrate_name: D-Galactose 6-phosphate; NADP+

enzyme: galactose 1-dehydrogenase

substrate: D-Galactose 6-phosphate; NADP+


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)

assay_conditions_summary: pH 9

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


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


organism: Thermotoga maritima

substrate_name: thio-NAD+

assay_conditions_summary: pH 7.4; 353.15 K; cofactor NADP+

substrate: thio-NAD+


organism: Taenia crassiceps

substrate_name: Unknown

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

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


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

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


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.

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

substrate: Unknown


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

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.

enzyme: 4-hydroxybutyrate dehydrogenase

substrate: 3-hydroxypropane sulfonate


enzyme_display_name: estradiol 17beta-dehydrogenase

organism: Rattus norvegicus

enzyme: estradiol 17beta-dehydrogenase


substrate_name: Estrone; H+; NADPH

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


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+

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_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

enzyme: isocitrate dehydrogenase (NAD+)

substrate: NAD+; Isocitrate


enzyme_display_name: isocitrate dehydrogenase (NADP+)

organism: Streptococcus suis

substrate_name: Isocitrate; NADP+

assay_conditions_summary: cofactor 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

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

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)

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)


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.


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