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Literature summary for 5.3.3.1 extracted from

  • van der Kamp, M.W.; Chaudret, R.; Mulholland, A.J.
    QM/MM modelling of ketosteroid isomerase reactivity indicates that active site closure is integral to catalysis (2013), FEBS J., 280, 3120-3131.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
D38E the mutant gives similar free energies to the native enzyme, with catalytic constants approximately 200-300times less than in wild type enzyme Comamonas testosteroni

Inhibitors

Inhibitors Comment Organism Structure
5alpha-androstan-3,17-dione
-
Comamonas testosteroni

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5-Androstene-3,17-dione Comamonas testosteroni
-
4-Androstene-3,17-dione
-
?

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5-Androstene-3,17-dione
-
Comamonas testosteroni 4-Androstene-3,17-dione
-
?

Synonyms

Synonyms Comment Organism
DELTA5-3-keto steroid isomerase
-
Comamonas testosteroni
ketosteroid isomerase
-
Comamonas testosteroni
KSI
-
Comamonas testosteroni