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Literature summary for 1.1.1.50 extracted from

  • Li, X.; Bertics, P.J.; Karavolas, H.J.
    Regional distribution of cytosolic and particulate 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductases in female rat brain (1997), J. Steroid Biochem. Mol. Biol., 60, 311-318.
    View publication on PubMed

Localization

Localization Comment Organism GeneOntology No. Textmining
cytoplasmic membrane integral membrane protein Rattus norvegicus
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-
cytoplasmic membrane NADH-linked 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity Rattus norvegicus
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-
cytosol NADPH-linked 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity Rattus norvegicus 5829
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Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5alpha-dihydrotestosterone + NAD(P)H + H+ Rattus norvegicus NADH-linked, particulate enzyme prefers oxidative reaction, while the NADPH-linked, cytosolic enzyme prefers the reductive reaction 5alpha-androstane-3alpha,17beta-diol + NAD(P)+
-
r
5alpha-pregnan-3,20-dione + NAD(P)H + H+ Rattus norvegicus 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity, utilizing NADH as cofactor when of particulate origin and NADPH when of cytosolic origin 5alpha-pregnane-3alpha-ol-20-one + NAD(P)+
-
r
5alpha-pregnan-3,20-dione + NADPH Rattus norvegicus
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3alpha-hydroxy-5alpha-pregnan-20-one + NADP+
-
r

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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NADPH- and NADH-linked 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity
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Source Tissue

Source Tissue Comment Organism Textmining
brain distribution in brain regions of cytosolic and particulate 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5alpha-dihydrotestosterone + NAD(P)H + H+ NADH-linked, particulate enzyme prefers oxidative reaction, while the NADPH-linked, cytosolic enzyme prefers the reductive reaction Rattus norvegicus 5alpha-androstane-3alpha,17beta-diol + NAD(P)+
-
r
5alpha-pregnan-3,20-dione + NAD(P)H 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity, utilizing NADH as cofactor when of particulate origin and NADPH when of cytosolic origin Rattus norvegicus 3alpha-hydroxy-5alpha-pregnan-20-one + NAD(P)+
-
?
5alpha-pregnan-3,20-dione + NAD(P)H + H+ 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity, utilizing NADH as cofactor when of particulate origin and NADPH when of cytosolic origin Rattus norvegicus 5alpha-pregnane-3alpha-ol-20-one + NAD(P)+
-
r
5alpha-pregnan-3,20-dione + NADPH
-
Rattus norvegicus 3alpha-hydroxy-5alpha-pregnan-20-one + NADP+
-
?
5alpha-pregnan-3,20-dione + NADPH
-
Rattus norvegicus 3alpha-hydroxy-5alpha-pregnan-20-one + NADP+
-
r
5beta-dihydrotestosterone + NAD(P)H NADH-linked, particulate enzyme prefers oxidative reaction, while the NADPH-linked, cytosolic enzyme prefers the reductive reaction Rattus norvegicus 5beta-androstan-3alpha,17beta-diol + NAD(P)+
-
r

Synonyms

Synonyms Comment Organism
5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase
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Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
NADH plasma membrane NADH-linked 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity Rattus norvegicus
NADPH cytosolic NADPH-linked 5alpha-dihydroprogesterone 3alpha-hydroxysteroid oxidoreductase activity Rattus norvegicus