column_label: Table 2: Kinetic Parameters for the C-Terminal Arginine Mutants of R-HPCDH with Respect to 2-KPC and 2-Butanone Reduction (Biochemistry 2004, volume 43, number 21, pages 6763-6771); printed column heads enzyme | Vmax (units per mg) | Km (mM) | kcat (s^-1) | kcat/Km (M^-1 s^-1) under each of the two ketone-substrate spans 2-KPC and 2-butanone. Cited cell set: Table 2, 2-KPC span, enzyme row WT; column Vmax (units per mg) = 51.9; column Km (mM) = 0.092; column kcat (s^-1) = 24.5; column kcat/Km (M^-1 s^-1) = 2.7 x 10^5. captured primary segment: Table 2 row WT | ketone substrate 2-KPC | Vmax 51.9 units per mg | Km 0.092 mM | kcat 24.5 s^-1 | kcat/Km 2.7 x 10^5 M^-1 s^-1

normalized_value_unit_evidence: Km: printed Table 2 cell 0.092 mM; the printed column head is already mM, so no unit conversion applies and the paper value is 0.092 mM. kcat: printed Table 2 cell 24.5 s^-1; the printed column head is already s^-1, so no unit conversion applies and the paper value is 24.5 s^(-1). kcat/Km: printed Table 2 cell 2.7 x 10^5 M^-1 s^-1, that is 270000.0 M^-1 s^-1; 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 270000.0 / 1000 = 270.0 s^-1 mM^-1. Quotient disclosure for this row: 24.5 / 0.092 = 266.30434782608694 s^-1 mM^-1, which is the value the catalog carries; in the printed unit that is 266304.3478260869 M^-1 s^-1, and the printed cell 2.7 x 10^5 M^-1 s^-1 renders it at the precision the table prints.

raw_value_unit_evidence: Table 2, 2-KPC span, enzyme row WT: Km = 0.092 mM; kcat = 24.5 s^-1; printed kcat/Km = 2.7 x 10^5 M^-1 s^-1.

row_label: Table 2, 2-KPC span, enzyme row WT


enzyme_display_name: 2-(R)-hydroxypropyl-CoM dehydrogenase

organism: Xanthobacter autotrophicus

source_db: brenda

verification_status: unverified

km_display: Not reported

ki_display: Not reported

kcat_over_km_display: Not reported

protein_accession_database: UniProt

source_license: CC BY 4.0

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R203A to reconstruct the assayed variant sequence.

mutation_type: substitution

data_origin: experimental

enzyme: 2-(R)-hydroxypropyl-CoM dehydrogenase

status: unverified

source: brenda


organism: Xanthobacter autotrophicus (strain ATCC BAA-1158 / Py2)

source_db: uniprot

kcat_display: Not reported

mutation_signature: Unknown

km_unit: mM

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

proof_lines: kcat is 25.8 sec(-1) for R-HPC oxidation (at pH 7.5). kcat is 24.5 sec(-1) for 2-KPC reduction (at pH 7.5) (PubMed:11851420). kcat is 26.8 sec(-1) with R-HPC as substrate. kcat is 0.044 sec(-1) with S-HPC as substrate. kcat is 2.9 sec(-1) w

source: uniprot


substrate_name: NADH (at pH 7.5)

assay_conditions_summary: pH 7.5; cofactor NADH

substrate: NADH (at pH 7.5)


enzyme_display_name: NADPH-dependent 3-keto-steroid reductase Hsd3b5

organism: Rattus norvegicus

substrate_name: dihydrotestosterone (in the presence of NADPH)

assay_conditions_summary: cofactor NADPH

proof_lines: Catalytic efficiency for dihydrotestosterone reduction is 20-fold better in the presence of NADPH than in the presence of NADH.


enzyme_display_name: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1

proof_lines: Vmax for dihydrotestosterone reduction is 15-fold higher in the presence of NADH than in the presence of NADPH.

substrate: dihydrotestosterone (in the presence of NADPH)


enzyme_display_name: D-specific alpha-keto acid dehydrogenase

organism: Enterococcus faecium

substrate_name: pyruvate (in the presence of NADPH at pH 5.6)

verification_status: verified

assay_conditions_summary: pH 5.6; buffer 50 mM sodium phosphate; cofactor NADPH

column_label: Table II row pyruvate; VanH column Km (mM).

raw_value_unit_evidence: Table II VanH row pyruvate: Km 1.45 mM.

row_label: pyruvate

table_label: Table II, Kinetic Data for VanH and D-Lactate Dehydrogenases

status: verified


substrate_name: alpha-ketobutyrate (in the presence of NADPH at pH 5.6)

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

column_label: Table II row alpha-ketobutyrate; VanH column Km (mM).

normalized_value_unit_evidence: Km 2.6 mM.

raw_value_unit_evidence: Table II VanH row alpha-ketobutyrate: Km 2.6 mM.

row_label: alpha-ketobutyrate

enzyme: D-specific alpha-keto acid dehydrogenase


substrate_name: alpha-ketovalerate (in the presence of NADPH at pH 5.6)

column_label: Table II row alpha-ketovalerate; VanH column Km (mM).

normalized_value_unit_evidence: Km 40 mM.

raw_value_unit_evidence: Table II VanH row alpha-ketovalerate: Km 40 mM.

row_label: alpha-ketovalerate


substrate_name: alpha-ketocaproate (in the presence of NADPH at pH 5.6)

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

column_label: Table II row alpha-ketocaproate; VanH column Km (mM).

normalized_value_unit_evidence: Km 20 mM.

raw_value_unit_evidence: Table II VanH row alpha-ketocaproate: Km 20 mM.

row_label: alpha-ketocaproate


substrate_name: alpha-ketoisocaproate (in the presence of NADPH at pH 5.6)

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

column_label: Table II row alpha-ketoisocaproate; VanH column Km (mM).

normalized_value_unit_evidence: Km 31 mM.

raw_value_unit_evidence: Table II VanH row alpha-ketoisocaproate: Km 31 mM.

row_label: alpha-ketoisocaproate


substrate_name: NADPH (at pH 5.6)

assay_conditions_summary: pH 5.6; cofactor NADPH

proof_lines: kcat is 40 sec(-1) with pyruvate as substrate (in the presence of NADPH at pH 5.6) (PubMed:1931965). kcat is 10.7 sec(-1) with pyruvate as substrate (in the presence of NADPH at pH 5.6) (PubMed:9605319). kcat is 35 sec(-1) with alpha-ketobu

substrate: NADPH (at pH 5.6)


substrate_name: NADH (at pH 5.6)

assay_conditions_summary: pH 5.6; cofactor NADH

column_label: Table II VanH cofactor row Km (NADH) (uM).

normalized_value_unit_evidence: Km 0.021 mM after converting 21 uM to mM.

raw_value_unit_evidence: Table II row Km (NADH): 21 uM.

row_label: Km (NADH)

substrate: NADH (at pH 5.6)


enzyme_display_name: Aldo-keto reductase family 1 member C1

organism: Homo sapiens

substrate_name: (s)-tetralol

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

enzyme: Aldo-keto reductase family 1 member C1

substrate: (s)-tetralol


enzyme_display_name: 2-(S)-hydroxypropyl-CoM dehydrogenase 3

smiles: CCC(=O)C

proof_lines: kcat is 5.5 sec(-1) with R-HPC as substrate. kcat is 25 sec(-1) with S-HPC as substrate. kcat is 11 sec(-1) with 2-KPC as substrate. kcat is 0.044 sec(-1) with 2-butanone as substrate. kcat is 2.0 sec(-1) with 2-propanol as substrate. kcat

enzyme: 2-(S)-hydroxypropyl-CoM dehydrogenase 3


smiles: CC(C)O


smiles: CCC(C)O


substrate_name: NAD(+)

substrate: NAD(+)


substrate_name: NADH

assay_conditions_summary: cofactor NADH

substrate: NADH


enzyme_display_name: 3beta-hydroxysteroid 3-dehydrogenase

organism: Oryctolagus cuniculus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M304S with inferred residue-numbering offset -2 to reconstruct the assayed variant sequence.

enzyme: 3beta-hydroxysteroid 3-dehydrogenase


substrate_name: methylglyoxal

smiles: CC(=O)C=O

substrate: methylglyoxal


substrate_name: progesterone (reduction)

verification_status: corrected

assay_conditions_summary: pH 7; cofactor NADPH

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

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

row_label: Progesterone reduction / AKR1C1

substrate: progesterone (reduction)

status: corrected


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

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


assay_conditions_summary: pH 7; cofactor NADP+

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

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


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

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

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


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)


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

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


kcat_over_km_origin: calculated

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

sequence_source: multiple

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

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

source_databases_merged: brenda skid


enzyme_display_name: 2-(S)-hydroxypropyl-CoM dehydrogenase

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

enzyme: 2-(S)-hydroxypropyl-CoM dehydrogenase


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


organism: Corynebacterium sp.

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K232G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R238H with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K232S to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K232M to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K232Q to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature R235G could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R238E with inferred residue-numbering offset +2 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved sequence already matches the mutant residue(s) after applying an inferred residue-numbering offset -7, so it is treated as a source-provided variant sequence.


proof_lines:
isoenzyme I
isoenzyme II


substrate_name: NADPH

substrate: NADPH


organism: Xanthobacter sp.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature F22Y with inferred residue-numbering offset -7 to reconstruct the assayed variant sequence.


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

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

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

row_label: DhtS; enzyme AKR1C1

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


enzyme_display_name: Dehydrogenase/reductase SDR family member 11

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

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

normalized_value_unit_evidence: Km=0.0052 mM converted from 5.2 uM

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

table_label: Table 1


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

column_label: Table 1; row 3,17-Diketosteroids / 4-Androstene-3,17-dione; Km column

normalized_value_unit_evidence: Km=0.0046 mM converted from 4.6 uM

raw_value_unit_evidence: Table 1 3,17-Diketosteroids / 4-Androstene-3,17-dione Km 4.6 uM

enzyme: Dehydrogenase/reductase SDR family member 11


substrate_name: progesterone (at 37 degrees Celsius)

column_label: Table 1; row 3,20-Diketosteroids / Progesterone; Km column

normalized_value_unit_evidence: Km=0.0034 mM converted from 3.4 uM

raw_value_unit_evidence: Table 1 3,20-Diketosteroids / Progesterone Km 3.4 uM

row_label: 3,20-Diketosteroids / Progesterone

substrate: progesterone (at 37 degrees Celsius)


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

column_label: Table 1; row 3,20-Diketosteroids / 5beta-Pregnane-3,20-dione; Km column

normalized_value_unit_evidence: Km=0.015 mM converted from 15 uM

raw_value_unit_evidence: Table 1 3,20-Diketosteroids / 5beta-Pregnane-3,20-dione Km 15 uM


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

column_label: Table 2; row C18-steroid / 17beta-Estradiol; Km column

normalized_value_unit_evidence: Km=0.016 mM converted from 16 uM

raw_value_unit_evidence: Table 2 C18-steroid / 17beta-Estradiol Km 16 uM

row_label: C18-steroid / 17beta-Estradiol

table_label: Table 2


substrate_name: testosterone (at 37 degrees Celsius)

column_label: Table 2; row C19-steroids / Testosterone; Km column

normalized_value_unit_evidence: Km=0.03 mM converted from 30 uM

raw_value_unit_evidence: Table 2 C19-steroids / Testosterone Km 30 uM

row_label: C19-steroids / Testosterone

substrate: testosterone (at 37 degrees Celsius)


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


substrate_name: isolithocholic acid (at 37 degrees Celsius)

proof_lines:
DHRS11
bile acid isomerization
7beta-OH dehydrogenases


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


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

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


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

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

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

normalized_value_unit_evidence: Km=0.201 mM converted from 201 uM

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

table_label: Table 3


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

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

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

normalized_value_unit_evidence: Km=0.42 mM converted from 420 uM

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

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


substrate_name: alpha-tetralone (at 37 degrees Celsius)

