substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


enzyme_display_name: Aldo-keto reductase family 1 member B15

organism: Homo sapiens

substrate_name: acrolein

source_db: uniprot

verification_status: unverified

kcat_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

mutation_signature: Unknown

protein_accession_database: UniProt

source_license: 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.

smiles: C=CC=O

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

data_origin: experimental

enzyme: Aldo-keto reductase family 1 member B15

substrate: acrolein

status: unverified

source: uniprot


smiles: CCCCC=CC=O


smiles: CCCCCC=CC(O)CC=O


smiles: CCCCCC=CC(=O)C


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


substrate_name: farnesal

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

substrate: farnesal


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

substrate: NADPH


enzyme_display_name: 17-beta-hydroxysteroid dehydrogenase type 6

organism: Rattus norvegicus

proof_lines: Vmax was measured using transfected cell lysates.


substrate_name: androsterone

enzyme: 17-beta-hydroxysteroid dehydrogenase type 6

substrate: androsterone


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


substrate_name: testosterone

substrate: testosterone


substrate_name: estradiol

substrate: estradiol


substrate_name: NAD

substrate: NAD


substrate_name: NADP

substrate: NADP


enzyme_display_name: UniProt O93874

organism: Curvularia lunata

source_db: skid

source_license: CC BY-NC-ND 4.0

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

enzyme: UniProt O93874

source: skid


substrate_name: NADP+

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: pH 8; 298.15 K; cofactor NAD+

substrate: NAD+


substrate_name: NADH

assay_conditions_summary: pH 8; 298.15 K; cofactor NADH

substrate: NADH


enzyme_display_name: mannitol 2-dehydrogenase

organism: Aspergillus fumigatus

substrate_name: L-sorbitol

source_db: brenda

kcat_over_km_origin: calculated

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

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

assay_conditions_summary: pH 10; buffer 100 mM glycine/NaOH

proof_lines: at 25°C, in 100 mM glycine/NaOH buffer pH 10.0

enzyme: mannitol 2-dehydrogenase

substrate: L-sorbitol

source: brenda


substrate_name: D-xylulose

verification_status: corrected

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

column_label: Primary Wiley full article, Table 1, D-Xylulose row, kcat/Km column; caption supplies open-chain correction and pH 7.1.

normalized_value_unit_evidence: kcat 64 s^-1; Km 1.7 mM; explicit corrected kcat/Km 39 s^-1 mM^-1.

row_label: D-Xylulose

table_label: Table 1. Kinetic constants of AfM2DH for reactions with different polyol and ketose substrates

substrate: D-xylulose

status: corrected


substrate_name: D-fructose

assay_conditions_summary: pH 7.1; buffer 100 mM Tris/HCl; cofactor NADPH

column_label: Primary Wiley full article, Table 1, D-Fructose row, kcat/Km column; caption supplies open-chain correction and pH 7.1.

normalized_value_unit_evidence: kcat 86 s^-1; Km 0.60 mM; explicit corrected kcat/Km 140 s^-1 mM^-1.

row_label: D-Fructose

source_databases_merged: brenda uniprot

substrate: D-fructose


substrate_name: D-arabinitol

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

assay_conditions_summary: pH 10

column_label: Primary Wiley full article, Table 1, D-Arabinitol row, kcat/Km column; caption supplies polyol-oxidation pH 10.0.

normalized_value_unit_evidence: kcat 162 s^-1; Km 163 mM; explicit kcat/Km 0.99 s^-1 mM^-1.

row_label: D-Arabinitol

substrate: D-arabinitol


verification_status: verified

assay_conditions_summary: pH 7.1; buffer 100 mM Tris/HCl; cofactor NADH

column_label: Primary Wiley full article, Table 2, K_NADH row, AfM2DH column.

normalized_value_unit_evidence: Km NADH 0.015 mM.

raw_value_unit_evidence: Table 2 AfM2DH column, K_NADH row: 15 +/- 8 uM.

row_label: K_NADH; AfM2DH column

table_label: Table 2. Kinetic parameters of AfM1PDH and AfM2DH at 25 C and pH 7.1

status: verified


assay_conditions_summary: pH 7.1; buffer 100 mM glycine/NaOH; cofactor NAD+

column_label: Primary Wiley full article, Table 2, K_NAD row, AfM2DH column.

