Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.1.1.152 extracted from

  • Roe, C.R.; Kaplan, N.O.
    Purification and substrate specificities of bacterial hydroxysteroid dehydrogenases (1969), Biochemistry, 8, 5093-5103.
    View publication on PubMed

Application

Application Comment Organism
analysis selective microquantitation of steroid substrates Comamonas testosteroni

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
47000
-
meniscus depletion method, gel filtration Comamonas testosteroni

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3alpha-hydroxy-5beta-androstane-17-one + NAD+ Comamonas testosteroni etiocholanolone, strong substrate specificity 5beta-androstane-3,17-dione + NADH
-
ir

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni
-
2 strains, ATCC 11996 and STDH-m
-

Purification (Commentary)

Purification (Comment) Organism
to homogeneity, chromatography techniques, preparative gel electrophoresis Comamonas testosteroni

Source Tissue

Source Tissue Comment Organism Textmining
cell culture
-
Comamonas testosteroni
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3alpha-hydroxy-5beta-androstane-17-one + NAD+ etiocholanolone, strong substrate specificity Comamonas testosteroni 5beta-androstane-3,17-dione + NADH
-
ir

Cofactor

Cofactor Comment Organism Structure
NAD+
-
Comamonas testosteroni