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Literature summary for 1.1.1.50 extracted from

  • Hwang, C.C.; Chang, P.R.; Wang, T.P.
    Contribution of remote substrate binding energy to the enzymatic rate acceleration for 3alpha-hydroxysteroid dehydrogenase/carbonyl reductase (2017), Chem. Biol. Interact., 276, 133-140 .
    View publication on PubMed
Search for more literature for 1.1.1.50

Cloned(Commentary)

Cloned (Comment) Organism
-
 Comamonas testosteroni

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
androsterone + NAD+ Comamonas testosteroni
-
 androstanedione + NADH + H+
-
 ?

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni P80702
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Comamonas testosteroni

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-decalol + NAD+
-
 Comamonas testosteroni ? + NADH + H+
-
 ?
androstenol + NAD+
-
 Comamonas testosteroni ? + NADH + H+
-
 ?
androsterone + NAD+
-
 Comamonas testosteroni androstanedione + NADH + H+
-
 ?
androsterone + NAD+ the rate limiting step is the release of NADH Comamonas testosteroni androstanedione + NADH + H+
-
 ?
cyclohexanol + NAD+
-
 Comamonas testosteroni ? + NADH + H+
-
 ?

Synonyms

Synonyms Comment Organism
3alpha-HSD/CR
-
 Comamonas testosteroni
3alpha-hydroxysteroid dehydrogenase/carbonyl reductase
-
 Comamonas testosteroni

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
2.2
-
 2-decalol pH 10.5, 25°C Comamonas testosteroni
2.5
-
 Cyclohexanol pH 10.5, 25°C Comamonas testosteroni
230
-
 androstenol pH 10.5, 25°C Comamonas testosteroni
500
-
 androsterone pH 10.5, 25°C Comamonas testosteroni