column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row R42G; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 50.1 uM; kcat cell = 5.90 min^-1; kcat/Km cell = 0.32 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | R42G hSPR, the site-directed R42G single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 50.1 uM | Table 5 kcat Redox 5.90 min^-1 | Table 5 kcat/Km Redox printed cell 0.32 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 50.1 uM; 1 uM is 1/1000 mM, so 50.1 / 1000 = 0.0501 mM; the export stores 0.0501 mM. kcat: printed kcat Redox cell 5.90 min^-1; the printed turnover column is per MINUTE, so 5.90 / 60 = 0.09833333333333334 s^(-1); the export stores 0.098 s^(-1). kcat/Km: printed kcat/Km Redox cell 0.32 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.32 x 16.666666666666668 = 5.333333333333334 s^-1 mM^-1; the export stores 1.9560878243512976 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row R42G, Redox columns: Km = 50.1 uM; kcat = 5.90 min^-1; kcat/Km = 0.32 under the printed column head kcat/Km Redox (min^-1 uM^-1).

row_label: Table 5, enzyme row R42G, Redox columns


organism: Homo sapiens

source_db: brenda

verification_status: corrected

ki_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

km_unit: mM

sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature D257H to reconstruct the assayed variant sequence.

mutation_type: substitution

assay_conditions_summary: pH 6.4; buffer 50 mM phosphate; cofactor NADPH

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row D257H; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 1.9 uM; kcat cell = 6.44 min^-1; kcat/Km cell = 3.39 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | D257H hSPR, the site-directed D257H single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 1.9 uM | Table 5 kcat Redox 6.44 min^-1 | Table 5 kcat/Km Redox printed cell 3.39 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 1.9 uM; 1 uM is 1/1000 mM, so 1.9 / 1000 = 0.0019 mM; the export stores 0.0019 mM. kcat: printed kcat Redox cell 6.44 min^-1; the printed turnover column is per MINUTE, so 6.44 / 60 = 0.10733333333333334 s^(-1); the export stores 0.107 s^(-1). kcat/Km: printed kcat/Km Redox cell 3.39 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 3.39 x 16.666666666666668 = 56.50000000000001 s^-1 mM^-1; the export stores 56.31578947368421 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row D257H, Redox columns: Km = 1.9 uM; kcat = 6.44 min^-1; kcat/Km = 3.39 under the printed column head kcat/Km Redox (min^-1 uM^-1).

data_origin: experimental

status: corrected

source: brenda


substrate_name: sepiapterin

assay_conditions_summary: pH 6.4; 310.15 K; buffer 100 mM potassium phosphate; cofactor NADPH

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row D257H; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 60.6 uM; kcat cell = 9.4 min^-1; kcat/Km cell = 0.16 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | D257H hSPR, the site-directed D257H single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 60.6 uM | Table 5 kcat SPR 9.4 min^-1 | Table 5 kcat/Km SPR printed cell 0.16 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 60.6 uM; 1 uM is 1/1000 mM, so 60.6 / 1000 = 0.0606 mM; the export stores 0.0606 mM. kcat: printed kcat SPR cell 9.4 min^-1; the printed turnover column is per MINUTE, so 9.4 / 60 = 0.15666666666666668 s^(-1); the export stores 0.156 s^(-1). kcat/Km: printed kcat/Km SPR cell 0.16 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.16 x 16.666666666666668 = 2.666666666666667 s^-1 mM^-1; the export stores 2.5742574257425743 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row D257H, SPR columns: Km = 60.6 uM; kcat = 9.4 min^-1; kcat/Km = 0.16 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row D257H, SPR columns

substrate: sepiapterin


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature M205G to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row M205G; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 13.4 uM; kcat cell = 13.45 min^-1; kcat/Km cell = 1.08 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | M205G hSPR, the site-directed M205G single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 13.4 uM | Table 5 kcat Redox 13.45 min^-1 | Table 5 kcat/Km Redox printed cell 1.08 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 13.4 uM; 1 uM is 1/1000 mM, so 13.4 / 1000 = 0.0134 mM; the export stores 0.0133 mM. kcat: printed kcat Redox cell 13.45 min^-1; the printed turnover column is per MINUTE, so 13.45 / 60 = 0.22416666666666665 s^(-1); the export stores 0.22 s^(-1). kcat/Km: printed kcat/Km Redox cell 1.08 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 1.08 x 16.666666666666668 = 18.000000000000004 s^-1 mM^-1; the export stores 16.54135338345865 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row M205G, Redox columns: Km = 13.4 uM; kcat = 13.45 min^-1; kcat/Km = 1.08 under the printed column head kcat/Km Redox (min^-1 uM^-1).


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature N99A to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row N99A; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 126.0 uM; kcat cell = 17.40 min^-1; kcat/Km cell = 0.14 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | N99A hSPR, the site-directed N99A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 126.0 uM | Table 5 kcat Redox 17.40 min^-1 | Table 5 kcat/Km Redox printed cell 0.14 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 126.0 uM; 1 uM is 1/1000 mM, so 126.0 / 1000 = 0.126 mM; the export stores 0.126 mM. kcat: printed kcat Redox cell 17.40 min^-1; the printed turnover column is per MINUTE, so 17.40 / 60 = 0.29 s^(-1); the export stores 0.29 s^(-1). kcat/Km: printed kcat/Km Redox cell 0.14 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.14 x 16.666666666666668 = 2.333333333333334 s^-1 mM^-1; the export stores 2.3015873015873014 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row N99A, Redox columns: Km = 126.0 uM; kcat = 17.40 min^-1; kcat/Km = 0.14 under the printed column head kcat/Km Redox (min^-1 uM^-1).

row_label: Table 5, enzyme row N99A, Redox columns


column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row M205G; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 133.8 uM; kcat cell = 25.7 min^-1; kcat/Km cell = 0.19 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | M205G hSPR, the site-directed M205G single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 133.8 uM | Table 5 kcat SPR 25.7 min^-1 | Table 5 kcat/Km SPR printed cell 0.19 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 133.8 uM; 1 uM is 1/1000 mM, so 133.8 / 1000 = 0.1338 mM; the export stores 0.133 mM. kcat: printed kcat SPR cell 25.7 min^-1; the printed turnover column is per MINUTE, so 25.7 / 60 = 0.4283333333333333 s^(-1); the export stores 0.428 s^(-1). kcat/Km: printed kcat/Km SPR cell 0.19 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 0.19 x 16.666666666666668 = 3.166666666666667 s^-1 mM^-1; the export stores 3.2180451127819545 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row M205G, SPR columns: Km = 133.8 uM; kcat = 25.7 min^-1; kcat/Km = 0.19 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row M205G, SPR columns


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:P35270 and applied mutation signature Y259A to reconstruct the assayed variant sequence.

column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row Y259A; columns Km SPR (uM), kcat SPR (min^-1) and kcat/Km SPR (min^-1 uM^-1); Km cell = 25.5 uM; kcat cell = 36.2 min^-1; kcat/Km cell = 1.42 under the printed column head kcat/Km SPR (min^-1 uM^-1). captured primary segment: sepiapterin | Y259A hSPR, the site-directed Y259A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km SPR 25.5 uM | Table 5 kcat SPR 36.2 min^-1 | Table 5 kcat/Km SPR printed cell 1.42 under the column head kcat/Km SPR (min^-1 uM^-1) | sepiapterin reduction assayed by formation of BH2 from sepiapterin by HPLC in 100 mM potassium phosphate buffer, pH 6.4, with 100 uM NADPH and 50 uM sepiapterin at 37 C

normalized_value_unit_evidence: Km: printed Km SPR cell 25.5 uM; 1 uM is 1/1000 mM, so 25.5 / 1000 = 0.0255 mM; the export stores 0.025 mM. kcat: printed kcat SPR cell 36.2 min^-1; the printed turnover column is per MINUTE, so 36.2 / 60 = 0.6033333333333334 s^(-1); the export stores 0.6 s^(-1). kcat/Km: printed kcat/Km SPR cell 1.42 under the column head kcat/Km SPR (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 1.42 x 16.666666666666668 = 23.666666666666668 s^-1 mM^-1; the export stores 23.999999999999996 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row Y259A, SPR columns: Km = 25.5 uM; kcat = 36.2 min^-1; kcat/Km = 1.42 under the printed column head kcat/Km SPR (min^-1 uM^-1).

row_label: Table 5, enzyme row Y259A, SPR columns


column_label: Table 5: Kinetic parameters of wild type and mutant sepiapterin reductases, printed column heads enzyme | Km SPR | Km Redox | kcat SPR | kcat Redox | kcat/Km SPR | kcat/Km Redox, with the printed units Km in uM, kcat in min^-1 and kcat/Km in min^-1 uM^-1. Journal page 19232 (PDF page 13). Table 5, enzyme row Y259A; columns Km Redox (uM), kcat Redox (min^-1) and kcat/Km Redox (min^-1 uM^-1); Km cell = 19.6 uM; kcat cell = 48.30 min^-1; kcat/Km cell = 2.46 under the printed column head kcat/Km Redox (min^-1 uM^-1). captured primary segment: 9,10-phenanthrenequinone | Y259A hSPR, the site-directed Y259A single-substitution mutant of recombinant human sepiapterin reductase carrying an N-terminal hexahistidine tag and the 261 original full-length amino acids | Table 5 Km Redox 19.6 uM | Table 5 kcat Redox 48.30 min^-1 | Table 5 kcat/Km Redox printed cell 2.46 under the column head kcat/Km Redox (min^-1 uM^-1) | redox cycling assayed with 9,10-phenanthrenequinone by quantifying the formation of H2O2 in 50 mM phosphate buffer, pH 7.8, with 0.2 mM NADPH

normalized_value_unit_evidence: Km: printed Km Redox cell 19.6 uM; 1 uM is 1/1000 mM, so 19.6 / 1000 = 0.0196 mM; the export stores 0.0196 mM. kcat: printed kcat Redox cell 48.30 min^-1; the printed turnover column is per MINUTE, so 48.30 / 60 = 0.8049999999999999 s^(-1); the export stores 0.805 s^(-1). kcat/Km: printed kcat/Km Redox cell 2.46 under the column head kcat/Km Redox (min^-1 uM^-1); 1 min^-1 uM^-1 is 16.666666666666668 s^-1 mM^-1, so 2.46 x 16.666666666666668 = 41.0 s^-1 mM^-1; the export stores 41.07142857142858 s^(-1)*mM^(-1).

raw_value_unit_evidence: Journal page 19232, Table 5, enzyme row Y259A, Redox columns: Km = 19.6 uM; kcat = 48.30 min^-1; kcat/Km = 2.46 under the printed column head kcat/Km Redox (min^-1 uM^-1).