normalized_value_unit_evidence: Km NAD+ 0.11 mM.

raw_value_unit_evidence: Table 2 AfM2DH column, K_NAD row: 0.11 +/- 0.02 mM.

row_label: K_NAD; AfM2DH column


enzyme_display_name: 4-hydroxybutyrate dehydrogenase

organism: Escherichia coli

substrate_name: Succinic semialdehyde

sequence_source: multiple

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

assay_conditions_summary: pH 7.2; buffer 100 mM MOPS-KOH; cofactor NADH

proof_lines: in 100 mM MOPS-KOH buffer (pH 7.2), 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: Succinic semialdehyde


substrate_name: methylglyoxal

smiles: CC(=O)C=O

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

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

substrate: methylglyoxal


assay_conditions_summary: cofactor NADH


substrate_name: gamma-hydroxybutyrate

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

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

substrate: gamma-hydroxybutyrate


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: 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


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

column_label: Table 2 row Androsterone under Reductive reactions; Km column.

raw_value_unit_evidence: Table 2 reports Km 2.8 +/- 0.2 uM for Androsterone.

row_label: Reductive reactions; Androsterone

table_label: Table 2: Kinetic parameters of AKR1B15.1


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

column_label: PMC Table 3 columns Substrate, Km (uM), kcat (min^-1), and kcat/Km (uM^-1 min^-1); row Delta4-Androstenedione reports Km 1.9 +/- 0.2 uM.

raw_value_unit_evidence: Km raw_value=1.9 +/- 0.2 uM raw_unit=uM

row_label: Reductive reactions / Delta4-Androstenedione

table_label: PMC Table 3 Kinetic constants of AKR1B15.1


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

column_label: Table 2 row Estrone under Reductive reactions; Km column.

raw_value_unit_evidence: Table 2 reports Km 2.5 +/- 0.4 uM for Estrone.

row_label: Reductive reactions; Estrone


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

column_label: Table 2 row Acetoacetyl-CoA under Reductive reactions; Km column.

raw_value_unit_evidence: Table 2 reports Km 63.4 +/- 7.4 uM for Acetoacetyl-CoA.

row_label: Reductive reactions; Acetoacetyl-CoA


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

column_label: Table 2 row Testosterone under Oxidative reactions; Km column.

raw_value_unit_evidence: Table 2 reports Km 7.1 +/- 1.5 uM for Testosterone.

row_label: Oxidative reactions; Testosterone


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

column_label: Table 2 row 17beta-Estradiol under Oxidative reactions; Km column.

raw_value_unit_evidence: Table 2 reports Km 9.1 +/- 1.2 uM for 17beta-Estradiol.

row_label: Oxidative reactions; 17beta-Estradiol


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

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

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


substrate_name: 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)

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


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: Aldo-keto reductase family 1 member C3

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

enzyme: Aldo-keto reductase family 1 member C3


substrate_name: testosterone (oxidation)

substrate: testosterone (oxidation)


enzyme_display_name: Aldo-keto reductase family 1 member C4

organism: Macaca fuscata fuscata

column_label: Table 2; row 5a-Pregnane-3a,21-diol-20-one; jpDD4 (AKR1C4) Km column; footnote a: dehydrogenase activity assayed at pH 7.4; parenthesized human values ignored.

normalized_value_unit_evidence: normalized required Km-only paper value: 0.6 uM = 0.0006 mM.

raw_value_unit_evidence: Table 2 row 5a-Pregnane-3a,21-diol-20-one, jpDD4 column: Km=0.6 uM.

row_label: jpDD4 / 5a-Pregnane-3a,21-diol-20-one

table_label: Table 2

enzyme: Aldo-keto reductase family 1 member C4


column_label: Table 2; row 5a-Androstan-3a-ol-17-one; jpDD4 (AKR1C4) Km column; footnote a: dehydrogenase activity assayed at pH 7.4; parenthesized human values ignored.

normalized_value_unit_evidence: normalized required Km-only paper value: 0.7 uM = 0.0007 mM.