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

normalized_value_unit_evidence: Km=0.178 mM converted from 178 uM

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

row_label: Alicyclic ketones / alpha-Tetralone

substrate: alpha-tetralone (at 37 degrees Celsius)


substrate_name: loxoprofen (at 37 degrees Celsius)

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

normalized_value_unit_evidence: Km=0.74 mM converted from 740 uM

raw_value_unit_evidence: Table 3 Alicyclic ketones / Loxoprofen Km 740 uM

row_label: Alicyclic ketones / Loxoprofen

substrate: loxoprofen (at 37 degrees Celsius)


source_db: oed

column_label: Table 1. Kinetic Parameters for R- and S-HPCDH with physiological substrates in the forward and reverse directions, Table 1 / rR-HPCDH1 / 2-KPC: Km=68 uM; kcat=29 s^-1; kcat/Km=4.2 x 10^5 M^-1 s^-1.

row_label: Table 1 / rR-HPCDH1 / 2-KPC

source: oed


column_label: Table 1. Kinetic Parameters for R- and S-HPCDH with physiological substrates in the forward and reverse directions, Table 1 / rR-HPCDH1 / R-HPC: Km=96 uM; kcat=48 s^-1; kcat/Km=5.0 x 10^5 M^-1 s^-1.

row_label: Table 1 / rR-HPCDH1 / R-HPC


column_label: Table 1. Kinetic Parameters for R- and S-HPCDH with physiological substrates in the forward and reverse directions, Table 1 / rR-HPCDH1 / S-HPC: Km=220 uM; kcat=0.12 s^-1; kcat/Km=5.3 x 10^2 M^-1 s^-1.

row_label: Table 1 / rR-HPCDH1 / S-HPC


column_label: Table 5. Kinetic Parameters for rS-HPCDH3 and rR-HPCDH1 catalyzed oxidation of 2-butanol, Table 5 / rR-HPCDH1 / (R)-2-butanol: Km=220 mM; kcat=1.9 s^-1; kcat/Km=8.69 M^-1 s^-1.

row_label: Table 5 / rR-HPCDH1 / (R)-2-butanol


column_label: Table 5. Kinetic Parameters for rS-HPCDH3 and rR-HPCDH1 catalyzed oxidation of 2-butanol, Table 5 / rR-HPCDH1 / (S)-2-butanol: Km=350 mM; kcat=9.3 s^-1; kcat/Km=26.4 M^-1 s^-1.

row_label: Table 5 / rR-HPCDH1 / (S)-2-butanol


substrate_name: dehydroepiandrosterone

sequence_variant_note: Mutation signature S194G matches the mutant residue at offset +0 and the reference residue at offset +1; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.

substrate: dehydroepiandrosterone


substrate_name: NAD+

assay_conditions_summary: pH 7.4; 300.15 K; cofactor NAD+

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature K214A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature R211A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature S143A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

column_label: Table 2. Summary of Amino Acid Substitutions Made to the Putative rS-HPCDH3 Catalytic Residues Using Site-Directed Mutagenesis, Table 2 / S143A / S-HPC: Km=9500 uM; kcat=0.013 s^-1; kcat/Km=1.4 x 10^0 M^-1 s^-1.

row_label: Table 2 / S143A / S-HPC


sequence_variant_note: Mutation signature Y156A matches the mutant residue at offset +0 and the reference residue at offset -6; variant reconstruction was not applied because multiple plausible residue-numbering offsets are present.


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

column_label: Table 5. Kinetic Parameters for rS-HPCDH3 and rR-HPCDH1 catalyzed oxidation of 2-butanol, Table 5 / rS-HPCDH3 / (R)-2-butanol: Km=68 mM; kcat=1.0 s^-1; kcat/Km=14.8 M^-1 s^-1.

row_label: Table 5 / rS-HPCDH3 / (R)-2-butanol


column_label: Table 5. Kinetic Parameters for rS-HPCDH3 and rR-HPCDH1 catalyzed oxidation of 2-butanol, Table 5 / rS-HPCDH3 / (S)-2-butanol: Km=28 mM; kcat=2.6 s^-1; kcat/Km=92.8 M^-1 s^-1.

row_label: Table 5 / rS-HPCDH3 / (S)-2-butanol


smiles: CCC(C)=O


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q56841 and applied mutation signature K214A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; buffer 50 mM glycine; cofactor NAD+

column_label: Table 3 (Kinetic Parameters for wild-type rS-HPCDH3 and its alanine variants), block 'Substrate: 2-KPC', enzyme row 'K214A'; column 'Km (mM)' = 12 ± 0. 9; column 'kcat (s-1)' = 9.6 ± 0.3; column 'kcat/Km (M-1 s-1)' = 8.1 x 10^2; column 'Change in Km (x-fold)' and column 'Change in kcat (x-fold)' print unitless ratios to the wild-type row.

normalized_value_unit_evidence: Km: printed Table 3 cell 12 under the column head Km (mM); millimolar is already the canonical unit, so no unit conversion applies and the value is 12.0 mM. kcat: printed Table 3 cell 9.6 under the column head kcat (s-1); per-second is already the canonical unit, so no unit conversion applies and the value is 9.6 s^(-1). kcat/Km: printed Table 3 cell 8.1 x 10^2 under the column head kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 8.1 x 10^2 / 1000 = 0.81 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, block 'Substrate: 2-KPC', enzyme row 'K214A': the column headed Km (mM) prints 12 ± 0. 9; the column headed kcat (s-1) prints 9.6 ± 0.3; the column headed kcat/Km (M-1 s-1) prints 8.1 x 10^2.


sequence_variant_note: Resolved canonical sequence from uniprot_rest_accession:Q56841 and applied mutation signature R211A with inferred residue-numbering offset -6 to reconstruct the assayed variant sequence.

column_label: Table 3 (Kinetic Parameters for wild-type rS-HPCDH3 and its alanine variants), block 'Substrate: 2-KPC', enzyme row 'R211A'; column 'Km (mM)' = 11 ± 0.4; column 'kcat (s-1)' = 8.6 ± 0.2; column 'kcat/Km (M-1 s-1)' = 7.5 x 10^2; column 'Change in Km (x-fold)' and column 'Change in kcat (x-fold)' print unitless ratios to the wild-type row.

normalized_value_unit_evidence: Km: printed Table 3 cell 11 under the column head Km (mM); millimolar is already the canonical unit, so no unit conversion applies and the value is 11.0 mM. kcat: printed Table 3 cell 8.6 under the column head kcat (s-1); per-second is already the canonical unit, so no unit conversion applies and the value is 8.6 s^(-1). kcat/Km: printed Table 3 cell 7.5 x 10^2 under the column head kcat/Km (M-1 s-1); 1 M^-1 s^-1 is 0.001 s^-1 mM^-1, so 7.5 x 10^2 / 1000 = 0.75 s^-1 mM^-1.

raw_value_unit_evidence: Table 3, block 'Substrate: 2-KPC', enzyme row 'R211A': the column headed Km (mM) prints 11 ± 0.4; the column headed kcat (s-1) prints 8.6 ± 0.2; the column headed kcat/Km (M-1 s-1) prints 7.5 x 10^2.


proof_lines: kcat is 28 sec(-1) with S-HPC as substrate. kcat is 20 sec(-1) with 2-KPC as substrate. kcat is 2.4 sec(-1) with R-HPC as substrate.


substrate_name: NADPH


substrate_name: estrone (at 37 degrees Celsius)

proof_lines:
DHRS11
sex steroids
17beta-OH activities

substrate: estrone (at 37 degrees Celsius)


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

column_label: Table 1; row 17-Ketosteroids / 5alpha-Androstan-3alpha-ol-17-one; Km column

normalized_value_unit_evidence: Km=0.0013 mM converted from 1.3 uM

raw_value_unit_evidence: Table 1 17-Ketosteroids / 5alpha-Androstan-3alpha-ol-17-one Km 1.3 uM


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

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

normalized_value_unit_evidence: Km=0.011 mM converted from 11 uM

raw_value_unit_evidence: Table 1 17-Ketosteroids / DHEA Km 11 uM

row_label: 17-Ketosteroids / DHEA


substrate_name: DHEA sulfate (at 37 degrees Celsius)

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

normalized_value_unit_evidence: Km=0.012 mM converted from 12 uM

raw_value_unit_evidence: Table 1 17-Ketosteroids / DHEA sulfate Km 12 uM

row_label: 17-Ketosteroids / DHEA sulfate

substrate: DHEA sulfate (at 37 degrees Celsius)


substrate_name: dehydrolithocholic acid (at 37 degrees Celsius)

column_label: Table 1; row 3-Ketosteroids / Dehydrolithocholic acid; Km column

normalized_value_unit_evidence: Km=0.0011 mM converted from 1.1 uM

raw_value_unit_evidence: Table 1 3-Ketosteroids / Dehydrolithocholic acid Km 1.1 uM


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

column_label: Table 1; row 3-Ketosteroids / 20alpha-Hydroxyprogesterone; Km column

normalized_value_unit_evidence: Km=0.0051 mM converted from 5.1 uM

raw_value_unit_evidence: Table 1 3-Ketosteroids / 20alpha-Hydroxyprogesterone Km 5.1 uM


substrate_name: taurodehydrocholic acid (at 37 degrees Celsius)

column_label: Table 1; row 3-Ketosteroids / Taurodehydrocholic acid; Km column

normalized_value_unit_evidence: Km=0.044 mM converted from 44 uM

raw_value_unit_evidence: Table 1 3-Ketosteroids / Taurodehydrocholic acid Km 44 uM


substrate_name: dehydrocholic acid (at 37 degrees Celsius)


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


organism: Yersinia pestis

assay_conditions_summary: pH 7.8; 310.15 K; cofactor NADPH

proof_lines:
pH 7.8, 37°C
Raw SKiD Env: Temp=37°C, pH=7.8


substrate_name: 1-deoxy-D-xylulose 5-phosphate

column_label: Table 1; row label Y. pestis; column label Kcat DXP/Km DXP (M^-1 min^-1); raw value 4.6 x 10^5; raw unit M^-1 min^-1; normalized value kcat/Km=7.66667 s^-1*mM^-1; assay condition DXP varied. Table 1 also labels Km DXP (uM) and Kcat DXP (s^-1).

normalized_value_unit_evidence: Km normalized_value=0.2215 normalized_unit=mM; kcat normalized_value=1.7 normalized_unit=s^-1; kcat/Km=7.66667 s^-1*mM^-1 from explicit Kcat DXP/Km DXP table value conversion.

raw_value_unit_evidence: Table 1 row Y. pestis reports Km DXP=221.5 +/- 34.3 uM, Kcat DXP=1.7 s^-1, and Kcat DXP/Km DXP=4.6 x 10^5 M^-1 min^-1.

row_label: Y. pestis

table_label: Table 1, MEP synthase Apparent Kinetic Parameters

substrate: 1-deoxy-D-xylulose 5-phosphate


substrate_name: glycerol

smiles: C(C(CO)O)O

substrate: glycerol


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


substrate_name: dihydroxyacetone

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

substrate: dihydroxyacetone


enzyme_display_name: GDP-L-fucose synthase

organism: Escherichia coli (strain K12)

enzyme: GDP-L-fucose synthase


substrate_name: NADH

substrate: NADH


organism: Bacillus subtilis (strain 168)

substrate_name: DHAP

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

assay_conditions_summary: pH 8.2; cofactor NADH

column_label: Table 1, substrate row DHAP, KM (uM) column; condition footnote a.