enzyme_display_name: 20alpha-hydroxysteroid dehydrogenase

organism: Bifidobacterium adolescentis

substrate_name: cortisol

verification_status: unverified

mutation_signature: Unknown

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

assay_conditions_summary: pH 5

proof_lines: pH 5.0, temperature not specified in the publication

enzyme: 20alpha-hydroxysteroid dehydrogenase

substrate: cortisol

status: unverified


kcat_display: Not reported

kcat_over_km_display: Not reported

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


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


substrate_name: (S)-tetralol

substrate: (S)-tetralol


enzyme_display_name: UniProt Q04828

source_db: skid

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

sequence_source: multiple

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

source_databases_merged: skid uniprot

enzyme: UniProt Q04828

source: skid


enzyme_display_name: Aldo-keto reductase family 1 member C1

source_db: uniprot

enzyme: Aldo-keto reductase family 1 member C1

source: uniprot


organism: Equus caballus


organism: Tetrahymena pyriformis

substrate_name: NADPH

sequence: LAKTVPLNDGTNFPIFGG

wild_type_sequence: LAKTVPLNDGTNFPIFGG

assay_conditions_summary: pH 7; cofactor NADPH

proof_lines: 20-oxo and 20alpha-hydroxy-steroids, pH 7.0

substrate: NADPH


substrate_name: NADP+

assay_conditions_summary: pH 7; cofactor NADP+

substrate: NADP+


verification_status: verified

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

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

status: verified


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

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

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


substrate_name: testosterone (oxidation)

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

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

row_label: Testosterone oxidation / AKR1C1 (R)

substrate: testosterone (oxidation)


enzyme_display_name: Sepiapterin reductase

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 1.1 sec(-1) with sepiapterin as substrate (PubMed:10350607). kcat is 1.1 sec(-1) with NADPH as substrate (PubMed:10350607).

enzyme: Sepiapterin reductase


assay_conditions_summary: pH 7.5; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H222S to reconstruct the assayed variant sequence.


substrate_name: progesterone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T307V to reconstruct the assayed variant sequence.

substrate: progesterone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature D309L to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y305F with inferred residue-numbering offset +12 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature E127D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H222I to reconstruct the assayed variant sequence.


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R304L with inferred residue-numbering offset -3 to reconstruct the assayed variant sequence.


organism: Rattus norvegicus

proof_lines: +/-0.4, A, B and C loop changed, totally converted enzyme

proof_lines: +/-0.4, A and C loop changed, bifunctional enzyme


assay_conditions_summary: pH 7

source_databases_merged: brenda uniprot


proof_lines:
pH 7.0, 25°C
Raw SKiD Env: Temp=25°C, pH=7
Raw SKiD Env: Temp=25°C, pH=7.4

source_databases_merged: brenda skid uniprot


proof_lines: kcat is 9.7 sec(-1) with sepiapterin as substrate (PubMed:10350607). kcat is 11.1 sec(-1) with NADPH as substrate (PubMed:10350607).


proof_lines:
NADPH, intact cells
pH 7.0, 25°C
NADPH, cell homogenate


substrate_name: thionicotinamide adenine dinucleotide phosphate


substrate_name: 3-acetylpyridine adenine dinucleotide phosphate


organism: [Clostridium] scindens

substrate_name: NADH

sequence: AVKVAINGFGR

wild_type_sequence: AVKVAINGFGR

assay_conditions_summary: cofactor NADH

substrate: NADH


substrate_name: NAD+

assay_conditions_summary: cofactor NAD+

substrate: NAD+


organism: Oryctolagus cuniculus

substrate_name: all-trans-retinal

assay_conditions_summary: pH 7.4; buffer 0.1 M potassium phosphate; cofactor NADPH

column_label: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone.; row label: all- trans -Retinal; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone. row all- trans -Retinal reports Km=8.9 uM, kcat=0.51 min^-1, and kcat/Km=0.057 min^-1 uM^-1.

row_label: all- trans -Retinal

substrate: all-trans-retinal


smiles: CCCCCC(C=CC=O)O

column_label: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone.; row label: 4-Hydroxy-2-nonenal; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone. row 4-Hydroxy-2-nonenal reports Km=5.3 uM, kcat=0.52 min^-1, and kcat/Km=0.098 min^-1 uM^-1.


column_label: Table 2. Kinetic Constants for Hydroxysteroids and Other Alcohols Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) 17β-Hydroxysteroids 5β-Androstane-3α,17β-diol 1.4 15 11 5α-Androstane-3α,17β-diol 4.2 16 3.8 5-Androstene-3β,17β-diol 3.1 6.0 1.9 5β-Androstan-17β-ol-3-one 6.2 9.2 1.5 5α-Androstane-3β,17β-diol 2.2 1.9 0.86 5β-Androstane-3β,17β-diol 2.5 2.0 0.80 Testosterone 13 3.4 0.26 17β-Estradiol 1.3 0.67 0.52 5α-Dihydrotestosterone 18 2.8 0.16 20α-Hydroxysteroids 5β-Pregnane-3α,20α-diol 7.8 17 2.2 5α-Pregnane-3α,20α-diol 0.8 1.5 1.8 5β-Pregnan-20α-ol-3-one 5.7 9.2 1.6 20α-Hydroxyprogesterone 2.2 2.9 1.3 5α-Pregnan-20α-ol-3-one 11 9.5 0.86 Non-steroidal alcohols β-Ionol 18 14 0.61 ( S )-1-Tetralol 112 13 0.12 ( S )-1-Indanol 131 12 0.092 4-Chromanol 152 4.1 0.027 trans -Benzene dihydrodiol 260 6.5 0.025 Geraniol 180 2.0 0.011; row label: 17β-Estradiol; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 2. Kinetic Constants for Hydroxysteroids and Other Alcohols Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) 17β-Hydroxysteroids 5β-Androstane-3α,17β-diol 1.4 15 11 5α-Androstane-3α,17β-diol 4.2 16 3.8 5-Androstene-3β,17β-diol 3.1 6.0 1.9 5β-Androstan-17β-ol-3-one 6.2 9.2 1.5 5α-Androstane-3β,17β-diol 2.2 1.9 0.86 5β-Androstane-3β,17β-diol 2.5 2.0 0.80 Testosterone 13 3.4 0.26 17β-Estradiol 1.3 0.67 0.52 5α-Dihydrotestosterone 18 2.8 0.16 20α-Hydroxysteroids 5β-Pregnane-3α,20α-diol 7.8 17 2.2 5α-Pregnane-3α,20α-diol 0.8 1.5 1.8 5β-Pregnan-20α-ol-3-one 5.7 9.2 1.6 20α-Hydroxyprogesterone 2.2 2.9 1.3 5α-Pregnan-20α-ol-3-one 11 9.5 0.86 Non-steroidal alcohols β-Ionol 18 14 0.61 ( S )-1-Tetralol 112 13 0.12 ( S )-1-Indanol 131 12 0.092 4-Chromanol 152 4.1 0.027 trans -Benzene dihydrodiol 260 6.5 0.025 Geraniol 180 2.0 0.011 row 17β-Estradiol reports Km=1.3 uM, kcat=0.67 min^-1, and kcat/Km=0.52 min^-1 uM^-1.


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

column_label: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone.; row label: 4-Oxo-2-hexenal; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone. row 4-Oxo-2-hexenal reports Km=5.9 uM, kcat=0.69 min^-1, and kcat/Km=0.11 min^-1 uM^-1.


substrate_name: estrone

column_label: Table 1. Kinetic Constants for Ketosteroids Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) 3-Ketosteroids a ) 5α-Pregnan-20α-ol-3-one 5.9 4.6 0.78 5α-Dihydrotestosterone 3.4 1.5 0.44 17-Ketosteroids 4-Androstene-3,17-dione 1.0 2.6 2.6 5β-Androstan-3α-ol-17-one 1.7 4.0 2.4 DHEA 6.0 9.3 1.6 5α-Androstan-3α-ol-17-one 4.1 5.1 1.2 DHEA-3-sulfate 4.2 4.8 1.1 5β-Androstan-3β-ol-17-one 2.8 2.7 0.96 Estrone 1.1 1.0 0.91 7α-Hydroxy-DHEA 2.9 2.6 0.90 Estrone-3-sulfate 6.7 5.9 0.88 5α-Androstan-3β-ol-17-one 6.0 5.0 0.83 20-Ketosteroids Progesterone 0.6 1.6 2.7 5α-Pregnane-3,20-dione 0.5 1.1 2.2 4-Pregnen-3α-ol-20-one 1.0 1.9 1.9 5β-Pregnan-3α-ol-20-one 1.0 1.8 1.8 5β-Pregnane-3,20-dione 1.0 1.7 1.7 5α-Pregnan-3α-ol-20-one 1.3 1.9 1.5 5β-Pregnane-3α,21-diol-20-one 2.6 1.0 0.38 5α-Pregnane-3α,21-diol-20-one 6.2 1.1 0.18 a ) 5β-Androstan-17β-ol-3-one, 5β-pregnan-20α-ol-3-one, testosterone and 20α-hydroxyprogesterone were not reduced.; row label: Estrone; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 1. Kinetic Constants for Ketosteroids Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) 3-Ketosteroids a ) 5α-Pregnan-20α-ol-3-one 5.9 4.6 0.78 5α-Dihydrotestosterone 3.4 1.5 0.44 17-Ketosteroids 4-Androstene-3,17-dione 1.0 2.6 2.6 5β-Androstan-3α-ol-17-one 1.7 4.0 2.4 DHEA 6.0 9.3 1.6 5α-Androstan-3α-ol-17-one 4.1 5.1 1.2 DHEA-3-sulfate 4.2 4.8 1.1 5β-Androstan-3β-ol-17-one 2.8 2.7 0.96 Estrone 1.1 1.0 0.91 7α-Hydroxy-DHEA 2.9 2.6 0.90 Estrone-3-sulfate 6.7 5.9 0.88 5α-Androstan-3β-ol-17-one 6.0 5.0 0.83 20-Ketosteroids Progesterone 0.6 1.6 2.7 5α-Pregnane-3,20-dione 0.5 1.1 2.2 4-Pregnen-3α-ol-20-one 1.0 1.9 1.9 5β-Pregnan-3α-ol-20-one 1.0 1.8 1.8 5β-Pregnane-3,20-dione 1.0 1.7 1.7 5α-Pregnan-3α-ol-20-one 1.3 1.9 1.5 5β-Pregnane-3α,21-diol-20-one 2.6 1.0 0.38 5α-Pregnane-3α,21-diol-20-one 6.2 1.1 0.18 a ) 5β-Androstan-17β-ol-3-one, 5β-pregnan-20α-ol-3-one, testosterone and 20α-hydroxyprogesterone were not reduced. row Estrone reports Km=1.1 uM, kcat=1.0 min^-1, and kcat/Km=0.91 min^-1 uM^-1.

