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Literature summary 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

EC Number Protein Variants Comment Organism
5.3.3.1 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

EC Number Inhibitors Comment Organism Structure
5.3.3.1 5alpha-androstan-3,17-dione
-
Comamonas testosteroni

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
5.3.3.1 5-Androstene-3,17-dione Comamonas testosteroni
-
4-Androstene-3,17-dione
-
?

Organism

EC Number Organism UniProt Comment Textmining
5.3.3.1 Comamonas testosteroni
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.3.1 5-Androstene-3,17-dione
-
Comamonas testosteroni 4-Androstene-3,17-dione
-
?

Synonyms

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