raw_value_unit_evidence: Table 2 row 5a-Androstan-3a-ol-17-one, jpDD4 column: Km=0.7 uM.

row_label: jpDD4 / 5a-Androstan-3a-ol-17-one


substrate_name: NADPH

substrate: NADPH


substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: allopregnanolone (oxidation)

substrate: allopregnanolone (oxidation)


enzyme_display_name: 3-sulfolactaldehyde reductase

organism: Escherichia coli (strain K12)

enzyme: 3-sulfolactaldehyde reductase


substrate_name: NADH


organism: Leuconostoc pseudomesenteroides

substrate_name: D-mannitol

substrate: D-mannitol


substrate_name: D-fructose


organism: Cupriavidus necator

proof_lines: kcat is 8.4 sec(-1) with 4-hydroxybutanoate as substrate. kcat is 8.9 sec(-1) with NAD(+) as substrate.


substrate_name: NAD(+)

substrate: NAD(+)


enzyme_display_name: UniProt Q9BPX1

enzyme: UniProt Q9BPX1


substrate_name: progesterone

substrate: progesterone


substrate_name: androstanediol

substrate: androstanediol


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


substrate_name: tetramyristoyl cardiolipin

assay_conditions_summary: cofactor CoA

substrate: tetramyristoyl cardiolipin


substrate_name: tetralinoleoyl cardiolipin

substrate: tetralinoleoyl cardiolipin


enzyme_display_name: UniProt P14061

substrate_name: estrone

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

source_databases_merged: skid uniprot

enzyme: UniProt P14061

substrate: estrone


substrate_name: (s)-indan-1-ol (oxidation)

substrate: (s)-indan-1-ol (oxidation)


substrate_name: (s)-tetralol

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

substrate: (s)-tetralol


substrate_name: progesterone (reduction)

substrate: progesterone (reduction)


substrate_name: 5alpha-androstan-3,17-dione (reduction)

substrate: 5alpha-androstan-3,17-dione (reduction)


substrate_name: prostaglandin H2

substrate: prostaglandin H2


organism: Eimeria tenella


enzyme_display_name: Pyridoxine 4-dehydrogenase

proof_lines: kcat is 0.11 sec(-1) for the Kemp eliminase activity towards 5-nitrobenzisoxazole.

enzyme: Pyridoxine 4-dehydrogenase


enzyme_display_name: 17beta-estradiol 17-dehydrogenase

source_db: oed

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 7, substrate `Estrone`, Rat 17HSD5 column group: Km = 11 uM (normalized 0.011 mM); kcat = 2.7 min-1 (normalized 0.045000000000000005 s^-1); kcat/Km = 0.25 min-1 uM-1 (normalized 4.166666666666667 s^-1 mM^-1).

table_label: Table 2 (journal page 1058) 'Substrate specificity for steroids in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5', decoded plain-numeral transcription

enzyme: 17beta-estradiol 17-dehydrogenase

source: oed


organism: Pseudomonas fluorescens

substrate_name: D-Arabitol

column_label: Table 2; row label WT; 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

row_label: WT

substrate: D-Arabitol


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature D230A with inferred residue-numbering offset -14 to reconstruct the assayed variant sequence.

mutation_type: substitution

column_label: Table 1; row label D230A; substrate D-mannitol; checked column(s): 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

table_label: Table 1


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

column_label: Table 1; row label E133A; substrate D-mannitol; checked column(s): kcat, kcat_over_km, 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


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

column_label: Table 1; row label E133Q; substrate D-mannitol; checked column(s): kcat, kcat_over_km, 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


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

column_label: Table 1; row label H303A; substrate D-mannitol; checked column(s): kcat_over_km, 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


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 1; row label H303A/R373A/K381A; substrate D-mannitol; checked column(s): kcat_over_km, 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


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

column_label: Table 1; row label K381A; substrate D-mannitol; checked column(s): 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


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

column_label: Table 1; row label N191A; substrate D-mannitol; checked column(s): 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


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

column_label: Table 1; row label N300A; substrate D-mannitol; checked column(s): kcat_over_km, 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