row_label: Estrone

substrate: estrone


assay_conditions_summary: pH 7.4; buffer 0.1 M potassium phosphate; cofactor NADP+

column_label: Table 1; row_label: 5alpha-Pregnane-3alpha,21-diol-20-one; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

normalized_value_unit_evidence: normalized: kcat=0.018 s^-1; Km=0.0062 mM; kcat/Km=3 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for 5alpha-Pregnane-3alpha,21-diol-20-one: Km=6.2 uM; kcat=1.1 min^-1; kcat/Km=0.18 min^-1 uM^-1

table_label: Table 1


column_label: Table 1; row_label: 5beta-Pregnane-3alpha,21-diol-20-one; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for 5beta-Pregnane-3alpha,21-diol-20-one: Km=2.6 uM; kcat=1 min^-1; kcat/Km=0.38 min^-1 uM^-1


column_label: Table 1; row_label: 5beta-Pregnane-3,20-dione; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for 5beta-Pregnane-3,20-dione: Km=1 uM; kcat=1.7 min^-1; kcat/Km=1.7 min^-1 uM^-1


column_label: Table 1; row_label: 5alpha-Pregnane-3,20-dione; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for 5alpha-Pregnane-3,20-dione: Km=0.5 uM; kcat=1.1 min^-1; kcat/Km=2.2 min^-1 uM^-1


smiles: CCCCCCC=CC=O

column_label: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone.; row label: trans -2-Nonenal; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone. row trans -2-Nonenal reports Km=5.5 uM, kcat=1.2 min^-1, and kcat/Km=0.22 min^-1 uM^-1.

row_label: trans -2-Nonenal


substrate_name: ketotifen

column_label: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone.; row label: Ketotifen; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone. row Ketotifen reports Km=111 uM, kcat=1.2 min^-1, and kcat/Km=0.011 min^-1 uM^-1.

row_label: Ketotifen

substrate: ketotifen


substrate_name: isocaproaldehyde

smiles: CC(C)CCC=O

column_label: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone.; row label: Isocaproaldehyde; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone. row Isocaproaldehyde reports Km=68 uM, kcat=1.4 min^-1, and kcat/Km=0.021 min^-1 uM^-1.

row_label: Isocaproaldehyde

substrate: isocaproaldehyde


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

column_label: Table 3; row_label: 3-Deoxyglucosone; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for 3-Deoxyglucosone: Km=1400 uM; kcat=11 min^-1; kcat/Km=0.008 min^-1 uM^-1

table_label: Table 3


column_label: Table 3; row_label: TBQ; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for TBQ: Km=1 uM; kcat=11 min^-1; kcat/Km=11 min^-1 uM^-1

row_label: TBQ


column_label: Table 2; row_label: (S)-1-Indanol; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 2 cells for (S)-1-Indanol: Km=131 uM; kcat=12 min^-1; kcat/Km=0.092 min^-1 uM^-1

table_label: Table 2


column_label: Table 2; row_label: (S)-1-Tetralol; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

normalized_value_unit_evidence: normalized: kcat=0.217 s^-1; Km=0.112 mM; kcat/Km=2 s^-1 mM^-1

raw_value_unit_evidence: paper Table 2 cells for (S)-1-Tetralol: Km=112 uM; kcat=13 min^-1; kcat/Km=0.12 min^-1 uM^-1


substrate_name: beta-ionol

column_label: Table 2; row_label: beta-Ionol; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 2 cells for beta-Ionol: Km=18 uM; kcat=14 min^-1; kcat/Km=0.61 min^-1 uM^-1

row_label: beta-Ionol

substrate: beta-ionol


column_label: Table 2; row_label: 5-Androstene-3beta,17beta-diol; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 2 cells for 5-Androstene-3beta,17beta-diol: Km=3.1 uM; kcat=6 min^-1; kcat/Km=1.9 min^-1 uM^-1


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

column_label: Table 3; row_label: 4-Oxo-2-nonenal; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for 4-Oxo-2-nonenal: Km=1.8 uM; kcat=6.7 min^-1; kcat/Km=3.7 min^-1 uM^-1


column_label: Table 3; row_label: 4-Nitroacetophenone; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for 4-Nitroacetophenone: Km=1.2 uM; kcat=6.7 min^-1; kcat/Km=5.6 min^-1 uM^-1


substrate_name: befunolol

column_label: Table 3; row_label: Befunolol; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for Befunolol: Km=34 uM; kcat=7 min^-1; kcat/Km=0.79 min^-1 uM^-1

row_label: Befunolol

substrate: befunolol


substrate_name: methylglyoxal

smiles: CC(=O)C=O

column_label: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone.; row label: Methylglyoxal; columns: Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1).

raw_value_unit_evidence: Table 3. Kinetic Constants for Non-steroidal Carbonyl Compounds Substrate K m (μ M ) k cat (min −1 ) k cat / K m (min −1 μ M −1 ) Endogenous ketones Isatin 0.6 8.2 14 Diacetyl 19 9.5 0.50 Methylglyoxal 88 7.2 0.082 Acetoin 162 5.8 0.080 3-Deoxyglucosone 1400 11 0.008 Endogenous aldehydes 4-Oxo-2-nonenal 1.8 6.7 3.7 1-Nonanal 0.9 1.9 2.1 1-Hexanal 7.6 2.6 0.34 trans -2-Nonenal 5.5 1.2 0.22 trans -2-Hexenal 7.4 1.5 0.20 Acrolein 14 2.1 0.15 4-Oxo-2-hexenal 5.9 0.69 0.11 4-Hydroxy-2-nonenal 5.3 0.52 0.098 all- trans -Retinal 8.9 0.51 0.057 Isocaproaldehyde 68 1.4 0.021 Xenobiotics TBQ a ) 1.0 11 11 4-Nitroacetophenone 1.2 6.7 5.6 TBE 2.0 10 5.0 Befunolol 34 7.0 0.79 Pyridine-3-aldehyde 61 7.9 0.13 Menadione 18 7.5 0.12 α-Tetralone 53 3.2 0.060 Ketotifen 111 1.2 0.011 a ) 2- tert -Butyl-1,4-benzoquinone. row Methylglyoxal reports Km=88 uM, kcat=7.2 min^-1, and kcat/Km=0.082 min^-1 uM^-1.

row_label: Methylglyoxal

substrate: methylglyoxal


substrate_name: menadione

column_label: Table 3; row_label: Menadione; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

normalized_value_unit_evidence: normalized: kcat=0.125 s^-1; Km=0.018 mM; kcat/Km=2 s^-1 mM^-1

raw_value_unit_evidence: paper Table 3 cells for Menadione: Km=18 uM; kcat=7.5 min^-1; kcat/Km=0.12 min^-1 uM^-1

row_label: Menadione

substrate: menadione


substrate_name: pyridine 3-aldehyde

column_label: Table 3; row_label: Pyridine-3-aldehyde; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for Pyridine-3-aldehyde: Km=61 uM; kcat=7.9 min^-1; kcat/Km=0.13 min^-1 uM^-1

substrate: pyridine 3-aldehyde


substrate_name: isatin

column_label: Table 3; row_label: Isatin; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for Isatin: Km=0.6 uM; kcat=8.2 min^-1; kcat/Km=14 min^-1 uM^-1

row_label: Isatin

substrate: isatin


substrate_name: dehydroepiandrosterone

column_label: Table 1; row_label: DHEA; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for DHEA: Km=6 uM; kcat=9.3 min^-1; kcat/Km=1.6 min^-1 uM^-1

row_label: DHEA

substrate: dehydroepiandrosterone


substrate_name: diacetyl

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

column_label: Table 3; row_label: Diacetyl; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for Diacetyl: Km=19 uM; kcat=9.5 min^-1; kcat/Km=0.5 min^-1 uM^-1

row_label: Diacetyl

substrate: diacetyl


substrate_name: D-glyceraldehyde

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

substrate: D-glyceraldehyde


substrate_name: ethyl 3-oxovalerate

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

substrate: ethyl 3-oxovalerate


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


substrate_name: D-Lactaldehyde

smiles: CC(C=O)O

substrate: D-Lactaldehyde


substrate_name: ethyl benzoylacetate

substrate: ethyl benzoylacetate


substrate_name: (S)-ethyl 3-hydroxybutyrate

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

substrate: (S)-ethyl 3-hydroxybutyrate


substrate_name: DL-glyceraldehyde 3-phosphate

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

substrate: DL-glyceraldehyde 3-phosphate


substrate_name: hexanal

smiles: CCCCCC=O

column_label: Table 3; row_label: 1-Hexanal; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for 1-Hexanal: Km=7.6 uM; kcat=2.6 min^-1; kcat/Km=0.34 min^-1 uM^-1

substrate: hexanal


column_label: Table 1; row_label: 5alpha-Androstan-3beta-ol-17-one; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for 5alpha-Androstan-3beta-ol-17-one: Km=6 uM; kcat=5 min^-1; kcat/Km=0.83 min^-1 uM^-1


column_label: Table 1; row_label: 5alpha-Androstan-3alpha-ol-17-one; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for 5alpha-Androstan-3alpha-ol-17-one: Km=4.1 uM; kcat=5.1 min^-1; kcat/Km=1.2 min^-1 uM^-1


column_label: Table 1; row_label: 5beta-Androstan-3alpha-ol-17-one; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for 5beta-Androstan-3alpha-ol-17-one: Km=1.7 uM; kcat=4 min^-1; kcat/Km=2.4 min^-1 uM^-1


column_label: Table 2; row_label: 20alpha-Hydroxyprogesterone; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 2 cells for 20alpha-Hydroxyprogesterone: Km=2.2 uM; kcat=2.9 min^-1; kcat/Km=1.3 min^-1 uM^-1


substrate_name: alpha-tetralone

column_label: Table 3; row_label: alpha-Tetralone; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

normalized_value_unit_evidence: normalized: kcat=0.053 s^-1; Km=0.053 mM; kcat/Km=1 s^-1 mM^-1

raw_value_unit_evidence: paper Table 3 cells for alpha-Tetralone: Km=53 uM; kcat=3.2 min^-1; kcat/Km=0.06 min^-1 uM^-1

row_label: alpha-Tetralone

substrate: alpha-tetralone


substrate_name: testosterone

column_label: Table 2; row_label: Testosterone; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 2 cells for Testosterone: Km=13 uM; kcat=3.4 min^-1; kcat/Km=0.26 min^-1 uM^-1

row_label: Testosterone

substrate: testosterone


column_label: Table 2; row_label: 4-Chromanol; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 2 cells for 4-Chromanol: Km=152 uM; kcat=4.1 min^-1; kcat/Km=0.027 min^-1 uM^-1