row_label: DHAP

substrate: DHAP


column_label: Table 1, substrate row NADH, KM (uM) column; condition footnote a.

row_label: NADH


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

column_label: Table 1, substrate row G1P, KM (uM) column; condition footnote a.


substrate_name: NAD(+)

assay_conditions_summary: pH 8.2; cofactor NAD+

column_label: Table 1, substrate row NAD+, KM (uM) column; condition footnote a.

row_label: NAD+

substrate: NAD(+)


enzyme_display_name: 1,5-anhydro-D-fructose reductase

substrate_name: NADPH (at 25 degrees Celsius)

enzyme: 1,5-anhydro-D-fructose reductase

substrate: NADPH (at 25 degrees Celsius)


substrate_name: NADH (at 25 degrees Celsius)

substrate: NADH (at 25 degrees Celsius)


enzyme_display_name: sn-glycerol-1-phosphate dehydrogenase

organism: Bacillus subtilis

substrate_name: NAD+

assay_conditions_summary: pH 8.2; 318.15 K; cofactor NAD+

column_label: Literal AraM Table 1 NAD+ row under the reverse reaction with saturating 10 mM G1P; exact Km, kcat, and printed kcat/Km cells are bound to the same row and footnote-a assay condition.

normalized_value_unit_evidence: Source-row storage precision: kcat=0.008 s^-1; Km=0.059 mM; deterministic same-row quotient=0.13559322033898305 s^-1 mM^-1. Direct literal conversions are kcat=0.007666666666666667 s^-1 and Km=0.0593 mM; independently printed efficiency converts to 0.13 s^-1 mM^-1 and is not substituted for the component quotient.

table_label: Table 1. Steady-State Kinetic Constants of the G1PDH Activity of AraM

enzyme: sn-glycerol-1-phosphate dehydrogenase


assay_conditions_summary: pH 8.2; 318.15 K; cofactor NADH

column_label: Literal AraM Table 1 NADH row under the forward reaction with saturating 0.1 mM DHAP; exact Km, kcat, and printed kcat/Km cells are bound to the same row and footnote-a assay condition.

normalized_value_unit_evidence: Source-row storage precision: kcat=0.222 s^-1; Km=0.016 mM; deterministic same-row quotient=13.875 s^-1 mM^-1. Direct literal conversions are kcat=0.22166666666666668 s^-1 and Km=0.016 mM; independently printed efficiency converts to 13.833333333333334 s^-1 mM^-1 and is not substituted for the component quotient.


substrate_name: sn-Glycerol 1-phosphate

column_label: Literal AraM Table 1 G1P row under the reverse reaction with saturating 4 mM NAD+; exact Km, kcat, and printed kcat/Km cells are bound to the same row and footnote-a assay condition.

normalized_value_unit_evidence: Source-row storage precision: kcat=0.008 s^-1; Km=1.37 mM; deterministic same-row quotient=0.00583941605839416 s^-1 mM^-1. Direct literal conversions are kcat=0.008333333333333333 s^-1 and Km=1.37 mM; independently printed efficiency converts to 0.006 s^-1 mM^-1 and is not substituted for the component quotient.

substrate: sn-Glycerol 1-phosphate


substrate_name: glycerone phosphate

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

substrate: glycerone phosphate


substrate_name: 9,10-phenanthrenequinone with NADPH as cofactor


organism: Thermotoga maritima

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 358.15 K; cofactor NADPH

substrate: NADPH


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


organism: Zymomonas mobilis subsp. mobilis (strain ATCC 31821 / ZM4 / CP4)

assay_conditions_summary: pH 8; cofactor NADPH

column_label: Section 3 Results and discussion prose gives the DXP reductoisomerase Km value as 0.3 mM.

raw_value_unit_evidence: Km raw_value=0.3 raw_unit=mM

row_label: DXP reductoisomerase substrate DXP

table_label: Section 3 Results and discussion prose


column_label: Section 3 Results and discussion prose states NADPH is the cofactor with Km of 5 uM.

raw_value_unit_evidence: Km raw_value=5 raw_unit=uM

row_label: DXP reductoisomerase cofactor NADPH


organism: Sus scrofa

column_label: Abstract states the purified enzyme showed a Km value of 0.44 mM for AF at the optimum pH of 7.0.

raw_value_unit_evidence: Km raw_value=0.44 raw_unit=mM

row_label: porcine liver NADPH-dependent reductase with 1,5-anhydro-D-fructose

table_label: PubMed abstract PMID 9504428


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

organism: Mus musculus

substrate_name: estrone

substrate: estrone


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


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

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

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


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

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

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

row_label: DHT -> 3betaA-diol


organism: Escherichia coli


substrate_name: 1,2-Dideoxy-D-hexulose 6-phosphate

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

proof_lines:
Et-DXP
poor substrate

substrate: 1,2-Dideoxy-D-hexulose 6-phosphate


organism: Mycobacterium tuberculosis

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W203F to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature W203Y to reconstruct the assayed variant sequence.


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


substrate_name: dihydrotestosterone

column_label: Abstract reports expressed 3 beta HSD V has an apparent Km value for DHT of 0.47 microM.

raw_value_unit_evidence: Km raw_value=0.47 microM raw_unit=microM

row_label: Mouse expressed 3 beta HSD V / DHT

table_label: PubMed XML abstract PMID 7491113

enzyme: NADPH-dependent 3-keto-steroid reductase Hsd3b5

substrate: dihydrotestosterone


enzyme_display_name: NADPH-dependent 3-keto-steroid reductase Hsd3b4

assay_conditions_summary: cofactor NADPH

column_label: PMID 7491113 abstract reports expressed 3 beta HSD V has lower DHT Km than 3 beta HSD IV: 0.47 microM vs 2.2 microM respectively; PMID 8145763 establishes 3 beta HSD IV converts DHT to 5 alpha-androstanediol with NADPH.

raw_value_unit_evidence: Km raw_value=2.2 raw_unit=microM for DHT

row_label: mouse 3 beta HSD IV / Hsd3b4 converting dihydrotestosterone to 5 alpha-androstanediol

table_label: PubMed abstract PMID 7491113 with lead context PMID 8145763


substrate_name: 1-Fluoro-1-deoxy-D-xylulose 5-phosphate

substrate: 1-Fluoro-1-deoxy-D-xylulose 5-phosphate


organism: Taiwanofungus camphoratus

substrate_name: S-nitrosoglutathione

substrate: S-nitrosoglutathione


substrate_name: S-(hydroxymethyl)glutathione

substrate: S-(hydroxymethyl)glutathione


enzyme_display_name: UniProt P11766

source_db: skid

source_license: CC BY-NC-ND 4.0

enzyme: UniProt P11766

source: skid


enzyme_display_name: UniProt Q5JFV8

organism: Thermococcus kodakarensis

substrate_name: homoisocitrate

enzyme: UniProt Q5JFV8

substrate: homoisocitrate


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


substrate_name: isocitrate

substrate: isocitrate


enzyme_display_name: UniProt Q72IW9

organism: Thermus thermophilus

enzyme: UniProt Q72IW9


substrate: NAD+


organism: Homo sapiens

substrate_name: dihydrotestosterone (in the presence of NADH)

proof_lines:
3 beta-hydroxysteroid dehydrogenase
dihydrotestosterone
Homo sapiens

enzyme: 3 beta-hydroxysteroid dehydrogenase/Delta 5-->4-isomerase type 1


enzyme_display_name: xanthoxin dehydrogenase

organism: Arabidopsis thaliana

substrate_name: xanthoxin

proof_lines: no activity with xanthoxic acid, ethanol, isopropanol, butanol, cyclohexanol and 2,6-dimethylcyclohexanol.

source_databases_merged: brenda uniprot

enzyme: xanthoxin dehydrogenase

substrate: xanthoxin


enzyme_display_name: sorbose reductase

organism: Candida albicans

substrate_name: D-fructose

proof_lines:
pH 7.5, 25°C, positive cooperativity
pH 7.5, 25°C, Michaelis-Menten kinetics
K0.5-value, positive cooperativity

enzyme: sorbose reductase

substrate: D-fructose


enzyme_display_name: 2-(R)-hydroxypropyl-CoM dehydrogenase

organism: Xanthobacter sp.

proof_lines:
pH 7.5, 30 C
Raw SKiD Env: Temp=30 C, pH=7.5

enzyme: 2-(R)-hydroxypropyl-CoM dehydrogenase


enzyme_display_name: momilactone-A synthase

organism: Oryza sativa

substrate_name: oryzalexin A

assay_conditions_summary: pH 8

enzyme: momilactone-A synthase

substrate: oryzalexin A


assay_conditions_summary: pH 8; cofactor NAD+


organism: Gluconobacter oxydans

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

assay_conditions_summary: pH 6; 298.15 K; cofactor NADPH


substrate_name: D-mannitol

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

assay_conditions_summary: pH 10; 298.15 K; cofactor NADPH

substrate: D-mannitol


substrate_name: L-sorbose

substrate: L-sorbose


organism: Ensifer adhaerens

sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A13G to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from uniprot_accession and applied mutation signature A13G/S10G with inferred residue-numbering offset +23 to reconstruct the assayed variant sequence.


sequence_variant_note: Mutation signature A13G/S33D could not be applied safely because the resolved sequence does not match the expected reference residue(s).


sequence_variant_note: Resolved canonical sequence from accession_anchored:Q2I8V6/DQ140417.1/ABA25865.1 and applied mutation signature D176A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7.5; 303.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from accession_anchored:Q2I8V6/DQ140417.1/ABA25865.1 and applied mutation signature G206I to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from accession_anchored:Q2I8V6/DQ140417.1/ABA25865.1 and applied mutation signature H180A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 303.15 K; cofactor NADPH


sequence_variant_note: Resolved canonical sequence from accession_anchored:Q2I8V6/DQ140417.1/ABA25865.1 and applied mutation signature K94G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from accession_anchored:Q2I8V6/DQ140417.1/ABA25865.1 and applied mutation signature S10G to reconstruct the assayed variant sequence.


organism: Eubacterium barkeri

assay_conditions_summary: cofactor NADH


organism: Bacillus cereus

proof_lines:
pH 8.5, 37°C
pH 8.5, 37°C, recombinant enzyme


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


substrate_name: NADP+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NADP+

substrate: NADP+


substrate_name: NAD+

assay_conditions_summary: pH 8.5; 310.15 K; cofactor NAD+


organism: Unknown

substrate_name: Unknown

source_db: unknown

source_license: see source

sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5JFV8 and applied mutation signature T71V to reconstruct the assayed variant sequence.

substrate: Unknown

source: unknown


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5JFV8 and applied mutation signature S80A to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5JFV8 and applied mutation signature I82N to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5JFV8 and applied mutation signature L81P 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.


sequence_variant_note: Resolved canonical sequence from UniProtKB:Q5JFV8 and applied mutation signature L83R to reconstruct the assayed variant sequence.