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

column_label: Table 1; row label N300D; substrate D-mannitol; checked column(s): kcat, 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 2; row label D230A; substrate D-Arabitol; checked column(s): kcat, 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 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 6, substrate `4-Chlorobenzaldehyde`, Rat 17HSD5 column group: Km = 263 uM (normalized 0.263 mM); kcat = 6.5 min-1 (normalized 0.10833333333333334 s^-1); kcat/Km = 0.02 min-1 uM-1 (normalized 0.33333333333333337 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


column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 10, substrate `4-Nitroacetophenone`, Rat 17HSD5 column group: Km = 84 uM (normalized 0.084 mM); kcat = 8.3 min-1 (normalized 0.13833333333333334 s^-1); kcat/Km = 0.10 min-1 uM-1 (normalized 1.666666666666667 s^-1 mM^-1).


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (A), printed row 2, substrate `5a-Dihydrotestosterone`, Rat 17HSD5 column group: Km = 28 uM (normalized 0.028 mM); kcat = 18 min-1 (normalized 0.3 s^-1); kcat/Km = 0.65 min-1 uM-1 (normalized 10.833333333333334 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 18 min-1 / 60 = 0.3 s^-1; the catalog holds 0.3 s^(-1). Km: printed cell 28 uM / 1000 = 0.028 mM; the catalog holds 0.028 mM. kcat/Km: the paper prints the cell 0.65 min-1 uM-1, which is 0.65 x 1000 / 60 = 10.833333333333334 s^-1 mM^-1; the catalog holds 10.714285714285714 s^(-1)*mM^(-1).


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 5, substrate `5a-Androstane-3,17-dione`, Rat 17HSD5 column group: Km = 2.4 uM (normalized 0.0024 mM); kcat = 2.5 min-1 (normalized 0.041666666666666664 s^-1); kcat/Km = 1.1 min-1 uM-1 (normalized 18.333333333333332 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 2.5 min-1 / 60 = 0.041666666666666664 s^-1; the catalog holds 0.042 s^(-1). Km: printed cell 2.4 uM / 1000 = 0.0024 mM; the catalog holds 0.002 mM. kcat/Km: the paper prints the cell 1.1 min-1 uM-1, which is 1.1 x 1000 / 60 = 18.333333333333332 s^-1 mM^-1; the catalog holds 21.0 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 5, substrate `5a-Androstane-3,17-dione`, Rat 17HSD5 column group: Km = 2.4 uM; kcat = 2.5 min-1; kcat/Km = 1.1 min-1 uM-1.


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (A), printed row 6, substrate `5a-Androstane-3a,17b-diol`, Rat 17HSD5 column group: Km = 19 uM (normalized 0.019 mM); kcat = 8.4 min-1 (normalized 0.14 s^-1); kcat/Km = 0.44 min-1 uM-1 (normalized 7.333333333333334 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 8.4 min-1 / 60 = 0.14 s^-1; the catalog holds 0.14 s^(-1). Km: printed cell 19 uM / 1000 = 0.019 mM; the catalog holds 0.019 mM. kcat/Km: the paper prints the cell 0.44 min-1 uM-1, which is 0.44 x 1000 / 60 = 7.333333333333334 s^-1 mM^-1; the catalog holds 7.36842105263158 s^(-1)*mM^(-1).


column_label: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 2, substrate `5b-Androstane-3,17-dione`, Rat 17HSD5 column group: Km = 6.2 uM (normalized 0.0062 mM); kcat = 1.6 min-1 (normalized 0.02666666666666667 s^-1); kcat/Km = 0.25 min-1 uM-1 (normalized 4.166666666666667 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 1.6 min-1 / 60 = 0.02666666666666667 s^-1; the catalog holds 0.027 s^(-1). Km: printed cell 6.2 uM / 1000 = 0.0062 mM; the catalog holds 0.006 mM. kcat/Km: the paper prints the cell 0.25 min-1 uM-1, which is 0.25 x 1000 / 60 = 4.166666666666667 s^-1 mM^-1; the catalog holds 4.5 s^(-1)*mM^(-1).

raw_value_unit_evidence: Table 2 (journal page 1058), decoded plain-numeral transcription, group (C), printed row 2, substrate `5b-Androstane-3,17-dione`, Rat 17HSD5 column group: Km = 6.2 uM; kcat = 1.6 min-1; kcat/Km = 0.25 min-1 uM-1.


