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Literature summary extracted from

  • Ueda, S.; Oda, M.; Imamura, S.; Ohnishi, M.
    Kinetic study of the enzymatic cycling reaction conducted with 3alpha-hydroxysteroid dehydrogenase in the presence of excessive thio-NAD+ and NADH (2004), Anal. Biochem., 332, 84-89.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.1.50 expression in Escherichia coli Pseudomonas sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.1.50 additional information
-
 additional information kinetic modeling of an enzymatic cycling reaction Pseudomonas sp.

Organism

EC Number Organism UniProt Comment Textmining
1.1.1.50 Pseudomonas sp.
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.1.1.50 a 3alpha-hydroxysteroid + NAD(P)+ = a 3-oxosteroid + NAD(P)H + H+ ordered bi bi kinetic reaction mechanism with nucleotide cofactor binding first Pseudomonas sp.
a

Synonyms

EC Number Synonyms Comment Organism
1.1.1.50 3alpha-HSD
-
 Pseudomonas sp.
1.1.1.50 3alpha-hydroxysteroid dehydrogenase
-
 Pseudomonas sp.

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.1.50 37
-
 assay at Pseudomonas sp.

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.1.50 8
-
 assay at Pseudomonas sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.1.1.50 additional information kinetic model involving cofactor-enzyme complex formation kinetics Pseudomonas sp.
1.1.1.50 NAD+
-
 Pseudomonas sp.
1.1.1.50 NADH
-
 Pseudomonas sp.
1.1.1.50 thio-NAD+
-
 Pseudomonas sp.