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Literature summary extracted from

  • Penning, T.M.; Bennett, M.J.; Smith-Hoog, S.; Schlegel, B.P.; Jez, J.M.; Lewis, M.
    Structure and function of 3alpha-hydroxysteroid dehydrogenase (1997), Steroids, 62, 101-111.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.213 full-length cDNA gene is expressed in Escherichia coli DH5alpha Rattus norvegicus

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.1.1.213 vapor diffusion techniques using ammonium sulfate as precipitant Rattus norvegicus

Protein Variants

EC Number Protein Variants Comment Organism
1.1.1.213 C217A resistant to inactivation by secosteroids, therefore Cys217 is the point of covalent attachment of acetylenic ketones Rattus norvegicus
1.1.1.213 D50E 1/30th catalytic efficiency of wild type, unlikely to be the general amino acid for catalysis Rattus norvegicus
1.1.1.213 D50N 1/30th catalytic efficiency of wild type, unlikely to be the general amino acid for catalysis Rattus norvegicus
1.1.1.213 H117A 1/500th catalytic efficiency of wild type, unlikely to be the general amino acid for catalysis Rattus norvegicus
1.1.1.213 K84M inactive, unable to bind steroids Rattus norvegicus
1.1.1.213 K84R inactive, unable to bind steroids Rattus norvegicus
1.1.1.213 additional information positions of Tyr/Lys pair are conserved across the aldo-keto reductase and short-chain dehydrogenase/reductase family. Tyr retains ability to form ternary complex and acts as general acid Rattus norvegicus
1.1.1.213 W148Y can catalyse steroid oxidoreduction similar to wild type, plays no role in steroid binding or catalysis Rattus norvegicus
1.1.1.213 W227Y mainly influenced in steroid binding Rattus norvegicus
1.1.1.213 W86Y plays role in cofactor and steroid binding Rattus norvegicus
1.1.1.213 Y205F kinetically indistinguishable from the wild type, no general amino acid for catalysis in 3alpha-hydroxysteroid dehydrogenase Rattus norvegicus
1.1.1.213 Y55F inactive, unable to perform steroid oxidoreduction, strongest candidate for the general amino acid Rattus norvegicus
1.1.1.213 Y55S inactive, strongest candidate for the general amino acid Rattus norvegicus

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.1.213 acetylenic ketones inactivation by forming Michael adducts with enzyme nucleophiles Rattus norvegicus
1.1.1.213 cacodylate
-
 Rattus norvegicus
1.1.1.213 citrate
-
 Rattus norvegicus
1.1.1.213 D-glucose 6-phosphate
-
 Rattus norvegicus
1.1.1.213 zopolrestat
-
 Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.213 0.0012
-
 17beta-hydroxy-5alpha-androstan-3-one cloned human liver enzyme type I Rattus norvegicus
1.1.1.213 0.0041
-
 5alpha-androstan-3,17-dione recombinant wild type enzyme Rattus norvegicus
1.1.1.213 0.0042
-
 5alpha-androstan-3,17-dione Y205F Rattus norvegicus
1.1.1.213 0.0192
-
 17beta-hydroxy-5alpha-androstan-3-one cloned human liver enzyme type II Rattus norvegicus
1.1.1.213 0.027
-
 NADH recombinant wild type enzyme Rattus norvegicus
1.1.1.213 0.029
-
 3alpha-hydroxy-5alpha-androstan-17-one Y205F Rattus norvegicus
1.1.1.213 0.03
-
 NADH Y205F Rattus norvegicus
1.1.1.213 0.042 0.408 3alpha-hydroxy-5alpha-androstan-17-one
-
 Rattus norvegicus
1.1.1.213 0.046
-
 3alpha-hydroxy-5alpha-androstan-17-one recombinant wild type enzyme Rattus norvegicus
1.1.1.213 0.83
-
 NAD+ Y205F Rattus norvegicus
1.1.1.213 0.94
-
 NAD+ recombinant wild type enzyme Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.1.1.213 cytosol
-
 Rattus norvegicus 5829
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.1.1.213 additional information non-metallo enzyme Rattus norvegicus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.1.1.213 37029
-
 1 * 37029 Rattus norvegicus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.1.1.213 17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+ Rattus norvegicus regulation of the amount of androgen in prostate, high levels of substrate are required for normal and abnormal growth of prostate 3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
 r
1.1.1.213 5alpha-pregnan-3,20-dione + NAD(P)H + H+ Rattus norvegicus regulation of the amount of allosteric agonists that can bind to the GABA receptor in brain 5alpha-pregnan-3alpha-ol-20-one + NAD(P)+
-
 r

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.213 Rattus norvegicus
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.213 a 3alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+ aldoketoreductase superfamily Rattus norvegicus
a
1.1.1.213 a 3alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+ bi bi mechanism, pyridine nucleotide binds first and leaves last Rattus norvegicus
a

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.1.1.213 liver
-
 Rattus norvegicus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.1.213 additional information
-
 enzyme contains conserved catalytic tetrad of Asp50, Tyr55, Lys84 and His117 Rattus norvegicus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.1.213 17beta-hydroxy-5alpha-androstan-3-one + NAD(P)H + H+ regulation of the amount of androgen in prostate, high levels of substrate are required for normal and abnormal growth of prostate Rattus norvegicus 3alpha,17beta-dihydroxy-5alpha-androstan + NAD(P)+
-
 r
1.1.1.213 3alpha-hydroxy-5alpha-androstan-17-one + NAD+
-
 Rattus norvegicus 5alpha-androstan-3,17-dione + NADH
-
 r
1.1.1.213 5alpha-pregnan-3,20-dione + NAD(P)H + H+ regulation of the amount of allosteric agonists that can bind to the GABA receptor in brain Rattus norvegicus 5alpha-pregnan-3alpha-ol-20-one + NAD(P)+
-
 r

Subunits

EC Number Subunits Comment Organism
1.1.1.213 monomer 1 * 37029 Rattus norvegicus
1.1.1.213 More (alpha/beta)8-barrel fold Rattus norvegicus

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.1.213 0.267
-
 5alpha-androstan-3,17-dione Y205F Rattus norvegicus
1.1.1.213 0.283
-
 NADH recombinant wild type enzyme Rattus norvegicus
1.1.1.213 0.283
-
 5alpha-androstan-3,17-dione recombinant wild type enzyme Rattus norvegicus
1.1.1.213 0.367
-
 NADH Y205F Rattus norvegicus
1.1.1.213 1.13
-
 3alpha-hydroxy-5alpha-androstan-17-one Y205F Rattus norvegicus
1.1.1.213 1.13
-
 NAD+ recombinant wild type enzyme Rattus norvegicus
1.1.1.213 1.25
-
 3alpha-hydroxy-5alpha-androstan-17-one recombinant wild type enzyme Rattus norvegicus
1.1.1.213 1.43
-
 NAD+ Y205F Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.213 additional information 4-pro-(R) hydrogen is transferred from the A-face of the cofactor to the B-face of the steroid Rattus norvegicus
1.1.1.213 NAD+
-
 Rattus norvegicus
1.1.1.213 NADH
-
 Rattus norvegicus
1.1.1.213 NADP+
-
 Rattus norvegicus
1.1.1.213 NADPH preferred Rattus norvegicus