column_label: table label: Table 1. Substrate specificity for non-steroidal substrates in the oxidation and reduction reactions catalyzed by TBER1 and rat 17HSD5.; row label: TBE (Reduction section of Table 1); column label: Rat 17HSD5 Km (uM), Rat 17HSD5 kcat (min-1) and Rat 17HSD5 kcat/Km (min-1 uM-1) cells of this one table row; no cell is taken from the TBER1 column group and no cell is taken from any other row; raw value: Km 16 uM, kcat 9.2 min-1, kcat/Km 0.58 min-1 uM-1; raw unit: uM for Km, min-1 for kcat, min-1 uM-1 for kcat/Km; normalized value: Km 0.016 mM, kcat 0.153 s^-1, kcat/Km 9.5625 s^-1 mM^-1; normalized unit: mM, s^-1, s^-1 mM^-1; condition label: Km (uM), kcat (min-1), and kcat/Km (min-1 uM-1) values were determined at pH 7.4 with NAD(H) for TBER1 and with NADP(H) for rat 17HSD5 as the coenzyme. This record reads the Rat 17HSD5 column group of this one row, so the coenzyme for these cells is NADP(H). Unit note: the CiteSeerX text layer renders the printed micro sign as m, so the transcribed footnote reads Km (mM) and kcat/Km (min-1 mM-1) Exported assay conditions: pH 7.4, 298.15 K; the exported row carries no cofactor annotation, so no cofactor record is contradicted.

normalized_value_unit_evidence: Km 16 uM divided by 1000 gives 0.016 mM at the export's stored precision; exported Km 0.016 mM. kcat 9.2 min-1 divided by 60 gives 0.153 s^-1 at the export's stored precision; exported kcat 0.153 s^-1. kcat/Km is recorded as the quotient of this same row's own two cells as stored, 0.153 s^-1 divided by 0.016 mM giving 9.5625 s^-1 mM^-1, and of nothing else; exported kcat/Km 9.5625 s^-1 mM^-1.

raw_value_unit_evidence: Table 1, Reduction section, row TBE, Rat 17HSD5 column group: Km 16 uM; kcat 9.2 min-1; kcat/Km 0.58 min-1 uM-1.

row_label: TBE


column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Reduction, printed row 1, substrate `9,10-Phenanthrenequinone`, Rat 17HSD5 column group: Km = 0.5 uM (normalized 0.0005 mM); kcat = 18 min-1 (normalized 0.3 s^-1); kcat/Km = 36 min-1 uM-1 (normalized 600.0 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 18 min-1 / 60 = 0.3 s^-1; the catalog holds 0.3 s^(-1). Km: printed cell 0.5 uM / 1000 = 0.0005 mM; the catalog holds 0.0005 mM. kcat/Km: the paper prints the cell 36 min-1 uM-1, which is 36 x 1000 / 60 = 600.0 s^-1 mM^-1; the catalog holds 600.0 s^(-1)*mM^(-1).


substrate_name: 9alpha,11beta-Prostaglandin F2

column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Oxidation, printed row 7, substrate `9a,11b-PGF2`, Rat 17HSD5 column group: Km = 161 uM (normalized 0.161 mM); kcat = 1.8 min-1 (normalized 0.03 s^-1); kcat/Km = 0.01 min-1 uM-1 (normalized 0.16666666666666669 s^-1 mM^-1).

normalized_value_unit_evidence: kcat: printed cell 1.8 min-1 / 60 = 0.03 s^-1; the catalog holds 0.03 s^(-1). Km: printed cell 161 uM / 1000 = 0.161 mM; the catalog holds 0.161 mM. kcat/Km: the paper prints the cell 0.01 min-1 uM-1, which is 0.01 x 1000 / 60 = 0.16666666666666669 s^-1 mM^-1; the catalog holds 0.18633540372670807 s^(-1)*mM^(-1).