kcat_over_km_origin: calculated


substrate_name: dehydroepiandrosterone 3-sulfate

column_label: Table 1; row_label: DHEA-3-sulfate; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for DHEA-3-sulfate: Km=4.2 uM; kcat=4.8 min^-1; kcat/Km=1.1 min^-1 uM^-1

substrate: dehydroepiandrosterone 3-sulfate


substrate_name: acetoin

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

column_label: Table 3; row_label: Acetoin; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for Acetoin: Km=162 uM; kcat=5.8 min^-1; kcat/Km=0.08 min^-1 uM^-1

row_label: Acetoin

substrate: acetoin


substrate_name: Estrone 3-sulfate

column_label: Table 1; row_label: Estrone-3-sulfate; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for Estrone-3-sulfate: Km=6.7 uM; kcat=5.9 min^-1; kcat/Km=0.88 min^-1 uM^-1

substrate: Estrone 3-sulfate


substrate_name: n-octyl acetoacetate

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

substrate: n-octyl acetoacetate


substrate_name: n-hexyl acetoacetate

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

substrate: n-hexyl acetoacetate


proof_lines:
Tetrahymena pyriformis
20 alpha-hydroxysteroid dehydrogenase


substrate_name: n-butyl acetoacetate

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

substrate: n-butyl acetoacetate


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


substrate_name: benzyl acetoacetate

substrate: benzyl acetoacetate


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


substrate_name: ethyl 2-methylacetoacetate

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

substrate: ethyl 2-methylacetoacetate


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


substrate_name: ethyl acetoacetate

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

substrate: ethyl acetoacetate


substrate_name: acetoacetyl-CoA

assay_conditions_summary: cofactor CoA

substrate: acetoacetyl-CoA


substrate_name: ethyl pyruvate

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

substrate: ethyl pyruvate


substrate_name: ethyl 4-chloroacetoacetate

smiles: CCOC(=O)CC(=O)CCl

substrate: ethyl 4-chloroacetoacetate


substrate_name: isatin

substrate: isatin


substrate_name: methyl acetoacetate

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

substrate: methyl acetoacetate


substrate_name: (S)-methyl 3-hydroxybutyrate

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

substrate: (S)-methyl 3-hydroxybutyrate


smiles: CC(C(C)O)O


column_label: Table 2; row_label: 5alpha-Pregnane-3alpha,20alpha-diol; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 2 cells for 5alpha-Pregnane-3alpha,20alpha-diol: Km=0.8 uM; kcat=1.5 min^-1; kcat/Km=1.8 min^-1 uM^-1


smiles: CCCC=CC=O

column_label: Table 3; row_label: trans-2-Hexenal; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for trans-2-Hexenal: Km=7.4 uM; kcat=1.5 min^-1; kcat/Km=0.2 min^-1 uM^-1


substrate_name: progesterone

column_label: Table 1; row_label: Progesterone; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for Progesterone: Km=0.6 uM; kcat=1.6 min^-1; kcat/Km=2.7 min^-1 uM^-1

row_label: Progesterone

substrate: progesterone


column_label: Table 1; row_label: 5alpha-Pregnan-3alpha-ol-20-one; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for 5alpha-Pregnan-3alpha-ol-20-one: Km=1.3 uM; kcat=1.9 min^-1; kcat/Km=1.5 min^-1 uM^-1


column_label: Table 1; row_label: 5beta-Pregnan-3alpha-ol-20-one; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

normalized_value_unit_evidence: normalized: kcat=0.03 s^-1; Km=0.001 mM; kcat/Km=30 s^-1 mM^-1

raw_value_unit_evidence: paper Table 1 cells for 5beta-Pregnan-3alpha-ol-20-one: Km=1 uM; kcat=1.8 min^-1; kcat/Km=1.8 min^-1 uM^-1


km_display: Not reported

column_label: Table 2; row_label: 5alpha-Androstane-3alpha,17beta-diol; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 2 cells for 5alpha-Androstane-3alpha,17beta-diol: Km=4.2 uM; kcat=16 min^-1; kcat/Km=3.8 min^-1 uM^-1


column_label: Table 2; row_label: 5beta-Androstane-3alpha,17beta-diol; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 2 cells for 5beta-Androstane-3alpha,17beta-diol: Km=1.4 uM; kcat=15 min^-1; kcat/Km=11 min^-1 uM^-1


substrate_name: Nonanal

smiles: CCCCCCCCC=O

column_label: Table 3; row_label: 1-Nonanal; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for 1-Nonanal: Km=0.9 uM; kcat=1.9 min^-1; kcat/Km=2.1 min^-1 uM^-1

substrate: Nonanal


substrate_name: geraniol

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

column_label: Table 2; row_label: Geraniol; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 2 cells for Geraniol: Km=180 uM; kcat=2 min^-1; kcat/Km=0.011 min^-1 uM^-1

row_label: Geraniol

substrate: geraniol


substrate_name: acrolein

smiles: C=CC=O

column_label: Table 3; row_label: Acrolein; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 3 cells for Acrolein: Km=14 uM; kcat=2.1 min^-1; kcat/Km=0.15 min^-1 uM^-1

row_label: Acrolein

substrate: acrolein


column_label: Table 1; row_label: 4-Androstene-3,17-dione; columns Km (uM), kcat (min^-1), kcat/Km (min^-1 uM^-1)

raw_value_unit_evidence: paper Table 1 cells for 4-Androstene-3,17-dione: Km=1 uM; kcat=2.6 min^-1; kcat/Km=2.6 min^-1 uM^-1


proof_lines: H+ + NADPH + 5alpha-Pregnane-3,20-dione = NADP+ + 20alpha-Hydroxy-5alpha-pregnan-3-one


source_db: oed

assay_conditions_summary: pH 7; 298.15 K; cofactor NAD+

column_label: Table 1, substrate row '4-Pregnen-20α-ol-3-one (Oxi)', AKR1C4 column group: Km cell = 0.3, kcat cell = 0.34, kcat/Km cell = 1.1. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.34 min^-1 normalizes to 0.005666666666666667 s^-1 (divide by 60); Km raw 0.3 uM normalizes to 0.0003 mM (divide by 1000); kcat/Km = 0.005666666666666667 s^-1 / 0.0003 mM = 18.888888888888893 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 1.1 min^-1 uM^-1 normalizes to 18.333333333333332 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '4-Pregnen-20α-ol-3-one (Oxi)'; AKR1C4 column group; Km cell = 0.3 uM; kcat cell = 0.34 min^-1; printed kcat/Km cell = 1.1 min^-1 uM^-1.

row_label: 4-Pregnen-20α-ol-3-one (Oxi) | AKR1C4 column group

table_label: Table 1. Comparison of kinetic constants for substrate pairs in the reduction and oxidation catalyzed by human AKR1C isoenzymes

source: oed


column_label: Table 1, substrate row '4-Pregnen-20α-ol-3-one (Oxi)', AKR1C2 column group: Km cell = 7.3, kcat cell = 0.13, kcat/Km cell = 0.02. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.13 min^-1 normalizes to 0.0021666666666666666 s^-1 (divide by 60); Km raw 7.3 uM normalizes to 0.0073 mM (divide by 1000); kcat/Km = 0.0021666666666666666 s^-1 / 0.0073 mM = 0.2968036529680365 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.02 min^-1 uM^-1 normalizes to 0.3333333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '4-Pregnen-20α-ol-3-one (Oxi)'; AKR1C2 column group; Km cell = 7.3 uM; kcat cell = 0.13 min^-1; printed kcat/Km cell = 0.02 min^-1 uM^-1.

row_label: 4-Pregnen-20α-ol-3-one (Oxi) | AKR1C2 column group


assay_conditions_summary: pH 7; 298.15 K; cofactor NADP+

column_label: Table 1, substrate row '5α-Pregnan-20α-ol-3-one (Oxi)', AKR1C4 column group: Km cell = 0.2, kcat cell = 0.64, kcat/Km cell = 3.2. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.64 min^-1 normalizes to 0.010666666666666666 s^-1 (divide by 60); Km raw 0.2 uM normalizes to 0.0002 mM (divide by 1000); kcat/Km = 0.010666666666666666 s^-1 / 0.0002 mM = 53.33333333333333 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 3.2 min^-1 uM^-1 normalizes to 53.333333333333336 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-Pregnan-20α-ol-3-one (Oxi)'; AKR1C4 column group; Km cell = 0.2 uM; kcat cell = 0.64 min^-1; printed kcat/Km cell = 3.2 min^-1 uM^-1.

row_label: 5α-Pregnan-20α-ol-3-one (Oxi) | AKR1C4 column group


column_label: Table 1, substrate row '5α-Pregnan-20α-ol-3-one (Oxi)', AKR1C1 column group: Km cell = 2.7, kcat cell = 9.1, kcat/Km cell = 3.4. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 9.1 min^-1 normalizes to 0.15166666666666667 s^-1 (divide by 60); Km raw 2.7 uM normalizes to 0.0027 mM (divide by 1000); kcat/Km = 0.15166666666666667 s^-1 / 0.0027 mM = 56.172839506172835 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 3.4 min^-1 uM^-1 normalizes to 56.666666666666664 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-Pregnan-20α-ol-3-one (Oxi)'; AKR1C1 column group; Km cell = 2.7 uM; kcat cell = 9.1 min^-1; printed kcat/Km cell = 3.4 min^-1 uM^-1.

row_label: 5α-Pregnan-20α-ol-3-one (Oxi) | AKR1C1 column group


column_label: Table 1, substrate row '5β-Pregnan-20α-ol-3-one (Oxi)', AKR1C4 column group: Km cell = 0.3, kcat cell = 0.50, kcat/Km cell = 1.7. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.50 min^-1 normalizes to 0.008333333333333333 s^-1 (divide by 60); Km raw 0.3 uM normalizes to 0.0003 mM (divide by 1000); kcat/Km = 0.008333333333333333 s^-1 / 0.0003 mM = 27.77777777777778 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 1.7 min^-1 uM^-1 normalizes to 28.333333333333332 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5β-Pregnan-20α-ol-3-one (Oxi)'; AKR1C4 column group; Km cell = 0.3 uM; kcat cell = 0.50 min^-1; printed kcat/Km cell = 1.7 min^-1 uM^-1.

row_label: 5β-Pregnan-20α-ol-3-one (Oxi) | AKR1C4 column group


column_label: Table 1, substrate row '3α5α-THP (Red)', AKR1C4 column group: Km cell = 0.9, kcat cell = 0.6, kcat/Km cell = 0.67. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.6 min^-1 normalizes to 0.01 s^-1 (divide by 60); Km raw 0.9 uM normalizes to 0.0009 mM (divide by 1000); kcat/Km = 0.01 s^-1 / 0.0009 mM = 11.111111111111112 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.67 min^-1 uM^-1 normalizes to 11.166666666666666 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '3α5α-THP (Red)'; AKR1C4 column group; Km cell = 0.9 uM; kcat cell = 0.6 min^-1; printed kcat/Km cell = 0.67 min^-1 uM^-1.

