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Literature summary for 5.3.3.1 extracted from

  • Childs, W.; Boxer, S.G.
    Proton affinity of the oxyanion hole in the active site of ketosteroid isomerase (2010), Biochemistry, 49, 2725-2731.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 5.3.3.1

Protein Variants

Protein Variants Comment Organism
D40N inhibition compared to wild-type enzyme, overview Pseudomonas putida

Inhibitors

Inhibitors Comment Organism Structure
2,6-dihydroxynaphthalene
-
 Pseudomonas putida
6-bromo-2-naphthol
-
 Pseudomonas putida
6-cyano-2-naphthol
-
 Pseudomonas putida
6-methoxy-2-naphthol
-
 Pseudomonas putida
equilenin
-
 Pseudomonas putida
additional information inhibitor development, a series of substituted naphthol inhibitors shows substantial variations in the contributions of the protonated and deprotonated forms when bound to the active site. Method of quantifying the contributions of each protonation state show the oxyanion hole in the active site of wild-type DELTA5-3-ketosteroid isomerase to have a proton affinity equal to a solution pKa of 10.05, which is similar to the measured pKa of 10.0 of the reaction intermediate Pseudomonas putida

Organism

Organism UniProt Comment Textmining
Pseudomonas putida
-
-
-

Synonyms

Synonyms Comment Organism
DELTA5-3-ketosteroid isomerase
-
 Pseudomonas putida
ketosteroid isomerase
-
 Pseudomonas putida

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
 additional information dissociation constants of inhibitors Pseudomonas putida