substrate: 9alpha,11beta-Prostaglandin F2


column_label: Table 1 (journal page 1058), decoded plain-numeral transcription, Oxidation, printed row 6, substrate `b-3-Hydroxyhexobarbital`, Rat 17HSD5 column group: Km = 840 uM (normalized 0.84 mM); kcat = 3.5 min-1 (normalized 0.058333333333333334 s^-1); kcat/Km = 0.004 min-1 uM-1 (normalized 0.06666666666666668 s^-1 mM^-1).


assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+

column_label: PMID 16788056 Table 2, steroid substrates; row 16-Ketoestrone; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 0.7 uM, kcat 5.2 min^-1, kcat/Km 7.5 min^-1 uM^-1.

raw_value_unit_evidence: Km 0.7 uM; kcat 5.2 min^-1; kcat/Km 7.5 min^-1 uM^-1

row_label: 16-Ketoestrone / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row 17a-Hydroxyprogesterone; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 50 uM, kcat 6.2 min^-1, kcat/Km 0.12 min^-1 uM^-1.

raw_value_unit_evidence: Km 50 uM; kcat 6.2 min^-1; kcat/Km 0.12 min^-1 uM^-1

row_label: 17a-Hydroxyprogesterone / Rat 17HSD5


column_label: PMID 16788056 Table 1, non-steroidal substrates; row R-Camphorquinone; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 1.6 uM, kcat 11 min^-1, kcat/Km 6.9 min^-1 uM^-1.

raw_value_unit_evidence: Km 1.6 uM; kcat 11 min^-1; kcat/Km 6.9 min^-1 uM^-1

row_label: R-Camphorquinone / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row 4-Pregenen-20a-ol-3-one; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 24 uM, kcat 8.5 min^-1, kcat/Km 0.35 min^-1 uM^-1.

raw_value_unit_evidence: Km 24 uM; kcat 8.5 min^-1; kcat/Km 0.35 min^-1 uM^-1

row_label: 4-Pregenen-20a-ol-3-one / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row 21-Dehydrocortisol; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 2.8 uM, kcat 7.2 min^-1, kcat/Km 2.6 min^-1 uM^-1.

raw_value_unit_evidence: Km 2.8 uM; kcat 7.2 min^-1; kcat/Km 2.6 min^-1 uM^-1

row_label: 21-Dehydrocortisol / Rat 17HSD5


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

column_label: PMID 16788056 Table 1, non-steroidal substrates; row 2,3-Pentanedione; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 57 uM, kcat 8.8 min^-1, kcat/Km 0.15 min^-1 uM^-1.

raw_value_unit_evidence: Km 57 uM; kcat 8.8 min^-1; kcat/Km 0.15 min^-1 uM^-1

row_label: 2,3-Pentanedione / Rat 17HSD5


column_label: PMID 16788056 Table 1, non-steroidal substrates; row Acetylpyridine; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 266 uM, kcat 4.5 min^-1, kcat/Km 0.02 min^-1 uM^-1.

raw_value_unit_evidence: Km 266 uM; kcat 4.5 min^-1; kcat/Km 0.02 min^-1 uM^-1

row_label: Acetylpyridine / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row 5b-Androstan-3a-ol-17-one; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 6.7 uM, kcat 1.3 min^-1, kcat/Km 0.20 min^-1 uM^-1.

raw_value_unit_evidence: Km 6.7 uM; kcat 1.3 min^-1; kcat/Km 0.20 min^-1 uM^-1

row_label: 5b-Androstan-3a-ol-17-one / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row Dehydroepiandrosterone; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 11 uM, kcat 5.0 min^-1, kcat/Km 0.45 min^-1 uM^-1.

raw_value_unit_evidence: Km 11 uM; kcat 5.0 min^-1; kcat/Km 0.45 min^-1 uM^-1

row_label: Dehydroepiandrosterone / Rat 17HSD5


column_label: PMID 16788056 Table 2, steroid substrates; row 4-Androsten-3a-ol-17-one; Rat 17HSD5 Km/kcat/kcat/Km columns; raw Km 8.5 uM, kcat 1.9 min^-1, kcat/Km 0.22 min^-1 uM^-1.