row_label: 3α5α-THP (Red) | AKR1C4 column group


column_label: Table 1, substrate row '3α5α-THP (Red)', AKR1C2 column group: Km cell = 3.1, kcat cell = 0.26, kcat/Km cell = 0.08. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.26 min^-1 normalizes to 0.004333333333333333 s^-1 (divide by 60); Km raw 3.1 uM normalizes to 0.0031 mM (divide by 1000); kcat/Km = 0.004333333333333333 s^-1 / 0.0031 mM = 1.3978494623655915 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.08 min^-1 uM^-1 normalizes to 1.3333333333333333 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '3α5α-THP (Red)'; AKR1C2 column group; Km cell = 3.1 uM; kcat cell = 0.26 min^-1; printed kcat/Km cell = 0.08 min^-1 uM^-1.

row_label: 3α5α-THP (Red) | AKR1C2 column group


column_label: Table 1, substrate row '3α5α-THP (Red)', AKR1C1 column group: Km cell = 2.0, kcat cell = 4.4, kcat/Km cell = 2.2. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 4.4 min^-1 normalizes to 0.07333333333333333 s^-1 (divide by 60); Km raw 2.0 uM normalizes to 0.002 mM (divide by 1000); kcat/Km = 0.07333333333333333 s^-1 / 0.002 mM = 36.666666666666664 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 2.2 min^-1 uM^-1 normalizes to 36.666666666666664 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '3α5α-THP (Red)'; AKR1C1 column group; Km cell = 2.0 uM; kcat cell = 4.4 min^-1; printed kcat/Km cell = 2.2 min^-1 uM^-1.

row_label: 3α5α-THP (Red) | AKR1C1 column group


assay_conditions_summary: pH 7; 298.15 K; cofactor NADPH

column_label: Table 1, substrate row '3α,5β-THP (Red)', AKR1C4 column group: Km cell = 0.5, kcat cell = 0.73, kcat/Km cell = 1.5. Km, kcat and kcat/Km come from the same substrate row and the same isoenzyme column group, so they are one measurement.

normalized_value_unit_evidence: kcat raw 0.73 min^-1 normalizes to 0.012166666666666666 s^-1 (divide by 60); Km raw 0.5 uM normalizes to 0.0005 mM (divide by 1000); kcat/Km = 0.012166666666666666 s^-1 / 0.0005 mM = 24.333333333333332 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 1.5 min^-1 uM^-1 normalizes to 25.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '3α,5β-THP (Red)'; AKR1C4 column group; Km cell = 0.5 uM; kcat cell = 0.73 min^-1; printed kcat/Km cell = 1.5 min^-1 uM^-1.

row_label: 3α,5β-THP (Red) | AKR1C4 column group


substrate_name: cortisone

assay_conditions_summary: pH 6.3; cofactor NADH

column_label: PMC209996 abstract reports cortisone reduction with Km = 22 microM; this normalizes to 0.022 mM.

raw_value_unit_evidence: Km raw_value=22 microM raw_unit=microM

row_label: Prose segment: cortisone reduction

table_label: PMC209996 abstract

substrate: cortisone


substrate_name: cortisol

column_label: PMC209996 abstract reports cortisol reduction with Km = 32 microM; this normalizes to 0.032 mM.

raw_value_unit_evidence: Km raw_value=32 microM raw_unit=microM

row_label: Prose segment: cortisol reduction

substrate: cortisol


assay_conditions_summary: pH 7.9; cofactor NAD+

column_label: PMC209996 abstract reports 20alpha-dihydrocortisol oxidation with Km = 41 microM; this normalizes to 0.041 mM.

raw_value_unit_evidence: Km raw_value=41 microM raw_unit=microM

row_label: Prose segment: 20alpha-dihydrocortisol oxidation


enzyme_display_name: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)

substrate_name: NADPH

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S46A/S196A/S214A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.4; 298.15 K; buffer 100 mM sodium phosphate; cofactor NADPH

column_label: Table 1: Kinetic parameters of phosphorylated and non-phosphorylated SPRs; row Non-phosphorylated rSPR (A46A196A214; S46A/S196A/S214A triple mutant); columns kcat(NADPH) (s^-1), Km(NADPH) (uM), kcat/Km(NADPH) (s^-1 uM^-1)

raw_value_unit_evidence: kcat: Table 1 Non-phosphorylated rSPR (A46A196A214; S46A/S196A/S214A triple mutant) column kcat(NADPH) (s^-1) = 10.5 s^-1; km: Table 1 Non-phosphorylated rSPR (A46A196A214; S46A/S196A/S214A triple mutant) column Km(NADPH) (uM) = 2.5 uM; kcat_over_km: Table 1 Non-phosphorylated rSPR (A46A196A214; S46A/S196A/S214A triple mutant) column kcat/Km(NADPH) (s^-1 uM^-1) = 4.2 s^-1 uM^-1

substrate: NADPH


column_label: Table 1: Kinetic parameters of phosphorylated and non-phosphorylated SPRs; row Non-phosphorylated rSPR (wild-type); columns kcat(NADPH) (s^-1), Km(NADPH) (uM), kcat/Km(NADPH) (s^-1 uM^-1)

raw_value_unit_evidence: kcat: Table 1 Non-phosphorylated rSPR (wild-type) column kcat(NADPH) (s^-1) = 11.1 s^-1; km: Table 1 Non-phosphorylated rSPR (wild-type) column Km(NADPH) (uM) = 2.8 uM; kcat_over_km: Table 1 Non-phosphorylated rSPR (wild-type) column kcat/Km(NADPH) (s^-1 uM^-1) = 4.0 s^-1 uM^-1

row_label: Non-phosphorylated rSPR (wild-type)

enzyme: sepiapterin reductase (L-erythro-7,8-dihydrobiopterin forming)


substrate_name: Sepiapterin

column_label: Table 1: Kinetic parameters of phosphorylated and non-phosphorylated SPRs; row Non-phosphorylated rSPR (A46A196A214; S46A/S196A/S214A triple mutant); columns kcat(Sepiapterin) (s^-1), Km(Sepiapterin) (uM), kcat/Km(Sepiapterin) (s^-1 uM^-1)

raw_value_unit_evidence: kcat: Table 1 Non-phosphorylated rSPR (A46A196A214; S46A/S196A/S214A triple mutant) column kcat(Sepiapterin) (s^-1) = 8.9 s^-1; km: Table 1 Non-phosphorylated rSPR (A46A196A214; S46A/S196A/S214A triple mutant) column Km(Sepiapterin) (uM) = 12.2 uM; kcat_over_km: Table 1 Non-phosphorylated rSPR (A46A196A214; S46A/S196A/S214A triple mutant) column kcat/Km(Sepiapterin) (s^-1 uM^-1) = 0.7 s^-1 uM^-1

substrate: Sepiapterin


column_label: Table 1: Kinetic parameters of phosphorylated and non-phosphorylated SPRs; row Non-phosphorylated rSPR (wild-type); columns kcat(Sepiapterin) (s^-1), Km(Sepiapterin) (uM), kcat/Km(Sepiapterin) (s^-1 uM^-1)

raw_value_unit_evidence: kcat: Table 1 Non-phosphorylated rSPR (wild-type) column kcat(Sepiapterin) (s^-1) = 9.7 s^-1; km: Table 1 Non-phosphorylated rSPR (wild-type) column Km(Sepiapterin) (uM) = 12.6 uM; kcat_over_km: Table 1 Non-phosphorylated rSPR (wild-type) column kcat/Km(Sepiapterin) (s^-1 uM^-1) = 0.8 s^-1 uM^-1


organism: Mus musculus


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S213A to reconstruct the assayed variant sequence.

column_label: Table 1: Kinetic parameters of phosphorylated and non-phosphorylated SPRs; row Non-phosphorylated hSPR (S213A; Table text S213CA); columns kcat(NADPH) (s^-1), Km(NADPH) (uM), kcat/Km(NADPH) (s^-1 uM^-1)

raw_value_unit_evidence: kcat: Table 1 Non-phosphorylated hSPR (S213A; Table text S213CA) column kcat(NADPH) (s^-1) = 1.3 s^-1; km: Table 1 Non-phosphorylated hSPR (S213A; Table text S213CA) column Km(NADPH) (uM) = 11.5 uM; kcat_over_km: Table 1 Non-phosphorylated hSPR (S213A; Table text S213CA) column kcat/Km(NADPH) (s^-1 uM^-1) = 0.1 s^-1 uM^-1


column_label: Table 1: Kinetic parameters of phosphorylated and non-phosphorylated SPRs; row Phosphorylated hSPR (wild-type); columns kcat(NADPH) (s^-1), Km(NADPH) (uM), kcat/Km(NADPH) (s^-1 uM^-1)

raw_value_unit_evidence: kcat: Table 1 Phosphorylated hSPR (wild-type) column kcat(NADPH) (s^-1) = 1.5 s^-1; km: Table 1 Phosphorylated hSPR (wild-type) column Km(NADPH) (uM) = 12.3 uM; kcat_over_km: Table 1 Phosphorylated hSPR (wild-type) column kcat/Km(NADPH) (s^-1 uM^-1) = 0.1 s^-1 uM^-1

row_label: Phosphorylated hSPR (wild-type)


column_label: Table 1: Kinetic parameters of phosphorylated and non-phosphorylated SPRs; row Non-phosphorylated hSPR (S213A; Table text S213CA); columns kcat(Sepiapterin) (s^-1), Km(Sepiapterin) (uM), kcat/Km(Sepiapterin) (s^-1 uM^-1)

raw_value_unit_evidence: kcat: Table 1 Non-phosphorylated hSPR (S213A; Table text S213CA) column kcat(Sepiapterin) (s^-1) = 1.3 s^-1; km: Table 1 Non-phosphorylated hSPR (S213A; Table text S213CA) column Km(Sepiapterin) (uM) = 13.5 uM; kcat_over_km: Table 1 Non-phosphorylated hSPR (S213A; Table text S213CA) column kcat/Km(Sepiapterin) (s^-1 uM^-1) = 0.09 s^-1 uM^-1


column_label: Table 1: Kinetic parameters of phosphorylated and non-phosphorylated SPRs; row Phosphorylated hSPR (wild-type); columns kcat(Sepiapterin) (s^-1), Km(Sepiapterin) (uM), kcat/Km(Sepiapterin) (s^-1 uM^-1)

raw_value_unit_evidence: kcat: Table 1 Phosphorylated hSPR (wild-type) column kcat(Sepiapterin) (s^-1) = 1.3 s^-1; km: Table 1 Phosphorylated hSPR (wild-type) column Km(Sepiapterin) (uM) = 13.7 uM; kcat_over_km: Table 1 Phosphorylated hSPR (wild-type) column kcat/Km(Sepiapterin) (s^-1 uM^-1) = 0.09 s^-1 uM^-1


organism: Dictyostelium discoideum

substrate_name: sepiapterin

column_label: The abstract reports Km values for NADPH and sepiapterin were 51.8+/-2.7 microM and 40+/-2 microM, respectively.

