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Literature summary for 1.1.1.64 extracted from

  • Inano, H.; Tamaoki, B.
    Relationship between steroids and pyridine nucleotides in the oxido-reduction catalyzed by the 17beta-hydroxysteroid dehydrogenase purified from the porcine testicular microsomal fraction (1975), Eur. J. Biochem., 53, 319-326.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.0046
-
NADP+
-
Sus scrofa
0.0108
-
NADPH
-
Sus scrofa
0.1012
-
NAD+
-
Sus scrofa
0.177
-
NADH
-
Sus scrofa

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
17beta-estradiol + NADP+ Sus scrofa
-
estrone + NADPH
-
r
testosterone + NADP+ Sus scrofa
-
androst-4-ene-3,17-dione + NADPH + H+
-
r

Organism

Organism UniProt Comment Textmining
Sus scrofa
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
testis
-
Sus scrofa
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
17beta-estradiol + NADP+
-
Sus scrofa estrone + NADPH
-
r
dehydroepiandrosterone + NADPH
-
Sus scrofa androst-5-ene-3beta,17beta-diol + NADP+
-
r
testosterone + NAD+
-
Sus scrofa androst-4-ene-3,17-dione + NADH + H+
-
?
testosterone + NADP+
-
Sus scrofa androst-4-ene-3,17-dione + NADPH + H+
-
r

Cofactor

Cofactor Comment Organism Structure
NAD+ less than 30% activity compared to NADP+ Sus scrofa
NADP+
-
Sus scrofa