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Literature summary for 1.1.1.50 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)

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Pseudomonas sp.
-
-
-

Reaction

Reaction Comment Organism Reaction ID
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.

Synonyms

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

Temperature Optimum [°C]

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

pH Optimum

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

Cofactor

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