raw_value_unit_evidence: Km raw_value=40 microM raw_unit=microM

row_label: Prose segment: sepiapterin Km

table_label: PubMed PMID 10987137 abstract

substrate: sepiapterin


raw_value_unit_evidence: Km raw_value=51.8 microM raw_unit=microM

row_label: Prose segment: NADPH Km


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

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


substrate_name: Progesterone

substrate: Progesterone


column_label: Abstract states the Km value for 17 alpha-hydroxyprogesterone is 2.9 microM.

raw_value_unit_evidence: Km raw_value=2.9 raw_unit=microM

row_label: Tetrahymena pyriformis 20 alpha-hydroxysteroid dehydrogenase with 17 alpha-hydroxyprogesterone

table_label: PubMed abstract PMID 8280099


substrate_name: Camphorquinone

substrate: Camphorquinone


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


substrate_name: Phenylglyoxal

proof_lines: reduced several nonsteroidal carbonyl compounds

substrate: Phenylglyoxal


substrate_name: benzene dihydrodiol

substrate: benzene dihydrodiol


enzyme_display_name: UniProt G9FRD7

organism: Clostridium sardiniense

substrate_name: chenodeoxycholic acid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt G9FRD7

substrate: chenodeoxycholic acid


substrate_name: NADP+

proof_lines:
Raw SKiD Env: Temp=25°C, pH=8
Raw SKiD Env: Temp=-----, pH=-----

substrate: NADP+


column_label: Table 1; row 3alpha,5beta-THP (Red); AKR1C2 kcat/Km column; table note gives Km in uM and kcat in min^-1.

normalized_value_unit_evidence: normalized paper values: Km=0.0045 mM; kcat=0.42/60=0.007 s^-1; kcat/Km=0.09*1000/60=1.5 s^-1 mM^-1. Current export kcat/Km=1.4.

raw_value_unit_evidence: Table 1 row 3alpha,5beta-THP (Red), AKR1C2 columns: Km=4.5 uM; kcat=0.42 min^-1; kcat/Km=0.09 min^-1 uM^-1.

row_label: AKR1C2 / 3alpha,5beta-THP (Red)


column_label: Table 1; row 5alpha-DHP (Red); AKR1C4 kcat/Km column; table note gives Km in uM and kcat in min^-1.

raw_value_unit_evidence: Table 1 row 5alpha-DHP (Red), AKR1C4 columns: Km=0.6 uM; kcat=1.2 min^-1; kcat/Km=2.0 min^-1 uM^-1.

row_label: AKR1C4 / 5alpha-DHP (Red)


column_label: Table 1; row 5alpha-DHP (Red); AKR1C2 kcat/Km column; table note gives Km in uM and kcat in min^-1.

raw_value_unit_evidence: Table 1 row 5alpha-DHP (Red), AKR1C2 columns: Km=0.6 uM; kcat=0.48 min^-1; kcat/Km=0.70 min^-1 uM^-1.

row_label: AKR1C2 / 5alpha-DHP (Red)


column_label: Table 1; row 5alpha-DHP (Red); AKR1C1 kcat/Km column; table note gives Km in uM and kcat in min^-1.

raw_value_unit_evidence: Table 1 row 5alpha-DHP (Red), AKR1C1 columns: Km=1.1 uM; kcat=2.6 min^-1; kcat/Km=2.4 min^-1 uM^-1.

row_label: AKR1C1 / 5alpha-DHP (Red)


column_label: Table 1; row 5beta-DHP (Red); AKR1C4 kcat/Km column; table note gives Km in uM and kcat in min^-1.

raw_value_unit_evidence: Table 1 row 5beta-DHP (Red), AKR1C4 columns: Km=0.7 uM; kcat=3.4 min^-1; kcat/Km=4.9 min^-1 uM^-1.

row_label: AKR1C4 / 5beta-DHP (Red)


column_label: Table 1; row 5beta-DHP (Red); AKR1C2 kcat/Km column; table note gives Km in uM and kcat in min^-1.

raw_value_unit_evidence: Table 1 row 5beta-DHP (Red), AKR1C2 columns: Km=0.7 uM; kcat=1.1 min^-1; kcat/Km=1.6 min^-1 uM^-1.

row_label: AKR1C2 / 5beta-DHP (Red)


column_label: Table 1; row 5beta-DHP (Red); AKR1C1 kcat/Km column; table note gives Km in uM and kcat in min^-1.

raw_value_unit_evidence: Table 1 row 5beta-DHP (Red), AKR1C1 columns: Km=1.2 uM; kcat=3.0 min^-1; kcat/Km=2.5 min^-1 uM^-1.

row_label: AKR1C1 / 5beta-DHP (Red)


enzyme_display_name: glycerol 2-dehydrogenase (NADP+)

organism: Dunaliella parva

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

enzyme: glycerol 2-dehydrogenase (NADP+)


assay_conditions_summary: cofactor NADP+


substrate_name: dihydroxyacetone

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

substrate: dihydroxyacetone


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


enzyme_display_name: 7alpha-hydroxysteroid dehydrogenase

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

proof_lines: mutant enzyme T15A/R16A/R194A, pH and temperature not specified in the publication

enzyme: 7alpha-hydroxysteroid dehydrogenase


proof_lines: mutant enzyme R16A/R194A, pH and temperature not specified in the publication


proof_lines: mutant enzyme T15A, pH and temperature not specified in the publication


proof_lines: mutant enzyme R16A, pH and temperature not specified in the publication


proof_lines: mutant enzyme R194A, pH and temperature not specified in the publication


organism: Brevibacterium fuscum

substrate_name: cholic acid

substrate: cholic acid


substrate_name: NADH

proof_lines:
with dehydrocholic acid
with 7,12-diketolithocholic acid

substrate: NADH


substrate_name: NAD+

proof_lines:
with cholic acid
with 12-ketolithocholic acid

substrate: NAD+


substrate_name: 12-oxolithocholic acid

substrate: 12-oxolithocholic acid


substrate_name: Dehydrocholic acid

substrate: Dehydrocholic acid


substrate_name: 7,12-Diketolithocholic acid

substrate: 7,12-Diketolithocholic acid


organism: Phycomyces blakesleeanus

substrate_name: NADPH

substrate: NADPH


assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

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

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


proof_lines: mutant enzyme Q255L/C260S, at pH 8.0 and 25°C


organism: Schizosaccharomyces pombe


enzyme_display_name: 3-hydroxybutyryl-CoA dehydrogenase

organism: Clostridium kluyveri

assay_conditions_summary: pH 6.5; 298.15 K; cofactor CoA

enzyme: 3-hydroxybutyryl-CoA dehydrogenase


assay_conditions_summary: pH 6.5; 298.15 K; cofactor NADPH


proof_lines: mutant R194G, pH and temperature not specified in the publication


proof_lines: mutant R16G, pH and temperature not specified in the publication


enzyme_display_name: erythrulose reductase

organism: Bos taurus

assay_conditions_summary: cofactor NADPH

enzyme: erythrulose reductase


substrate_name: D-erythrulose

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

substrate: D-erythrulose


organism: Gluconobacter oxydans

assay_conditions_summary: pH 6.5; 298.15 K; buffer 50 mM potassium phosphate

proof_lines: at pH 6.5, in 50 mM potassium phosphate buffer, at 25°C


organism: Clostridium acetobutylicum

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H138A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; cofactor NADH


assay_conditions_summary: pH 7.5; cofactor CoA


organism: Stenotrophomonas maltophilia

assay_conditions_summary: pH 7.5; 295.15 K; cofactor NAD+


organism: Bacteroides fragilis

assay_conditions_summary: pH 8.5; cofactor NAD+

proof_lines: with cholic acid as substrate, pH 8.5, 37°C

proof_lines: with chenodeoxycholic acid as substrate, pH 8.5, 37°C


organism: Escherichia coli (strain K12)

substrate_name: NAD(+)

proof_lines: kcat is 3798 sec(-1) with cholate as substrate (PubMed:2007545). kcat is 491 sec(-1) with chenodeoxycholate as substrate (PubMed:2007545). kcat is 206 sec(-1) with taurochenodeoxycholate as substrate (PubMed:2007545). kcat is 188 sec(-1) wi

substrate: NAD(+)


enzyme_display_name: 3-hydroxyacyl-CoA dehydrogenase type-2

organism: Homo sapiens

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

assay_conditions_summary: cofactor CoA

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

enzyme: 3-hydroxyacyl-CoA dehydrogenase type-2


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


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


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


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


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

assay_conditions_summary: cofactor NADH


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


substrate_name: tetramyristoyl cardiolipin

assay_conditions_summary: pH 8; buffer 10 mM Tris-HCl pH 8; cofactor CoA

column_label: Table 1: Kinetic parameters of enzymes, row HSD10 with lipid species CL 14:0, column Km, raw_value=140 raw_unit=uM. Normalized to 0.14 mM.

normalized_value_unit_evidence: Km 140 uM -> 0.14 mM, matching CatLog 0.14 mM.

raw_value_unit_evidence: Table 1 row HSD10, lipid species CL 14:0: Km=140 uM; kcat/Km=0.74 min^-1 uM^-1.

table_label: Table 1: Kinetic parameters of enzymes

substrate: tetramyristoyl cardiolipin


substrate_name: tetralinoleoyl cardiolipin

column_label: Table 1: Kinetic parameters of enzymes, row HSD10 with lipid species CL 18:2, column Km, raw_value=148 raw_unit=uM. Normalized to 0.148 mM. A separate HSD10 CL 18:2(ox) row reports 40 uM for peroxidized CL and is excluded from this unoxidized substrate mapping.

normalized_value_unit_evidence: Km 148 uM -> 0.148 mM, matching CatLog 0.148 mM.

raw_value_unit_evidence: Table 1 row HSD10, lipid species CL 18:2: Km=148 uM; kcat/Km=0.72 min^-1 uM^-1.

substrate: tetralinoleoyl cardiolipin


substrate_name: chenodeoxycholic acid


substrate_name: cholic acid


substrate_name: NADP+


substrate_name: taurochenodeoxycholate

assay_conditions_summary: cofactor NAD+

column_label: PMC scanned page 2177 Table 5 visually shows taurochenodeoxycholic acid with Km 0.19 mM and kcat 206 s^-1.