enzyme_display_name: diacetyl reductase [(R)-acetoin forming]

organism: Shouchella clausii

substrate_name: diacetyl

ki_unit: mM

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

substrate: diacetyl


organism: Metallosphaera sedula

substrate_name: malonate semialdehyde

substrate: malonate semialdehyde


substrate_name: NADPH

assay_conditions_summary: pH 7.4; 338.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: NADP-retinol dehydrogenase

protein_accession_database: NCBI Protein

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

assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 2. Kinetic parameters for cofactors of BcALDH in oxidation and reduction reactions using all-trans-retinal as a cosubstrate; row NADPH reduction; Km column raw 40 +/- 1.0 uM; kcat column raw 0.033 +/- 0.00 min^-1; kcat/Km column raw 0.83 +/- 0.05 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.04 normalized_unit=mM; kcat normalized_value=0.00055 normalized_unit=s^-1; kcat/Km normalized_value=0.01375 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=40 +/- 1.0 raw_unit=uM; kcat raw_value=0.033 +/- 0.00 raw_unit=min^-1; kcat/Km raw_value=0.83 +/- 0.05 raw_unit=mM^-1 min^-1

row_label: NADPH reduction

enzyme: NADP-retinol dehydrogenase


assay_conditions_summary: pH 7; cofactor NAD+

column_label: Table 2. Kinetic parameters for cofactors of BcALDH in oxidation and reduction reactions using all-trans-retinal as a cosubstrate; row NAD+ oxidation; Km column raw 4.0 +/- 0.2 uM; kcat column raw 0.10 +/- 0.01 min^-1; kcat/Km column raw 25 +/- 0.1 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.004 normalized_unit=mM; kcat normalized_value=0.0017 normalized_unit=s^-1; kcat/Km normalized_value=0.425 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=4.0 +/- 0.2 raw_unit=uM; kcat raw_value=0.10 +/- 0.01 raw_unit=min^-1; kcat/Km raw_value=25 +/- 0.1 raw_unit=mM^-1 min^-1

row_label: NAD+ oxidation


assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 2. Kinetic parameters for cofactors of BcALDH in oxidation and reduction reactions using all-trans-retinal as a cosubstrate; row NADP+ oxidation; Km column raw 4.2 +/- 0.3 uM; kcat column raw 0.11 +/- 0.02 min^-1; kcat/Km column raw 26 +/- 0.2 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.0042 normalized_unit=mM; kcat normalized_value=0.0018 normalized_unit=s^-1; kcat/Km normalized_value=0.4285714285714286 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=4.2 +/- 0.3 raw_unit=uM; kcat raw_value=0.11 +/- 0.02 raw_unit=min^-1; kcat/Km raw_value=26 +/- 0.2 raw_unit=mM^-1 min^-1

row_label: NADP+ oxidation


substrate_name: retinal

column_label: Table 1. Kinetic parameters for aldehyde substrates of BcALDH in oxidation activity using NAD+ as a cosubstrate; row all-trans-retinal -> all-trans-retinoic acid; Km column raw 7 +/- 0.1 uM; kcat column raw 0.28 +/- 0.03 min^-1; kcat/Km column raw 40 +/- 0.2 mM^-1 min^-1.

normalized_value_unit_evidence: Km normalized_value=0.007 normalized_unit=mM; kcat normalized_value=0.0047 normalized_unit=s^-1; kcat/Km normalized_value=0.6714285714285715 normalized_unit=s^-1*mM^-1

raw_value_unit_evidence: Km raw_value=7 +/- 0.1 raw_unit=uM; kcat raw_value=0.28 +/- 0.03 raw_unit=min^-1; kcat/Km raw_value=40 +/- 0.2 raw_unit=mM^-1 min^-1

substrate: retinal


enzyme_display_name: Aldo-keto reductase family 1 member B15

substrate_name: all-trans-retinal

assay_conditions_summary: cofactor CoA

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

enzyme: Aldo-keto reductase family 1 member B15

substrate: all-trans-retinal


substrate_name: D,L-glyceraldehyde

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

substrate: D,L-glyceraldehyde


substrate_name: hexanal

smiles: CCCCCC=O

substrate: hexanal


substrate_name: acrolein

smiles: C=CC=O

substrate: acrolein


smiles: CCCC=CC=O


smiles: CCCCCC(C=CC=O)O


smiles: CCCCCC=CC(=O)C


substrate_name: farnesal

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

substrate: farnesal


enzyme_display_name: Retinol dehydrogenase 12

proof_lines: kcat is 36 min(-1) for all-trans-retinal as substrate. kcat is 45 min(-1) for 11-cis-retinal as substrate. kcat is 14 min(-1) for 9-cis-retinal as substrate. kcat is 27 min(-1) for all-trans-retinol as substrate. kcat is 7 min(-1) for 11-ci

enzyme: Retinol dehydrogenase 12


substrate_name: NADH

substrate: NADH


substrate_name: nonanal

smiles: CCCCCCCCC=O

substrate: nonanal


smiles: CCCCCCC=CC=O


smiles: CCC=CCCCCC=O


enzyme_display_name: Dehydrogenase/reductase SDR family member 4

organism: Oryctolagus cuniculus

substrate_name: 16-Ketoestrone (at pH6)

assay_conditions_summary: pH 6

proof_lines: kcat is 2 min(-1) with 5beta-Pregnane-3,20-dione as substrate (at pH7.4).

substrate: 16-Ketoestrone (at pH6)


substrate_name: all-trans-Retinal (at pH7.4)

enzyme: Dehydrogenase/reductase SDR family member 4

substrate: all-trans-Retinal (at pH7.4)


substrate_name: Isatin (at pH6)

substrate: Isatin (at pH6)


substrate_name: Propiophenone (at pH6)

substrate: Propiophenone (at pH6)


substrate_name: Heptanophenone (at pH6)

substrate: Heptanophenone (at pH6)


substrate_name: Nonanophenone (at pH6)

substrate: Nonanophenone (at pH6)


substrate_name: 4-Hexanoylpyridine (at pH6)

substrate: 4-Hexanoylpyridine (at pH6)


substrate_name: Hexanophenone (at pH6)

substrate: Hexanophenone (at pH6)


substrate_name: Valerophenone (at pH6)

substrate: Valerophenone (at pH6)


substrate_name: n-Butyrophenone (at pH6)

substrate: n-Butyrophenone (at pH6)


substrate_name: 3-Benzoylpyridine (at pH6)

substrate: 3-Benzoylpyridine (at pH6)


substrate_name: 4-Benzoylpyridine (at pH6)

substrate: 4-Benzoylpyridine (at pH6)


substrate_name: 2,3-Hexanedione (at pH6)

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

substrate: 2,3-Hexanedione (at pH6)


substrate_name: 1-phenyl-1,2-propanedione (at pH6)

substrate: 1-phenyl-1,2-propanedione (at pH6)


substrate_name: Benzil (at pH6)

substrate: Benzil (at pH6)


substrate_name: Diacetyl (at pH6)

substrate: Diacetyl (at pH6)


substrate_name: Pyridine-4-aldehyde (at pH6)

substrate: Pyridine-4-aldehyde (at pH6)


substrate_name: 1-Phenylisatin (at pH6)

substrate: 1-Phenylisatin (at pH6)


substrate_name: 9,10-Phenanthrenequinone (at pH6)

substrate: 9,10-Phenanthrenequinone (at pH6)


substrate_name: Menadione (at pH6)

substrate: Menadione (at pH6)


substrate_name: S-(-)-1-Phenyl-1-butanol (at pH7.4)

substrate: S-(-)-1-Phenyl-1-butanol (at pH7.4)


substrate_name: all-trans-Retinol (at pH7.4)

substrate: all-trans-Retinol (at pH7.4)


enzyme_display_name: NADP-dependent 3-hydroxy acid dehydrogenase YdfG

organism: Escherichia coli (strain K12)

substrate_name: NADP(+) (at pH 9 and at 30 degrees Celsius)

assay_conditions_summary: pH 9

proof_lines: The highest catalytic efficiency was observed with L-allo-threonine.


substrate_name: L-serine (at pH 9 and at 30 degrees Celsius)

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

enzyme: NADP-dependent 3-hydroxy acid dehydrogenase YdfG


substrate_name: D-threonine (at pH 9 and at 30 degrees Celsius)

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


substrate_name: L-glycerate (at pH 9 and at 30 degrees Celsius)

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


substrate_name: D-glycerate (at pH 9 and at 30 degrees Celsius)


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


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


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


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


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


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


organism: Sus scrofa

substrate_name: 16-Ketoestrone (at pH6)

proof_lines: kcat is 45 min(-1) with all-trans-Retinal as substrate (at pH7.4) (PubMed:12604222). kcat is 990 min(-1) with isatin as substrate (at pH6) (PubMed:12604222). kcat is 1180 min(-1) with 1-phenyl-1,2-propanedione as substrate (at pH6) (PubMed:

substrate: 16-Ketoestrone (at pH6)


substrate_name: all-trans-Retinal (at pH7.4)

substrate: all-trans-Retinal (at pH7.4)


substrate_name: isatin (at pH6)

substrate: isatin (at pH6)


substrate_name: Propiophenone (at pH6)

substrate: Propiophenone (at pH6)


substrate_name: Heptanophenone (at pH6)

substrate: Heptanophenone (at pH6)


substrate_name: Nonanophenone (at pH6)

substrate: Nonanophenone (at pH6)


substrate_name: 4-Hexanoylpyridine (at pH6)

substrate: 4-Hexanoylpyridine (at pH6)


substrate_name: Hexanophenone (at pH6)

substrate: Hexanophenone (at pH6)


substrate_name: Valerophenone (at pH6)

substrate: Valerophenone (at pH6)


substrate_name: n-Butyrophenone (at pH6)

substrate: n-Butyrophenone (at pH6)


substrate_name: 3-Benzoylpyridine (at pH6)

substrate: 3-Benzoylpyridine (at pH6)


substrate_name: 4-Benzoylpyridine (at pH6)

substrate: 4-Benzoylpyridine (at pH6)


substrate_name: 2,3-Hexanedione (at pH6)

substrate: 2,3-Hexanedione (at pH6)


substrate_name: 1-phenyl-1,2-propanedione (at pH6)

substrate: 1-phenyl-1,2-propanedione (at pH6)


substrate_name: Benzil (at pH6)

substrate: Benzil (at pH6)


substrate_name: Diacetyl (at pH6)

substrate: Diacetyl (at pH6)


substrate_name: Pyridine-4-aldehyde (at pH6)

substrate: Pyridine-4-aldehyde (at pH6)


substrate_name: 1-Phenylisatin (at pH6)

substrate: 1-Phenylisatin (at pH6)


substrate_name: 9,10-Phenanthrenequinone (at pH6)

substrate: 9,10-Phenanthrenequinone (at pH6)


substrate_name: Menadione (at pH6)

substrate: Menadione (at pH6)


substrate_name: S-(-)-1-Phenyl-1-butanol (at pH7.4)

substrate: S-(-)-1-Phenyl-1-butanol (at pH7.4)


substrate_name: all-trans-Retinol (at pH7.4)

substrate: all-trans-Retinol (at pH7.4)


enzyme_display_name: Retinol dehydrogenase 14

substrate_name: NADPH

assay_conditions_summary: cofactor NADPH

column_label: Abstract/prose sentence lists NADPH apparent Km = 0.32 uM, matching the UniProt exported row after conversion to 0.00032 mM.

raw_value_unit_evidence: Abstract/prose reports apparent Km for NADPH is 0.32 uM.

row_label: NADPH

table_label: Abstract/prose apparent Km sentence

enzyme: Retinol dehydrogenase 14

substrate: NADPH


substrate_name: NADP

assay_conditions_summary: cofactor NADP+

column_label: Abstract/prose sentence lists NADP+ apparent Km = 0.65 uM, matching the UniProt exported NADP/NADP+ row after conversion to 0.00065 mM.

raw_value_unit_evidence: Abstract/prose reports apparent Km for NADP+ is 0.65 uM.

row_label: NADP+ cofactor (export substrate label NADP)

substrate: NADP


substrate_name: all-trans-retinal

proof_lines: Vmax is measured per mg microsomal protein.

substrate: all-trans-retinal


substrate_name: all-trans-retinol

substrate: all-trans-retinol


substrate_name: NADH

column_label: Abstract/prose sentence lists NADH apparent Km = 1060 uM, matching the UniProt exported row after conversion to 1.06 mM.