raw_value_unit_evidence: Km 8.5 uM; kcat 1.9 min^-1; kcat/Km 0.22 min^-1 uM^-1

row_label: 4-Androsten-3a-ol-17-one / Rat 17HSD5


enzyme_display_name: Dehydrogenase/reductase SDR family member 11

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

assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 1; row 3,17-Diketosteroids / 5beta-Androstane-3,17-dione; Km column

normalized_value_unit_evidence: Km=0.0052 mM converted from 5.2 uM

raw_value_unit_evidence: Table 1 3,17-Diketosteroids / 5beta-Androstane-3,17-dione Km 5.2 uM


substrate_name: 4-androstene-3,17-dione (at 37 degrees Celsius)

assay_conditions_summary: cofactor NADPH

column_label: Table 1 row 4-Androstene-3,17-dione; KM (uM) = 4.6; Vmax = 52 mU/mg; Vmax/KM = 11 mU/mg/uM.

raw_value_unit_evidence: KM column reports 4.6 uM.

table_label: Table 1. Substrate specificity for ketosteroids.

enzyme: Dehydrogenase/reductase SDR family member 11


substrate_name: progesterone (at 37 degrees Celsius)

column_label: Table 1 row Progesterone; KM (uM) = 3.4; Vmax = 36 mU/mg; Vmax/KM = 11 mU/mg/uM.

raw_value_unit_evidence: KM column reports 3.4 uM.

row_label: Progesterone

substrate: progesterone (at 37 degrees Celsius)


substrate_name: 5-beta-pregnane-3,20-dione (at 37 degrees Celsius)

column_label: Table 1 row 5-beta-Pregnane-3,20-dione; KM (uM) = 15; Vmax = 123 mU/mg; Vmax/KM = 8.2 mU/mg/uM.

raw_value_unit_evidence: KM column reports 15 uM.


substrate_name: 17-beta-estradiol (at 37 degrees Celsius)

assay_conditions_summary: cofactor NADP+

column_label: Table 2 row 17-beta-Estradiol; KM (uM) = 16; Vmax = 246 mU/mg; corresponding ketosteroid = Estrone.

raw_value_unit_evidence: KM column reports 16 uM.

table_label: Table 2. Substrate specificity for hydroxysteroids.


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)


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


substrate_name: isolithocholic acid (at 37 degrees Celsius)

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


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

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)


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


substrate_name: Dimethylglyoxal

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

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).

substrate: Isatin


substrate_name: NAD+

proof_lines:
NAD+
preferred coenzyme
pH 7.4

substrate: NAD+


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

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

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)


substrate_name: meso-erythritol

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

substrate: meso-erythritol


substrate_name: D-Arabitol

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

substrate: D-Arabitol


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


organism: Drosophila melanogaster

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

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

assay_conditions_summary: pH 6.4; cofactor CoA

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


substrate_name: (3S)-3-hydroxybutanoyl-CoA (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: 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)


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


organism: Clostridium kluyveri

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


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

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+


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)


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

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


enzyme_display_name: mannitol 2-dehydrogenase

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

table_label: Table 2

enzyme: mannitol 2-dehydrogenase

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.


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


km_display: Not reported


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

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


organism: Homo sapiens

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)


organism: Aspergillus fumigatus

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


organism: Rattus norvegicus

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


enzyme_display_name: Aldo-keto reductase family 1 member C3

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

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


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-]


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


enzyme_display_name: 4-hydroxybutyrate dehydrogenase

organism: Cupriavidus necator

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

assay_conditions_summary: pH 9; 296.15 K; cofactor NAD+

enzyme: 4-hydroxybutyrate dehydrogenase


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


substrate_name: Unknown

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

substrate: Unknown


enzyme_display_name: 17beta-estradiol 17-dehydrogenase

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

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


organism: Homo sapiens

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


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


enzyme_display_name: mannitol 2-dehydrogenase

organism: Pseudomonas sp.

substrate_name: D-mannitol

enzyme: mannitol 2-dehydrogenase

substrate: D-mannitol


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

organism: Homo sapiens

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

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).

enzyme: UniProt O29610


enzyme_display_name: UniProt Q4E4L7

organism: Trypanosoma cruzi

enzyme: UniProt Q4E4L7


enzyme_display_name: Isocitrate dehydrogenase [NADP], mitochondrial

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


organism: Homo sapiens

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: 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

organism: Homo sapiens

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