raw_value_unit_evidence: Km raw_value=0.19 raw_unit=mM

row_label: Taurochenodeoxycholic acid

table_label: Table 5. Substrate specificity of 7alpha-hydroxysteroid dehydrogenase

substrate: taurochenodeoxycholate


substrate_name: chenodeoxycholate

column_label: PMC scanned page 2177 Table 5 visually shows chenodeoxycholic acid with Km 0.43 mM and kcat 491 s^-1.

raw_value_unit_evidence: Km raw_value=0.43 raw_unit=mM

row_label: Chenodeoxycholic acid

substrate: chenodeoxycholate


substrate_name: cholate

column_label: PMID 9722677 Table II, Wild-type row, Km (CA) column explicitly reports 0.361 mM; the table footnote defines CA as cholic acid.

raw_value_unit_evidence: Km raw_value=0.361 raw_unit=mM

row_label: Wild-type

table_label: Table II. Kinetic constants for the wild-type and mutant forms of the 7alpha-HSDH

substrate: cholate


substrate_name: glycocholate

column_label: PMC scanned page 2177 Table 5 visually shows glycocholic acid with Km 1.25 mM and kcat 25 s^-1.

raw_value_unit_evidence: Km raw_value=1.25 raw_unit=mM

row_label: Glycocholic acid

substrate: glycocholate


substrate_name: taurocholate

column_label: PMC scanned page 2177 Table 5 visually shows taurocholic acid with Km 2.0 mM and kcat 188 s^-1.

raw_value_unit_evidence: Km raw_value=2.0 raw_unit=mM

row_label: Taurocholic acid

substrate: taurocholate


organism: Trichoderma reesei

substrate_name: NADPH

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Results prose: GLD2 reductive reaction cofactor Km near Table 1; Results prose reports reductive Km for NADPH; column(s) prose Km for NADPH in reductive reaction

raw_value_unit_evidence: Km raw_value=50 raw_unit=uM

row_label: GLD2 / NADPH cofactor, reductive reaction prose


assay_conditions_summary: pH 9.5; cofactor NADP+

column_label: Results prose: GLD2 oxidative reaction cofactor Km near Table 1; Results prose reports oxidative Km for NADP; column(s) prose Km for NADP in oxidative reaction

raw_value_unit_evidence: Km raw_value=110 raw_unit=uM

row_label: GLD2 / NADP cofactor, oxidative reaction prose

substrate: NADP+


substrate_name: dihydroxyacetone

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; Table 1 row GLD2 / Dihydroxyacetone; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=1 raw_unit=mM

row_label: GLD2 / Dihydroxyacetone

substrate: dihydroxyacetone


substrate_name: glycerol

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; Table 1 row GLD2 / Glycerol; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=350 raw_unit=mM

row_label: GLD2 / Glycerol

substrate: glycerol


enzyme_display_name: glycerol 2-dehydrogenase (NADP(+))

substrate_name: methylglyoxal

smiles: CC(=O)C=O

assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD2 / methylglyoxal; column(s) Km (mM); Vmax kcat value in parentheses (s^-1); Vmax/Km normalized as kcat divided by Km (s^-1*mM^-1)

normalized_value_unit_evidence: kcat normalized_value=120 normalized_unit=s^-1; kcat/Km normalized_value=0.0032 normalized_unit=s^-1*mM^-1; Km normalized_value=37500 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=120 raw_unit=s^-1; kcat/Km raw_value=0.0032 raw_unit=s^-1*mM^-1; Km raw_value=37 500 raw_unit=mM

row_label: GLD2 / methylglyoxal

enzyme: glycerol 2-dehydrogenase (NADP(+))

substrate: methylglyoxal


substrate_name: Acetoin

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

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD2 / Acetoin; column(s) Km (mM); Vmax kcat value in parentheses (s^-1); Vmax/Km normalized as kcat divided by Km (s^-1*mM^-1)

normalized_value_unit_evidence: kcat normalized_value=21 normalized_unit=s^-1; kcat/Km normalized_value=0.185840707964602 normalized_unit=s^-1*mM^-1; Km normalized_value=113 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=21 raw_unit=s^-1; kcat/Km raw_value=0.185840707964602 raw_unit=s^-1*mM^-1; Km raw_value=113 raw_unit=mM

row_label: GLD2 / Acetoin

substrate: Acetoin


substrate_name: D-Glyceraldehyde

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD2 / D-Glyceraldehyde; column(s) Km (mM); Vmax kcat value in parentheses (s^-1); Vmax/Km normalized as kcat divided by Km (s^-1*mM^-1)

normalized_value_unit_evidence: kcat normalized_value=7.5 normalized_unit=s^-1; kcat/Km normalized_value=0.078125 normalized_unit=s^-1*mM^-1; Km normalized_value=96 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=7.5 raw_unit=s^-1; kcat/Km raw_value=0.078125 raw_unit=s^-1*mM^-1; Km raw_value=96 raw_unit=mM

row_label: GLD2 / D-Glyceraldehyde

substrate: D-Glyceraldehyde


substrate_name: Dihydroxyacetone

smiles: O=C(CO)CO

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

normalized_value_unit_evidence: kcat normalized_value=86 normalized_unit=s^-1; kcat/Km normalized_value=86 normalized_unit=s^-1*mM^-1; Km normalized_value=1 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=86 raw_unit=s^-1; kcat/Km raw_value=86 raw_unit=s^-1*mM^-1; Km raw_value=1 raw_unit=mM

substrate: Dihydroxyacetone


substrate_name: Dimethylglyoxal

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

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD2 / Diacetyl; column(s) Km (mM); Vmax kcat value in parentheses (s^-1); Vmax/Km normalized as kcat divided by Km (s^-1*mM^-1)

normalized_value_unit_evidence: kcat normalized_value=88 normalized_unit=s^-1; kcat/Km normalized_value=6.76923076923077 normalized_unit=s^-1*mM^-1; Km normalized_value=13 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=88 raw_unit=s^-1; kcat/Km raw_value=6.76923076923077 raw_unit=s^-1*mM^-1; Km raw_value=13 raw_unit=mM

row_label: GLD2 / Diacetyl

substrate: Dimethylglyoxal


substrate_name: Glyoxal

smiles: O=CC=O

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

normalized_value_unit_evidence: kcat normalized_value=9.2 normalized_unit=s^-1; kcat/Km normalized_value=0.306666666666667 normalized_unit=s^-1*mM^-1; Km normalized_value=30 normalized_unit=mM

raw_value_unit_evidence: kcat raw_value=9.2 raw_unit=s^-1; kcat/Km raw_value=0.306666666666667 raw_unit=s^-1*mM^-1; Km raw_value=30 raw_unit=mM

row_label: GLD2 / Glyoxal

substrate: Glyoxal


enzyme_display_name: Glycerol 2-dehydrogenase (NADP(+))

organism: Hypocrea jecorina

substrate_name: D-glyceraldehyde

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

enzyme: Glycerol 2-dehydrogenase (NADP(+))

substrate: D-glyceraldehyde


substrate_name: diacetyl

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

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD2 / diacetyl; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=13 raw_unit=mM

row_label: GLD2 / diacetyl

substrate: diacetyl


substrate_name: glyoxal

smiles: C(=O)C=O

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD2 / glyoxal; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=30 raw_unit=mM

row_label: GLD2 / glyoxal

substrate: glyoxal


column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; Table 1 row GLD2 / methylglyoxal; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=37 500 raw_unit=mM


substrate_name: acetoin

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

column_label: Table 1. Specificities and kinetic properties of histidine-tagged and purified GLD1 and GLD2; row GLD2 / acetoin; column(s) Km (mM)

raw_value_unit_evidence: Km raw_value=113 raw_unit=mM

row_label: GLD2 / acetoin

substrate: acetoin


organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: D,L-glyceraldehyde

proof_lines: rate of oxidation of NADPH in the presence of several substrates

substrate: D,L-glyceraldehyde


substrate: NADPH


substrate_name: p-nitrobenzaldehyde

substrate: p-nitrobenzaldehyde


substrate_name: benzaldehyde

substrate: benzaldehyde


substrate_name: phenylglyoxal

substrate: phenylglyoxal


substrate_name: acrolein

substrate: acrolein


substrate_name: butyraldehyde

smiles: CCCC=O

substrate: butyraldehyde


substrate_name: L-Glyceraldehyde

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

normalized_value_unit_evidence: kcat normalized_value=18 normalized_unit=s^-1; Km normalized_value=8 normalized_unit=mM; kcat/Km normalized_value=2.25 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: kcat raw_value=18 raw_unit=s^-1; Km raw_value=8 raw_unit=mM; kcat/Km raw_value=2250 raw_unit=s^-1*M^-1

row_label: GLD2 / L-Glyceraldehyde

substrate: L-Glyceraldehyde


substrate_name: NADP+

assay_conditions_summary: pH 9.5; 303.15 K; cofactor NADP+

column_label: Table label: Table 1. The specificities and kinetic properties of the histidine-tagged and purified GLD1 and GLD2. Row: Glycerol. Enzyme column: GLD2. Cell read: Vmax 1200 nkat/mg with kcat 56 s^-1 in parentheses, per the caption `The activities are given in nkat per mg of protein and in kcat (in parentheses).`. metric: kcat; raw value: 56; raw unit: s^-1; normalized value: 56.0 s^(-1). The Km is the NADP cofactor Km from the gld2 Results prose: `for NADP was 110 lm.`; metric: Km; raw value: 110; raw unit: uM; normalized value: 0.11 mM. metric: kcat/Km; raw unit: s^-1 mM^-1; normalized value: 509.09090909090907 s^-1 mM^-1, the quotient of the two quoted values. assay condition: Purified histidine-tagged GLD2; oxidative assay conditions were 200 mM Tris/HCl (pH 9.5) and 1 mM NADP. Export row conditions: pH 9.5.

normalized_value_unit_evidence: GLD2 oxidative reaction: kcat 56 s^-1 = 56.0 s^(-1) (Table 1 Glycerol row, GLD2 column, the parenthesized kcat of Vmax cell `1200 (56)`); Km for NADP 110 uM = 0.11 mM (1 uM = 0.001 mM), from the prose `for NADP was 110 lm.`; kcat/Km = 56.0 s^-1 / 0.11 mM = 509.09090909090907 s^-1 mM^-1 (quotient of the two quoted values; the paper prints no kcat/Km for the NADP cofactor). Rendering quirks of the PDF text extraction: the micro sign renders as the letter l, so `110 lm` is the paper's 110 uM and `350 mm` is 350 mM; the centered dot renders as Æ and superscript -1 flattens to )1, so `nkatÆmg)1` is nkat per mg and `s)1ÆM)1` is s^-1 M^-1. The two-column PDF layout interleaves left- and right-column text per extracted line, so the prose sentence is split across lines of the extraction.