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

raw_value_unit_evidence: Abstract/prose reports apparent Km for NADH is 1060 uM.

substrate: NADH


enzyme_display_name: D-arabitol-phosphate dehydrogenase

organism: Enterococcus avium

assay_conditions_summary: pH 7.2; cofactor NADH

proof_lines: 20°C, pH 7.2, cosubstrate: D-xylulose 5-phosphate

enzyme: D-arabitol-phosphate dehydrogenase


assay_conditions_summary: pH 7.2; cofactor NADPH


substrate_name: NAD+

assay_conditions_summary: pH 8.5; cofactor NAD+

proof_lines: 20°C, pH 8.5: cosubstrate: D-arabitol 5-phosphate

proof_lines: 20°C, pH 8.5, cosubstrate: D-arabitol 1-phosphate

substrate: NAD+


substrate_name: NADP+

assay_conditions_summary: pH 8.5; cofactor NADP+

substrate: NADP+


substrate_name: D-arabitol 1-phosphate

proof_lines:
20°C, pH 8.5, cofactor: NAD+
20°C, pH 8.5, cofactor: NADP+

substrate: D-arabitol 1-phosphate


enzyme_display_name: diacetyl reductase [(S)-acetoin forming]

organism: Columba livia

assay_conditions_summary: pH 5.9; 298.15 K; cofactor NADH


substrate_name: diacetyl

assay_conditions_summary: pH 6.7; 298.15 K; cofactor NADH

enzyme: diacetyl reductase [(S)-acetoin forming]

substrate: diacetyl


enzyme_display_name: malate dehydrogenase [NAD(P)+]

organism: Flavobacterium frigidimaris

assay_conditions_summary: 283.15 K; cofactor NAD+

enzyme: malate dehydrogenase [NAD(P)+]


substrate_name: L-malate

substrate: L-malate


enzyme_display_name: Aldo-keto reductase family 1 member B1

organism: Homo sapiens

substrate_name: acrolein

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

enzyme: Aldo-keto reductase family 1 member B1

substrate: acrolein


smiles: CC(=CC=O)C


smiles: CC=CC=CC=O


organism: Geobacillus stearothermophilus

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


enzyme_display_name: D-xylose reductase [NAD(P)H]

organism: Yamadazyma tenuis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K274M to reconstruct the assayed variant sequence.

enzyme: D-xylose reductase [NAD(P)H]


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K274R to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 7; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K274G to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature K274R/N276D with inferred residue-numbering offset -23 to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature N276D to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature R280H to reconstruct the assayed variant sequence.


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S275A with inferred residue-numbering offset +11 to reconstruct the assayed variant sequence.


organism: Thermochaetoides thermophila

substrate_name: D-glucose

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

assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADPH

proof_lines: recombinant enzyme, pH 6.5, 30°C, with NADPH

substrate: D-glucose


assay_conditions_summary: pH 6.5; 303.15 K; cofactor NADH

proof_lines: recombinant enzyme, pH 6.5, 30°C, with D-xylose


substrate_name: L-arabinose

proof_lines: recombinant enzyme, pH 6.5, 55°C, with NADPH

substrate: L-arabinose


organism: Neurospora crassa

substrate_name: D-xylose

assay_conditions_summary: pH 6.3; 298.15 K; cofactor NADPH

proof_lines:
pH 6.3, 25°C, cosubstrate: NADH
pH 6.3, 25°C
pH 6.3, 25°C, cosubstrate: NADPH

substrate: D-xylose


assay_conditions_summary: pH 6.3; 298.15 K; cofactor NADH


organism: Scheffersomyces stipitis

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K21A with inferred residue-numbering offset +15 to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; cofactor NADH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K21A/N272D to reconstruct the assayed variant sequence.


proof_lines: pH 6.0, wild-type enzyme, wild-type enzyme


proof_lines: mutant K21A/N272D, cosubstrate NADH, pH 6.5, 35°C


proof_lines: mutant K21A, cosubstrate NADH, pH 6.5, 35°C


substrate_name: 5alpha-Pregnane-3,20-dione (at pH7.4)

substrate: 5alpha-Pregnane-3,20-dione (at pH7.4)


substrate_name: Dehydrolithocholic acid (at pH7.4)

substrate: Dehydrolithocholic acid (at pH7.4)


substrate_name: 2,3-Pentanedione (at pH6)

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

assay_conditions_summary: pH 6

substrate: 2,3-Pentanedione (at pH6)


substrate_name: Methyl benzoylformate (at pH6)

substrate: Methyl benzoylformate (at pH6)


substrate_name: 4-Nitrobenzaldehyde (at pH6)

substrate: 4-Nitrobenzaldehyde (at pH6)


enzyme_display_name: Aldo-keto reductase family 1 member B10

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

enzyme: Aldo-keto reductase family 1 member B10


enzyme_display_name: UniProt D3U1D9

organism: Klebsiella oxytoca

enzyme: UniProt D3U1D9


substrate_name: isethionate

substrate: isethionate


enzyme_display_name: UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)

organism: Ralstonia solanacearum

substrate_name: UDP-glucuronic acid

substrate: UDP-glucuronic acid


assay_conditions_summary: pH 7.6; cofactor NAD+

enzyme: UDP-glucuronic acid dehydrogenase (UDP-4-keto-hexauronic acid decarboxylating)


organism: Mus musculus

substrate_name: D,L-glyceraldehyde

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

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

substrate: D,L-glyceraldehyde


substrate_name: D-glucuronate

substrate: D-glucuronate


enzyme_display_name: (S)-sulfolactate dehydrogenase

organism: Chromohalobacter israelensis

substrate_name: NADH

assay_conditions_summary: pH 9; 298.15 K; buffer 25 mM Tris; cofactor NADH

proof_lines: apparent value, in 25 mM Tris buffer, pH 9.0 and 25°C

enzyme: (S)-sulfolactate dehydrogenase

substrate: NADH


assay_conditions_summary: pH 9; 298.15 K; buffer 25 mM Tris


substrate_name: NAD+

assay_conditions_summary: pH 9; 298.15 K; buffer 25 mM Tris; cofactor NAD+

substrate: NAD+


enzyme_display_name: Retinol dehydrogenase 11

substrate_name: all-trans-retinal

assay_conditions_summary: cofactor NADPH

proof_lines: kcat is 167 min(-1) for NADPH as substrate.

enzyme: Retinol dehydrogenase 11

substrate: all-trans-retinal


smiles: CCCCCCCCCO


substrate_name: NADPH

substrate: NADPH


enzyme_display_name: Malate dehydrogenase

organism: Aeropyrum pernix (strain ATCC 700893 / DSM 11879 / JCM 9820 / NBRC 100138 / K1)

substrate_name: (2S,3S)-tartrate (in the presence of NAD)

proof_lines: kcat is 2.6 sec(-1) for NAD-dependent malate oxidation. kcat is 1.4 sec(-1) for NADP-dependent malate oxidation.

enzyme: Malate dehydrogenase


substrate_name: NAD (in the presence of malate)

substrate: NAD (in the presence of malate)


substrate_name: NADP (in the presence of malate)

substrate: NADP (in the presence of malate)


substrate_name: glucose

substrate: glucose


enzyme_display_name: 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase

organism: Sphingomonas paucimobilis

assay_conditions_summary: cofactor NAD+

proof_lines:
in the presence of NAD+
in the presence of NADP+


substrate_name: NADP+

assay_conditions_summary: cofactor NADP+

enzyme: 2-hydroxy-4-carboxymuconate semialdehyde hemiacetal dehydrogenase

substrate: NADP+


organism: Chlorobaculum tepidum

substrate_name: diacetyl

substrate: diacetyl


enzyme_display_name: 5-exo-hydroxycamphor dehydrogenase

organism: Pseudomonas putida

enzyme: 5-exo-hydroxycamphor dehydrogenase


enzyme_display_name: isoeugenol synthase

organism: Daucus carota subsp. sativus

substrate_name: coniferyl acetate

enzyme: isoeugenol synthase

substrate: coniferyl acetate


assay_conditions_summary: pH 7; 303.15 K; cofactor NADPH


enzyme_display_name: eugenol synthase

organism: Ocimum kilimandscharicum

enzyme: eugenol synthase


substrate_name: 4-coumaryl acetate

substrate: 4-coumaryl acetate


organism: Phytopseudomonas straminea

assay_conditions_summary: 298.15 K; cofactor NADP+


substrate_name: Unknown

proof_lines: coenzyme NADP+, similar value with coenzyme NAD+

substrate: Unknown


organism: Larrea tridentata


enzyme_display_name: UniProt Q7NQL0

organism: Chromobacterium violaceum

substrate_name: UDP-alpha-D-glucuronate

enzyme: UniProt Q7NQL0

substrate: UDP-alpha-D-glucuronate


organism: Ocimum tenuiflorum


enzyme_display_name: benzil reductase [(S)-benzoin forming]

organism: Ogataea glucozyma

substrate_name: benzil

sequence_source: GenBank: AKP95857.1

assay_conditions_summary: pH 8; cofactor NADPH

enzyme: benzil reductase [(S)-benzoin forming]

substrate: benzil


enzyme_display_name: chanoclavine-I dehydrogenase

organism: Penicillium roqueforti

assay_conditions_summary: 303.15 K; cofactor NAD+

proof_lines: pH not specified in the publication, 30°C

enzyme: chanoclavine-I dehydrogenase


substrate_name: chanoclavine-I

substrate: chanoclavine-I


organism: Trichophyton benhamiae


assay_conditions_summary: pH 7.5; 310.15 K; cofactor NAD+


organism: Bordetella pertussis


proof_lines: presence of transaminase WlbC, 25°C, pH 8.5


assay_conditions_summary: pH 8.5; 298.15 K; cofactor NAD+


enzyme_display_name: (+)-thujan-3-ol dehydrogenase

organism: Tanacetum vulgare

enzyme: (+)-thujan-3-ol dehydrogenase


enzyme_display_name: (-)-endo-fenchol dehydrogenase

organism: Anethum foeniculum

substrate_name: (-)-endo-fenchol

enzyme: (-)-endo-fenchol dehydrogenase

substrate: (-)-endo-fenchol


organism: Ocimum gratissimum


organism: Weissella confusa

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

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


substrate_name: phenylglyoxylate

substrate: phenylglyoxylate


substrate_name: pyruvate

substrate: pyruvate


substrate_name: phenylpyruvate

substrate: phenylpyruvate


substrate_name: oxo-tert-leucine

substrate: oxo-tert-leucine


sequence_source: GenBank: AAQ61788.1

column_label: pmc3050068_jats.xml table-wrap T3: row Km for the UDP-sugar / column C. violaceum WlbA with UDP-GlcA = 0.20 +/- 0.02; row kcat = 0.00015 +/- 0.00001; row kcat/Km UDP-linked sugar = 0.75

raw_value_unit_evidence: Table 3 column C. violaceum WlbA with UDP-GlcA: Km 0.20 +/- 0.02 mM; kcat 0.00015 +/- 0.00001 s^-1; kcat/Km 0.75 M^-1 s^-1

row_label: C. violaceum WlbA with UDP-GlcA; rows Km for the UDP-sugar, kcat, kcat/Km UDP-linked sugar

table_label: Table 3 Kinetic Parameters


substrate_name: NAD+

assay_conditions_summary: pH 8.5; cofactor NAD+

column_label: pmc3050068_jats.xml table-wrap T3: row Km NAD+ / column C. violaceum WlbA with UDP-GlcNAcA = 0.47 +/- 0.07

normalized_value_unit_evidence: Km 0.47 mM

raw_value_unit_evidence: Table 3 column C. violaceum WlbA with UDP-GlcNAcA: Km NAD+ 0.47 +/- 0.07 mM

row_label: C. violaceum WlbA with UDP-GlcNAcA; row Km NAD+

substrate: NAD+


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


organism: Pimpinella anisum

sequence_source: UniProt: B8RCD2


enzyme_display_name: D-2-hydroxyacid dehydrogenase (NAD+)

organism: Lacticaseibacillus paracasei

substrate_name: NADH

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

source_databases_merged: brenda skid uniprot

enzyme: D-2-hydroxyacid dehydrogenase (NAD+)

substrate: NADH


proof_lines: pH 7.0, 30°C, mutant enzyme del I81/delK82/delN87/delP88


proof_lines: pH 7.0, 30°C, mutant enzyme del I81/delK82


proof_lines:
pH 7.0, 30°C, mutant enzyme del I81
pH 7.0, 30°C, mutant enzyme delK82
pH 7.0, 30°C, mutant enzyme delP88


