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Literature summary for 5.3.3.1 extracted from

  • Brooks, B.; Benisek, W.F.
    Mechanism of the reaction catalyzed by DELTA5-3-ketosteroid isomerase of Comamonas (Pseudomonas) testosteroni: kinetic properties of a modified enzyme in which tyrosine 14 is replaced by 3-fluorotyrosine (1994), Biochemistry, 33, 2682-2687.
    View publication on PubMed

Protein Variants

Protein Variants Comment Organism
Y55F/Y88F replacement of Tyr14 by 3-fluorotyrosine in the Y55,88F modified form of the isomerase results in a 4-fold decrease in turnover number Comamonas testosteroni

Organism

Organism UniProt Comment Textmining
Comamonas testosteroni
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Reaction

Reaction Comment Organism Reaction ID
a 3-oxo-DELTA5-steroid = a 3-oxo-DELTA4-steroid mechanism in which the transition state for enolization is dienolate-like, characterized by relatively little proton transfer from Tyr14 in the transition state, and the intermediate in the overall reaction is dienol-like. An alternative mechanism in which the intermediate is stabilized by a short, strong hydrogen bond can also be consistent with the data Comamonas testosteroni