raw_value_unit_evidence: Table 1 caption: `Table 1. The specificities and kinetic properties of the histidine-tagged and purified GLD1 and GLD2.` with `The activities are given in nkat per mg of protein and in kcat (in parentheses).`; metric header row: `Vmax (nkatÆmg)1Æs)1) Km (mM) Vmax ⁄ Km (s)1ÆM)1)`; enzyme header row: `GLD1 GLD2 GLD1 GLD2 GLD1 GLD2`; data row: `Glycerol ND 1200 (56) ND 350 160` | GLD2 cells read: Vmax = 1200 nkat/mg with kcat = 56 s^-1 in parentheses; Km (glycerol) = 350 mM; Vmax/Km = 160 s^-1 M^-1. The NADP cofactor Km comes from the gld2 Results prose sentence: `reaction, the Km for glycerol was 350 mm and the Km` continuing `for NADP was 110 lm.` which reads: in the oxidative reaction the Km for NADP = 110 uM.

row_label: GLD2 | Glycerol

substrate: NADP+


organism: Gallus gallus

substrate_name: ethyl pyruvate

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

substrate: ethyl pyruvate


assay_conditions_summary: pH 6.3; buffer pH 6; cofactor NADPH

column_label: Table II reports substrate row Acetoin, Km (mM) = 1.3 x 10; normalized Km = 13.0 mM.

normalized_value_unit_evidence: Km=13.0 mM; Table II reports values directly in mM using scientific notation where needed.

row_label: Acetoin / Km (mM) column

table_label: Table II / Kinetic constants for the substrates of D-erythrulose reductase from chicken liver


substrate_name: Phenanthrenequinone

column_label: Table II reports substrate row Phenanthrenequinone, Km (mM) = 2.1 x 10^-2; normalized Km = 0.021 mM.

normalized_value_unit_evidence: Km=0.021 mM; Table II reports values directly in mM using scientific notation where needed.

row_label: Phenanthrenequinone / Km (mM) column

substrate: Phenanthrenequinone


substrate_name: D-erythrulose

column_label: Table II reports substrate row D-Erythrulose, Km (mM) = 1.1 x 10^-1; normalized Km = 0.11 mM.

normalized_value_unit_evidence: Km=0.11 mM; Table II reports values directly in mM using scientific notation where needed.

row_label: D-Erythrulose / Km (mM) column

substrate: D-erythrulose


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

column_label: Table II reports substrate row 3,4-Hexanedione, Km (mM) = 1.9 x 10^-1; normalized Km = 0.19 mM.

normalized_value_unit_evidence: Km=0.19 mM; Table II reports values directly in mM using scientific notation where needed.

row_label: 3,4-Hexanedione / Km (mM) column


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

column_label: Table II reports substrate row 2,3-Pentanedione, Km (mM) = 2.4 x 10^-1; normalized Km = 0.24 mM.

normalized_value_unit_evidence: Km=0.24 mM; Table II reports values directly in mM using scientific notation where needed.

row_label: 2,3-Pentanedione / Km (mM) column


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

column_label: Table II reports substrate row 2,3-Heptanedione, Km (mM) = 2.6 x 10^-1; normalized Km = 0.26 mM.

normalized_value_unit_evidence: Km=0.26 mM; Table II reports values directly in mM using scientific notation where needed.

row_label: 2,3-Heptanedione / Km (mM) column


column_label: Table II reports substrate row Diacetyl, Km (mM) = 3.9 x 10^-1; normalized Km = 0.39 mM.

normalized_value_unit_evidence: Km=0.39 mM; Table II reports values directly in mM using scientific notation where needed.

row_label: Diacetyl / Km (mM) column


column_label: Table II reports substrate row 1,2-Cyclohexanedione, Km (mM) = 6.7 x 10^-1; normalized Km = 0.67 mM.

normalized_value_unit_evidence: Km=0.67 mM; Table II reports values directly in mM using scientific notation where needed.

row_label: 1,2-Cyclohexanedione / Km (mM) column


column_label: Table II reports substrate row (1S)-(+)-Camphorquinone, Km (mM) = 6.8 x 10^-1; normalized Km = 0.68 mM.

normalized_value_unit_evidence: Km=0.68 mM; Table II reports values directly in mM using scientific notation where needed.

row_label: (1S)-(+)-Camphorquinone / Km (mM) column


substrate_name: isatin

column_label: Table II reports substrate row Isatin, Km (mM) = 7.2 x 10^-1; normalized Km = 0.72 mM.

normalized_value_unit_evidence: Km=0.72 mM; Table II reports values directly in mM using scientific notation where needed.

row_label: Isatin / Km (mM) column

substrate: isatin


substrate_name: Methyl pyruvate

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

column_label: Table II reports substrate row Methyl pyruvate, Km (mM) = 1.1; normalized Km = 1.1 mM.

normalized_value_unit_evidence: Km=1.1 mM; Table II reports values directly in mM using scientific notation where needed.

row_label: Methyl pyruvate / Km (mM) column

substrate: Methyl pyruvate


organism: Bacteroides fragilis (strain ATCC 25285 / DSM 2151 / CCUG 4856 / JCM 11019 / LMG 10263 / NCTC 9343 / Onslow / VPI 2553 / EN-2)

substrate_name: cholate (at pH 8.5)

proof_lines: optimal activities at pH 8.5 (NAD reduction)

proof_lines: chenodeoxycholic acid and its conjugates

substrate: cholate (at pH 8.5)


substrate_name: chenodeoxycholate (at pH 8.5)

substrate: chenodeoxycholate (at pH 8.5)


substrate_name: glycocholate (at pH 8.5)

substrate: glycocholate (at pH 8.5)


substrate_name: glycochenodeoxycholate (at pH 8.5)

substrate: glycochenodeoxycholate (at pH 8.5)


substrate_name: taurocholate (at pH 8.5)

substrate: taurocholate (at pH 8.5)


substrate_name: taurochenodeoxycholate (at pH 8.5)

substrate: taurochenodeoxycholate (at pH 8.5)


substrate_name: 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate (at pH 6.5)


substrate_name: NADH (in the presence of 3alpha,12alpha-dihydroxy-7-oxo-5beta-cholanate, at pH 8.5)

assay_conditions_summary: pH 8.5; cofactor NADH


enzyme_display_name: UniProt A0A0J9X283

organism: Staphylococcus aureus

substrate_name: NADPH

enzyme: UniProt A0A0J9X283

substrate: NADPH


organism: Clostridium sardiniense

substrate_name: chenodeoxycholic acid

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature Q255L/C260S to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 298.15 K; cofactor NADP+

substrate: chenodeoxycholic acid


sequence_variant_note: Resolved sequence already matches the mutant residue(s), so it is treated as a source-provided variant sequence.


organism: Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv)

substrate_name: NAD (at pH 9.5 and at 30 degrees Celsius)

assay_conditions_summary: pH 9.5; cofactor NAD+

column_label: Table 1 reports NAD+ Km as 29.5 mM under the pH 9.5 forward-reaction condition.

raw_value_unit_evidence: Km = 29.5 mM for NAD+, standard error 2.78

row_label: NAD+


substrate_name: beta-hydroxybutyryl-CoA (at pH 9.5 and at 30 degrees Celsius)

assay_conditions_summary: pH 9.5; cofactor CoA

column_label: Table 1 reports beta-Hydroxybutyryl-CoA Km as 43.5 mM under the pH 9.5 forward-reaction condition.

raw_value_unit_evidence: Km = 43.5 mM for beta-Hydroxybutyryl-CoA, standard error 5.82

row_label: beta-Hydroxybutyryl-CoA


substrate_name: NADH (at pH 9.5 and at 30 degrees Celsius)


substrate_name: acetoacetyl-CoA (at pH 9.5 and at 30 degrees Celsius)


assay_conditions_summary: cofactor NADPH

column_label: PMID 7358641 / DOI 10.1093/oxfordjournals.jbchem.a132751, abstract prose, D-erythrulose reductase from chicken liver, NADPH Km = 7.9 uM.

raw_value_unit_evidence: Primary abstract reports Km values for NADH and NADPH of 67 uM and 7.9 uM, respectively; PubMed/Europe PMC render the microM symbol as 'micrometers'.

row_label: D-erythrulose reductase / NADPH

table_label: PubMed/Europe PMC abstract prose


substrate_name: NADH

column_label: PMID 7358641 / DOI 10.1093/oxfordjournals.jbchem.a132751, abstract prose, D-erythrulose reductase from chicken liver, NADH Km = 67 uM.

row_label: D-erythrulose reductase / NADH

substrate: NADH


organism: Saccharomyces cerevisiae


substrate_name: isatin


substrate_name: dl-camphorquinone

substrate: dl-camphorquinone


substrate_name: beta-naphthoquinone

substrate: beta-naphthoquinone


substrate_name: ninhydrin

substrate: ninhydrin


substrate_name: alloxan

substrate: alloxan


organism: Lactiplantibacillus plantarum

substrate_name: NAD+

proof_lines: with (+-)t-3,t-4-dihydroxycyclohexanecarboxylate and (-)-dihydroshikimate

substrate: NAD+


substrate_name: (-)-Dihydroshikimate

substrate: (-)-Dihydroshikimate


substrate_name: (-)-shikimate

substrate: (-)-shikimate


substrate_name: (-)-quinate

substrate: (-)-quinate


organism: Candida parapsilosis

substrate: isatin


substrate_name: ketopantoyl lactone

substrate: ketopantoyl lactone


organism: Spinacia oleracea


substrate_name: bornanedione

substrate: bornanedione


enzyme_display_name: hexadecanol dehydrogenase

organism: Acinetobacter sp.

substrate_name: hexadecanol

smiles: CCCCCCCCCCCCCCCCO

proof_lines: in crude extract of hexadecane-induced cells

proof_lines: in crude extract of hexadecanol-induced cells

enzyme: hexadecanol dehydrogenase

substrate: hexadecanol


enzyme_display_name: 2-alkyn-1-ol dehydrogenase

organism: Fusarium merismoides

smiles: C(C#CCO)O

enzyme: 2-alkyn-1-ol dehydrogenase


organism: Bacteroides fragilis

substrate_name: chenodeoxycholic acid


substrate_name: cholic acid

substrate: cholic acid


organism: Lactobacillus plantarum

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


organism: Candida orthopsilosis


substrate_name: NADPH

proof_lines:
enzyme form B
enzyme form A


organism: Candida dubliniensis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature H128A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T30A to reconstruct the assayed variant sequence.


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


enzyme_display_name: 2-dehydropantoate 2-reductase

organism: Escherichia coli

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature N98A with inferred residue-numbering offset +10 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.6; 298.15 K; cofactor NADPH

proof_lines: NADPH-dependent reduction of ketopantoate to pantoate

proof_lines: steady-state kinetics of active site mutants R31A, K72A, N98A

enzyme: 2-dehydropantoate 2-reductase