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

organism: Thermotoga maritima

assay_conditions_summary: pH 7.5; 343.15 K; cofactor NAD+

proof_lines: wild type enzyme, in 100 mM HEPES (pH 7.5), at 70°C


proof_lines: mutant enzyme N32D/R33L/T34S, in 100 mM HEPES (pH 7.5), at 70°C

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


proof_lines: mutant enzyme N32D, in 100 mM HEPES (pH 7.5), at 70°C


proof_lines: mutant enzyme N32D/R33I/T34I, in 100 mM HEPES (pH 7.5), at 70°C


proof_lines: mutant enzyme N32E/R33I7T34I, in 100 mM HEPES (pH 7.5), at 70°C


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


substrate_name: L-lactate

substrate: L-lactate


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


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


smiles: CCCCCCC(=O)C(=O)[O-]


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


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


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


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


smiles: CCCCCCC(C(=O)[O-])O


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

organism: Gossypium hirsutum

substrate_name: NADPH

assay_conditions_summary: pH 7.5; 310.15 K; cofactor NADPH

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

substrate: NADPH


substrate_name: Nonanal

smiles: CCCCCCCCC=O

substrate: Nonanal


enzyme_display_name: L-galactose 1-dehydrogenase

organism: Lathyrus oleraceus

substrate_name: L-galactose

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

proof_lines: pH 7.5, temperature not specified in the publication

enzyme: L-galactose 1-dehydrogenase

substrate: L-galactose


organism: Methanobrevibacter millerae

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADH


substrate_name: sulfopyruvate

substrate: sulfopyruvate


organism: Gluconacetobacter diazotrophicus

proof_lines: pH 7.5, temperature not specified in the publication, membrane-purified enzyme

proof_lines: pH 7.5, temperature not specified in the publication, cytoplasm-purified enzyme


substrate_name: NADP+

assay_conditions_summary: pH 7.5; cofactor NADP+

substrate: NADP+


assay_conditions_summary: pH 7.5; cofactor NAD+


organism: Methanothermus fervidus

assay_conditions_summary: pH 8; 343.15 K; cofactor NADH

proof_lines:
cosubstrate NADH, pH 8.0, 70°C
cosubstrate NADPH, pH 8.0, 70°C


substrate_name: oxaloacetate

substrate: oxaloacetate


enzyme_display_name: 8-hydroxygeraniol dehydrogenase

organism: Rauvolfia serpentina

substrate_name: Nerol; NADP+

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

assay_conditions_summary: pH 9; 298.15 K; cofactor NADP+

enzyme: 8-hydroxygeraniol dehydrogenase

substrate: Nerol; NADP+


assay_conditions_summary: pH 7


organism: Petunia x hybrida

substrate_name: coniferyl acetate

substrate: coniferyl acetate


organism: Musca domestica

substrate_name: sepiapterin

proof_lines:
pH 6.4, 37°C
pH 6.4, 37°C, recombinant enzyme

substrate: sepiapterin


enzyme_display_name: Benzil reductase ((S)-benzoin forming)

organism: Bacillus cereus

substrate_name: benzil (with NADPH at 37 degrees Celsius and pH 6.5)

assay_conditions_summary: pH 6.5; cofactor NADPH

proof_lines: kcat is 64.4 min(-1) with benzil as substrate. kcat is 165 min(-1) with 1-phenyl-1,2-propanedione as substrate. kcat is 7.4 min(-1) with 1,4-naphthoquinone as substrate. kcat is 1.2 min(-1) with p-nitrobenzaldehyde as substrate. kcat is 31.

enzyme: Benzil reductase ((S)-benzoin forming)


substrate_name: 1-phenyl-1,2-propanedione (with NADPH at 37 degrees Celsius and pH 6.5)


substrate_name: 1,4-naphthoquinone (with NADPH at 37 degrees Celsius and pH 6.5)


substrate_name: p-nitrobenzaldehyde (with NADPH and at 37 degrees Celsius and pH 6.5)


substrate_name: methyl benzoylformate (with NADPH and at 37 degrees Celsius and pH 6.5)


enzyme_display_name: CDP-paratose synthase

organism: Salmonella enterica subsp. enterica serovar Typhi

assay_conditions_summary: pH 8; 298.15 K; cofactor NADPH

enzyme: CDP-paratose synthase


enzyme_display_name: Retinol dehydrogenase 11

organism: Homo sapiens

assay_conditions_summary: cofactor NADPH

proof_lines: Vmax is measured per mg microsomal protein.

enzyme: Retinol dehydrogenase 11


substrate_name: NADP

substrate: NADP


substrate_name: all-trans-retinal

substrate: all-trans-retinal


substrate_name: all-trans-retinol

substrate: all-trans-retinol


enzyme_display_name: D-xylose reductase [NAD(P)H]

organism: Scheffersomyces stipitis

substrate_name: D-xylose

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_consensus_sequence and applied mutation signature K270S/N272P/S271G/R276F to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6; cofactor NADPH

proof_lines: pH 6.0, cofactor: NADPH, mutant enzyme K270S/N272P/S271G/R276F

proof_lines: pH 6.0, cofactor: NADH, mutant enzyme K270S/N272P/S271G/R276F

enzyme: D-xylose reductase [NAD(P)H]

substrate: D-xylose


substrate_name: NADPH

proof_lines: pH 6.0, mutant enzyme K270S/N272P/S271G/R276F


substrate_name: NADH

assay_conditions_summary: pH 6; cofactor NADH


proof_lines: pH 6.0, cofactor: NADH, wild-type enzyme

proof_lines: pH 6.0, cofactor: NADPH, wild-type enzyme

proof_lines: wild-type, cosubstrate NADPH, pH 6.5, 35°C


proof_lines: pH 6.0, wild-type enzyme, wild-type enzyme


organism: Methanocaldococcus jannaschii

assay_conditions_summary: pH 8; cofactor NADPH

proof_lines:
pH 8.0, 70°C
cosubstrate NADH, pH 8.0, 70°C
cosubstrate NADPH, pH 8.0, 70°C


substrate_name: 2-oxopentanedioic acid

assay_conditions_summary: pH 8; cofactor NADH

proof_lines:
pH 8.0, 70°C
cosubstrate NADH, pH 8.0, 70°C

substrate: 2-oxopentanedioic acid


enzyme_display_name: methylecgonone reductase

organism: Erythroxylum coca

substrate_name: NADP+

assay_conditions_summary: pH 6.8; cofactor NADP+

proof_lines: pH 6.8, temperature not specified in the publication

enzyme: methylecgonone reductase


enzyme_display_name: Dehydrogenase/reductase SDR family member 4

organism: Oryctolagus cuniculus

substrate_name: 4-Acetylpyridine (at pH6)

assay_conditions_summary: pH 6

proof_lines: kcat is 2 min(-1) with 5beta-Pregnane-3,20-dione as substrate (at pH7.4).

substrate: 4-Acetylpyridine (at pH6)


substrate_name: Pyridine-3-aldehyde (at pH6)

enzyme: Dehydrogenase/reductase SDR family member 4

substrate: Pyridine-3-aldehyde (at pH6)


substrate_name: 4-Nitroacetophenone (at pH6)

substrate: 4-Nitroacetophenone (at pH6)


enzyme_display_name: NADP-retinol dehydrogenase

organism: Danio rerio

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature M147G with inferred residue-numbering offset -1 to reconstruct the assayed variant sequence.

enzyme: NADP-retinol dehydrogenase


substrate_name: estrone

substrate: estrone


enzyme_display_name: zerumbone synthase

organism: Zingiber zerumbet

substrate_name: NAD+

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature Y155A to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 8; 310.15 K; cofactor NAD+

enzyme: zerumbone synthase

substrate: NAD+


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S142A 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.

assay_conditions_summary: pH 8; cofactor NAD+

column_label: Table label: Table 1. Kinetic parameters for recombinant wild-type ZSD1 and four mutants. ND, enzymatic activity was not detected.. Row: Wild-type. Substrate column group: 8-HAH. Columns read: Km (lM) cell 58.5, kcat (s)1) cell 1.3, kcat ⁄ Km (lM)1Æs)1) cell 2.2 · 10)2. metric: kcat; raw value: 1.3; raw unit: s^-1; normalized value: 1.3 s^(-1); metric: Km; raw value: 58.5; raw unit: uM; normalized value: 0.0585 mM; metric: kcat/Km; raw value: 1.3 / 58.5; raw unit: s^-1 over uM; normalized value: 22.22222222222222 s^-1 mM^-1; assay condition: Recombinant wild-type ZSD1 (Zingiber zerumbet short-chain dehydrogenase, expressed in Escherichia coli and purified); kinetics assay done in a volume of 1 mL with 20 mM KH2PO4 (pH 8.0), 1 mM NAD and 10 mM EDTA; the reaction was monitored at 37 C by absorbance at 340 nm. Export row conditions: pH 8.

normalized_value_unit_evidence: 8-HAH column group of Table 1 wild-type row: kcat 1.3 s^-1 = 1.3 s^(-1); Km 58.5 uM = 0.0585 mM (1 uM = 0.001 mM); kcat/Km = 1.3 s^-1 / 58.5 uM = 22.22222222222222 s^-1 mM^-1. The printed kcat ⁄ Km cell 2.2 · 10)2 lM)1Æs)1 is the paper's 2.2 x 10^-2 uM^-1 s^-1 = 22.0 s^-1 mM^-1; the exported quotient rounds to that printed cell at the printed cell's own precision, so the two agree. In the PDF text layer the micro sign renders as `l` (so `lM` is the paper's uM), the superscript minus one renders as `)1` (so `s)1` is s^-1 and `10)1` is 10^-1), the multiplication sign renders as `·`, the fraction slash in kcat ⁄ Km renders as `⁄`, and the middle dot in compound units renders as `Æ`.

raw_value_unit_evidence: Table 1. Kinetic parameters for recombinant wild-type ZSD1 and four mutants. ND, enzymatic activity was not detected. | substrate column-group header row of Table 1: NAD+                                          8-HAH                                         Borneol | metric header row (superscripts flattened by the PDF text layer): Km (lM)   kcat (s )   kcat ⁄ Km (lM Æs )      Km (lM)   kcat (s )   kcat ⁄ Km (lM Æs )      Km (lM)   kcat (s)1)   kcat ⁄ Km (lM)1Æs)1) | wild-type data row: Wild-type    27.3     3.8         1.39 · 10)1              58.5     1.3         2.2 · 10)2               22.8     4.1          1.79 · 10)1 | 8-HAH column group of the wild-type row reads: Km = 58.5 lM (58.5 uM); kcat = 1.3 s^-1; printed kcat ⁄ Km cell = 2.2 · 10)2 lM)1Æs)1 (2.2 x 10^-2 uM^-1 s^-1).

row_label: Wild-type | 8-HAH


sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature S144A to reconstruct the assayed variant sequence.


column_label: Table label: Table 1. Kinetic parameters for recombinant wild-type ZSD1 and four mutants. ND, enzymatic activity was not detected.. Row: Wild-type. Substrate column group: NAD+. Columns read: Km (lM) cell 27.3, kcat (s)1) cell 3.8, kcat ⁄ Km (lM)1Æs)1) cell 1.39 · 10)1. metric: kcat; raw value: 3.8; raw unit: s^-1; normalized value: 3.8 s^(-1); metric: Km; raw value: 27.3; raw unit: uM; normalized value: 0.0273 mM; metric: kcat/Km; raw value: 3.8 / 27.3; raw unit: s^-1 over uM; normalized value: 139.19413919413918 s^-1 mM^-1; assay condition: Recombinant wild-type ZSD1 (Zingiber zerumbet short-chain dehydrogenase, expressed in Escherichia coli and purified); kinetics assay done in a volume of 1 mL with 20 mM KH2PO4 (pH 8.0), 1 mM NAD and 10 mM EDTA; the reaction was monitored at 37 C by absorbance at 340 nm. Export row conditions: pH 8; cofactor NAD+.

normalized_value_unit_evidence: NAD+ column group of Table 1 wild-type row: kcat 3.8 s^-1 = 3.8 s^(-1); Km 27.3 uM = 0.0273 mM (1 uM = 0.001 mM); kcat/Km = 3.8 s^-1 / 27.3 uM = 139.19413919413918 s^-1 mM^-1. The printed kcat ⁄ Km cell 1.39 · 10)1 lM)1Æs)1 is the paper's 1.39 x 10^-1 uM^-1 s^-1 = 139.0 s^-1 mM^-1; the exported quotient rounds to that printed cell at the printed cell's own precision, so the two agree. In the PDF text layer the micro sign renders as `l` (so `lM` is the paper's uM), the superscript minus one renders as `)1` (so `s)1` is s^-1 and `10)1` is 10^-1), the multiplication sign renders as `·`, the fraction slash in kcat ⁄ Km renders as `⁄`, and the middle dot in compound units renders as `Æ`.

raw_value_unit_evidence: Table 1. Kinetic parameters for recombinant wild-type ZSD1 and four mutants. ND, enzymatic activity was not detected. | substrate column-group header row of Table 1: NAD+                                          8-HAH                                         Borneol | metric header row (superscripts flattened by the PDF text layer): Km (lM)   kcat (s )   kcat ⁄ Km (lM Æs )      Km (lM)   kcat (s )   kcat ⁄ Km (lM Æs )      Km (lM)   kcat (s)1)   kcat ⁄ Km (lM)1Æs)1) | wild-type data row: Wild-type    27.3     3.8         1.39 · 10)1              58.5     1.3         2.2 · 10)2               22.8     4.1          1.79 · 10)1 | NAD+ column group of the wild-type row reads: Km = 27.3 lM (27.3 uM); kcat = 3.8 s^-1; printed kcat ⁄ Km cell = 1.39 · 10)1 lM)1Æs)1 (1.39 x 10^-1 uM^-1 s^-1).

row_label: Wild-type | NAD+


enzyme_display_name: Zerumbone synthase

substrate_name: NAD

assay_conditions_summary: pH 8; cofactor NADP+

column_label: Table 1 wild-type row, NAD+ Km column reports 27.3 uM and kcat 3.8 s^-1; 27.3 uM normalizes to 0.0273 mM.

raw_value_unit_evidence: Km raw_value=27.3 raw_unit=uM; kcat raw_value=3.8 raw_unit=s^-1

row_label: Wild-type

table_label: Table 1. Kinetic parameters for recombinant wild-type ZSD1 and four mutants

enzyme: Zerumbone synthase

substrate: NAD


column_label: Table 1 wild-type row, 8-HAH Km column reports 58.5 uM and kcat 1.3 s^-1; 58.5 uM normalizes to 0.0585 mM.

raw_value_unit_evidence: Km raw_value=58.5 raw_unit=uM; kcat raw_value=1.3 raw_unit=s^-1


substrate_name: borneol

column_label: Table 1 wild-type row, Borneol Km column reports 22.8 uM and kcat 4.1 s^-1; 22.8 uM normalizes to 0.0228 mM.

raw_value_unit_evidence: Km raw_value=22.8 raw_unit=uM; kcat raw_value=4.1 raw_unit=s^-1

substrate: borneol


organism: Rasamsonia emersonii

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_mutation_ranked_match and applied mutation signature K271R/N273D to reconstruct the assayed variant sequence.

assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADH

substrate: NADH


assay_conditions_summary: pH 6.5; 310.15 K; cofactor NADPH

substrate: NADPH


enzyme_display_name: phosphonoacetaldehyde reductase (NADH)

organism: Streptomyces viridochromogenes

substrate_name: phosphonoacetaldehyde

proof_lines: in 50 mM HEPES, 200 mM NaCl, pH 7.5, temperature not specified in the publication

enzyme: phosphonoacetaldehyde reductase (NADH)

substrate: phosphonoacetaldehyde


assay_conditions_summary: pH 7.5; cofactor NADH


assay_conditions_summary: pH 6.8; cofactor NADPH

proof_lines: substrate inhibition, pH 6.8, temperature not specified in the publication

proof_lines: kcat is 0.24 sec(-1) for ecgonone methyl ester. kcat is 0.121 sec(-1) for NADPH. kcat is 5.538 sec(-1) for ecgonine methyl ester. kcat is 5.238 sec(-1) for NADP(+).


substrate: NADP+


substrate_name: methyl ecgonone

substrate: methyl ecgonone


substrate_name: methyl ecgonine

substrate: methyl ecgonine


enzyme_display_name: Methylecgonone reductase

substrate_name: NADP(+)

enzyme: Methylecgonone reductase

substrate: NADP(+)


organism: Spathaspora arborariae

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


enzyme_display_name: Aldo-keto reductase family 1 member B10

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

column_label: The abstract reports AKR1B10 reduces 4-oxonon-2-enal with Km = 0.3 mM and kcat = 40 min^-1.

raw_value_unit_evidence: Km raw_value=0.3 mM raw_unit=mM

row_label: Prose segment: 4-oxonon-2-enal Km

table_label: PubMed PMID 19013440 abstract

enzyme: Aldo-keto reductase family 1 member B10


smiles: CC(C)CCC=O

column_label: The abstract reports AKR1B10 reduces 4-methylpentanal with Km = 0.05 mM and kcat = 25 min^-1.

raw_value_unit_evidence: Km raw_value=0.05 mM raw_unit=mM

row_label: Prose segment: 4-methylpentanal Km


organism: Arabidopsis thaliana

assay_conditions_summary: pH 7.5; cofactor NAD+

proof_lines: pH 7.5, temperature not specified in the publication


substrate_name: L-galactose

substrate: L-galactose


assay_conditions_summary: pH 7.5; cofactor NADP+


substrate_name: L-fucose

substrate: L-fucose


enzyme_display_name: Eugenol synthase 1

organism: Clarkia breweri

substrate_name: coniferyl acetate

raw_value_unit_evidence: Km raw_value=93.3 raw_unit=uM

table_label: Table 3 - Kinetic parameters of C. breweri and P. hybrida EGS and IGS enzymes for coniferyl acetate

enzyme: Eugenol synthase 1

substrate: coniferyl acetate


enzyme_display_name: Eugenol synthase 2

raw_value_unit_evidence: Km raw_value=310.5 raw_unit=uM

enzyme: Eugenol synthase 2


enzyme_display_name: Benzil reductase ((S)-benzoin forming) IRC24

organism: Saccharomyces cerevisiae (strain ATCC 204508 / S288c)

substrate_name: benzil (with NADPH as cosubstrate)

proof_lines: kcat is 9.2 min(-1) with benzil as substrate. kcat is 86.2 min(-1) with 1-phenyl-1,2-propanedione as substrate.

substrate: benzil (with NADPH as cosubstrate)


enzyme: Benzil reductase ((S)-benzoin forming) IRC24


enzyme_display_name: UniProt P23457

organism: Rattus norvegicus

substrate_name: dihydrotestosterone

enzyme: UniProt P23457

substrate: dihydrotestosterone


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

organism: Gluconobacter oxydans

assay_conditions_summary: pH 7; 298.15 K; buffer 40 mM potassium phosphate

proof_lines: in 40 mM potassium phosphate buffer, at pH 7.0 and 25°C

proof_lines: kcat is 23 sec(-1). Can use NAD or NADP, but has a clear preference for NAD in vivo.


assay_conditions_summary: pH 7; 298.15 K; buffer 40 mM potassium phosphate; cofactor NAD+

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


enzyme_display_name: Isoeugenol synthase 1

organism: Petunia hybrida

substrate_name: coniferyl acetate (at pH 6.5 and 28 degrees Celsius)

proof_lines: kcat is 1.3 sec(-1) with coniferyl acetate as substrate.

enzyme: Isoeugenol synthase 1


substrate_name: NADPH (at pH 6.5 and 28 degrees Celsius)

assay_conditions_summary: pH 6.5; cofactor NADPH


enzyme_display_name: Aldo-keto reductase family 1 member B1

substrate_name: prostaglandin H2

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

enzyme: Aldo-keto reductase family 1 member B1

substrate: prostaglandin H2


enzyme_display_name: 3alpha-hydroxysteroid 3-dehydrogenase

enzyme: 3alpha-hydroxysteroid 3-dehydrogenase


substrate_name: D,L-glyceraldehyde

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

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

substrate: D,L-glyceraldehyde


substrate_name: all-trans-retinal

substrate: all-trans-retinal


substrate_name: NADPH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADPH


substrate_name: NADP+

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADP+


substrate_name: NADH

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NADH


substrate_name: NAD+

assay_conditions_summary: pH 7.4; 298.15 K; cofactor NAD+

substrate: NAD+


organism: Comamonas testosteroni

substrate_name: Cyclohexanol

proof_lines: reombinant His-tagged enzyme, pH 10.5, 25°C

substrate: Cyclohexanol


substrate_name: androsterone

proof_lines: pH 8.9, temperature not specified in the publication, NAD(P)+

substrate: androsterone


substrate_name: Fusidic acid

proof_lines: pH 8.9, temperature not specified in the publication

substrate: Fusidic acid


assay_conditions_summary: pH 7

proof_lines: pH 7.0, temperature not specified in the publication, NAD(P)H


substrate_name: cholic acid

substrate: cholic acid


substrate_name: androstandiol

substrate: androstandiol


substrate_name: Metyrapone

substrate: Metyrapone


substrate_name: metyrapol

substrate: metyrapol


substrate_name: Dehydrolithocholic acid

substrate: Dehydrolithocholic acid


substrate: NADPH


organism: Pseudomonas sp.


substrate_name: androstenol

assay_conditions_summary: pH 10.5; 298.15 K; cofactor NAD+

substrate: androstenol


proof_lines: reombinant His-tagged enzyme, pH 10.5, 25°C, with androstenol

proof_lines: reombinant His-tagged enzyme, pH 10.5, 25°C, with androsterone


enzyme_display_name: 5'-hydroxyaverantin dehydrogenase

organism: Levilactobacillus brevis

assay_conditions_summary: pH 7.5; 310.15 K; buffer 30 mM potassium phosphate

proof_lines: in 30 mM potassium phosphate buffer (pH 7.5), at 37°C

enzyme: 5'-hydroxyaverantin dehydrogenase


enzyme_display_name: Aldo-keto reductase family 1 member C2

organism: Homo sapiens

substrate_name: (s)-tetralol (oxidation)

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

enzyme: Aldo-keto reductase family 1 member C2

substrate: (s)-tetralol (oxidation)


substrate_name: benzene dihydrodiol (oxidation)

substrate: benzene dihydrodiol (oxidation)


substrate_name: prostaglandin D2 (reduction)

substrate: prostaglandin D2 (reduction)


enzyme_display_name: Aldo-keto reductase family 1 member C1

substrate_name: (s)-tetralol

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

enzyme: Aldo-keto reductase family 1 member C1

substrate: (s)-tetralol


substrate_name: dihydrotestosterone

substrate: dihydrotestosterone


substrate_name: NADPH

assay_conditions_summary: cofactor NADPH


substrate_name: NADP(+)

substrate: NADP(+)


substrate_name: allopregnanolone (oxidation)

substrate: allopregnanolone (oxidation)


enzyme_display_name: Aldo-keto reductase family 1 member C4

organism: Macaca fuscata fuscata

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

enzyme: Aldo-keto reductase family 1 member C4


enzyme_display_name: Aldo-keto reductase family 1 member C3

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

enzyme: Aldo-keto reductase family 1 member C3


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

organism: Thermoplasma acidophilum

substrate_name: beta-D-glucose

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

substrate: beta-D-glucose


organism: Saccharolobus solfataricus

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_unique and applied mutation signature T41V to reconstruct the assayed variant sequence.

proof_lines: pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41V

proof_lines: pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41V


substrate_name: D-xylose

substrate: D-xylose


sequence_variant_note: Mutation signature T41A could not be applied safely because the resolved sequence does not match the expected reference residue(s).

proof_lines: pH 7.5, 70°C, cosubstrate: NADP+, mutant enzyme T41A

proof_lines: pH 7.5, 70°C, cosubstrate: NAD+, mutant enzyme T41A


substrate_name: D-galactose

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

proof_lines: pH 7.5, 70°C, cosubstrate: NADP+, wild-type enzyme

proof_lines: pH 7.5, 70°C, cosubstrate: NAD+, wild-type enzyme

substrate: D-galactose


substrate_name: androsterone

sequence_variant_note: Resolved canonical sequence from uniprot_ec_organism_ranked_match and applied mutation signature R1C with inferred residue-numbering offset +6 to reconstruct the assayed variant sequence.

substrate: androsterone


assay_conditions_summary: pH 7; cofactor NADPH

column_label: Table 3 Kinetic parameters for 17-ketosteroid reduction and 17alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Androsterone reduction / AKR1C3; Km column raw 8.96 uM normalized 0.008960000000000001 mM

raw_value_unit_evidence: Km 8.96 uM

row_label: Androsterone reduction / AKR1C3


column_label: Table 2 Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C3; Km column raw 5.00 uM normalized 0.005 mM

raw_value_unit_evidence: Km 5.00 uM


substrate_name: testosterone (oxidation)

assay_conditions_summary: pH 7; cofactor NADP+

column_label: Table 3 Kinetic parameters for 17-ketosteroid reduction and 17alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C3 (R); Km column raw 24.3 uM normalized 0.024300000000000002 mM

raw_value_unit_evidence: Km 24.3 uM

row_label: Testosterone oxidation / AKR1C3 (R)

substrate: testosterone (oxidation)


column_label: Table 2 Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C2; Km column raw 22.0 uM normalized 0.022 mM

raw_value_unit_evidence: Km 22.0 uM


substrate_name: progesterone (reduction)

column_label: Table 4. Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation row Progesterone reduction / AKR1C1; columns Km (uM), Vmax (nmol/min per mg), 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 row Progesterone reduction / AKR1C1: Km 2.65 uM; Vmax 7.85 +/- 0.35; kcat 0.29 min^-1; kcat/Km 109 min^-1 mM^-1.

row_label: Progesterone reduction / AKR1C1

substrate: progesterone (reduction)


column_label: Table 4 Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3beta-Hydroxy-5beta-pregnan-20-one reduction / AKR1C1; Km column raw 16.2 uM normalized 0.0162 mM

raw_value_unit_evidence: Km 16.2 uM


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; Km column raw 14.7 uM normalized 0.0147 mM

raw_value_unit_evidence: Km 14.7 uM


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

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

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


column_label: Table 3 Kinetic parameters for 17-ketosteroid reduction and 17alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row Testosterone oxidation / AKR1C1 (R); Km column raw 39.8 uM normalized 0.039799999999999995 mM

raw_value_unit_evidence: Km 39.8 uM

row_label: Testosterone oxidation / AKR1C1 (R)


column_label: Table 4 Kinetic parameters for 20-ketosteroid reduction and 20alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 20alpha-Hydroxy-5beta-pregnan-3-one oxidation / AKR1C1; Km column raw 19.4 uM normalized 0.0194 mM

raw_value_unit_evidence: Km 19.4 uM


column_label: Table 2 Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 3alpha-Androstanediol oxidation / AKR1C4; Km column raw 10.5 uM normalized 0.0105 mM

raw_value_unit_evidence: Km 10.5 uM


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


column_label: Table 2 Kinetic parameters for 3-ketosteroid reduction and 3alpha-hydroxysteroid oxidation catalysed by homogeneous recombinant human 3alpha-HSD isoforms; row 5alpha-Androstane-3,17-dione reduction / AKR1C4; Km column raw 1.44 uM normalized 0.0014399999999999999 mM

raw_value_unit_evidence: Km 1.44 uM


assay_conditions_summary: pH 6.5; 343.15 K; cofactor NADP+

proof_lines:
pH 6.5, 70°C, cosubstrate: NADP+
pH 7.5, 70°C, cofactor: NADP+
pH 6.5, 70°C, cosubstrate: NAD+


substrate_name: L-arabinose

proof_lines: pH 8.0, 70°C, native enzyme from xylose-grown cell extract

substrate: L-arabinose


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

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


enzyme_display_name: D-xylose reductase [NAD(P)H]

organism: Yamadazyma tenuis

proof_lines:
pH 7, 25°C
pH 6.0, 25°C, cosubstrate: NADH
pH 7, 25°C, cosubstrate: NADH

enzyme: D-xylose reductase [NAD(P)H]


organism: Pseudomonas sp. B-0831

substrate_name: cholic acid

proof_lines: recombinant His-tagged mutant S114A/Y153F, pH 8.0, 37°C

substrate: cholic acid


proof_lines: recombinant His-tagged mutant K157A, pH 8.0, 37°C


proof_lines: recombinant His-tagged mutant Y153F, pH 8.0, 37°C


proof_lines: recombinant His-tagged mutant S114A, pH 8.0, 37°C


substrate_name: Dehydrocholic acid

substrate: Dehydrocholic acid


proof_lines: recombinant His-tagged wild-type enzyme, pH 8.0, 37°C


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


enzyme_display_name: isoeugenol synthase

substrate_name: coniferyl acetate

proof_lines: kcat is 0.99 sec(-1) with coniferyl acetate as substrate.

enzyme: isoeugenol synthase

substrate: coniferyl acetate


proof_lines: kcat is 0.60 sec(-1) with coniferyl acetate as substrate.


organism: Campylobacter jejuni

substrate_name: UDP-ManNAc

substrate: UDP-ManNAc


enzyme_display_name: 8-hydroxygeraniol dehydrogenase

organism: Nepeta racemosa

substrate_name: NADP+

assay_conditions_summary: pH 9.5; cofactor NADP+

column_label: Page 109 prose near Table II, NADP+ apparent Km: 18 uM.

raw_value_unit_evidence: Text reports apparent Km for NADP+ was 18 uM with 2.0 mM 10-hydroxynerol as substrate.

row_label: NADP+ with 10-hydroxynerol substrate

table_label: Page 109 prose near Table II

enzyme: 8-hydroxygeraniol dehydrogenase

substrate: NADP+


enzyme_display_name: perakine reductase

organism: Rauvolfia serpentina

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

enzyme: perakine reductase


organism: Streptomyces avermitilis

substrate_name: NAD+

assay_conditions_summary: pH 8; cofactor NAD+

substrate: NAD+


enzyme_display_name: 6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating

organism: Haloferax volcanii (strain ATCC 29605 / DSM 3757 / JCM 8879 / NBRC 14742 / NCIMB 2012 / VKM B-1768 / DS2)

proof_lines: The catalytic efficiency with NAD(+) is about 2000-fold higher than with NADP(+), indicating that NAD(+) is the physiological electron acceptor.


organism: Gluconobacter oxydans (strain 621H)

proof_lines: kcat is 23 sec(-1). Can use NAD or NADP, but has a clear preference for NAD in vivo.

enzyme: 6-phosphogluconate dehydrogenase, NAD(+)-dependent, decarboxylating


assay_conditions_summary: pH 9; 343.15 K; cofactor NADP+

proof_lines: pH 9.0, 70°C, cosubstrate: beta-D-glucose


assay_conditions_summary: pH 8; 343.15 K; cofactor NAD+


enzyme_display_name: versiconal hemiacetal acetate reductase

organism: Aspergillus parasiticus

substrate_name: versiconal hemiacetal acetate

assay_conditions_summary: pH 7.5; buffer 60 mM potassium phosphate

proof_lines: isoform VHA reductase II, in 60 mM potassium phosphate buffer (pH 7.5), at 37°C

proof_lines: isoform VHA reductase I, in 60 mM potassium phosphate buffer (pH 7.5), at 37°C

enzyme: versiconal hemiacetal acetate reductase

substrate: versiconal hemiacetal acetate


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

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


enzyme_display_name: NADPH-dependent D-xylose reductase

organism: Candida boidinii

substrate_name: NADPH

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

proof_lines: Mutations at positions 272 to 274 modify the cofactor specificity and increase specificity for NADH over NADPH.

enzyme: NADPH-dependent D-xylose reductase

substrate: NADPH


enzyme_display_name: GDP-L-colitose synthase

organism: Yersinia pseudotuberculosis

assay_conditions_summary: pH 7.5; cofactor NADPH

column_label: Prose reports that with NADPH the Km for 9 is 75 +/- 15 uM and Vmax is 0.037 +/- 0.003 uM min^-1.

raw_value_unit_evidence: Km raw_value=75 +/- 15 raw_unit=uM

row_label: ColC reaction with GDP-4-keto-3,6-dideoxy-D-mannose (9) and NADPH

table_label: Kinetic Properties of ColD and ColC / Figure 3B/prose

enzyme: GDP-L-colitose synthase


column_label: Table 1, substrate row '5α-DHDOC (Red)', AKR1C4 column group: Km cell = 1.7, kcat cell = 2.1, kcat/Km cell = 1.2. 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 2.1 min^-1 normalizes to 0.035 s^-1 (divide by 60); Km raw 1.7 uM normalizes to 0.0017 mM (divide by 1000); kcat/Km = 0.035 s^-1 / 0.0017 mM = 20.58823529411765 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 1.2 min^-1 uM^-1 normalizes to 20.0 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-DHDOC (Red)'; AKR1C4 column group; Km cell = 1.7 uM; kcat cell = 2.1 min^-1; printed kcat/Km cell = 1.2 min^-1 uM^-1.

row_label: 5α-DHDOC (Red) | AKR1C4 column group

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


column_label: Table 1, substrate row '5α-DHDOC (Red)', AKR1C2 column group: Km cell = 0.8, kcat cell = 0.49, kcat/Km cell = 0.61. 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 0.49 min^-1 normalizes to 0.008166666666666666 s^-1 (divide by 60); Km raw 0.8 uM normalizes to 0.0008 mM (divide by 1000); kcat/Km = 0.008166666666666666 s^-1 / 0.0008 mM = 10.208333333333334 s^-1 mM^-1, the quotient of the two same-cell-group Table 1 values; the separately printed kcat/Km cell 0.61 min^-1 uM^-1 normalizes to 10.166666666666666 s^-1 mM^-1.

raw_value_unit_evidence: Table 1; substrate row '5α-DHDOC (Red)'; AKR1C2 column group; Km cell = 0.8 uM; kcat cell = 0.49 min^-1; printed kcat/Km cell = 0.61 min^-1 uM^-1.

row_label: 5α-DHDOC (Red) | AKR1C2 column group