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Literature summary extracted from

  • Hanoian, P.; Hammes-Schiffer, S.
    Water in the active site of ketosteroid isomerase (2011), Biochemistry, 50, 6689-6700.
    View publication on PubMedView publication on EuropePMC

Protein Variants

EC Number Protein Variants Comment Organism
5.3.3.1 Y16F the number of water molecules directly hydrogen bonded to the ligand oxygen is one in the Y16F mutant Pseudomonas putida
5.3.3.1 Y16F/Y32F/Y57F the number of water molecules directly hydrogen bonded to the ligand oxygen is one in the Y16F/Y32F/Y57F mutant Pseudomonas putida
5.3.3.1 Y16S the number of water molecules directly hydrogen bonded to the ligand oxygen is approximately two in the Y16S mutant Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
5.3.3.1 Pseudomonas putida P07445
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
5.3.3.1 5,10-estrene-3,17-dione
-
Pseudomonas putida ?
-
?
5.3.3.1 5-Androstene-3,17-dione
-
Pseudomonas putida 4-Androstene-3,17-dione
-
?

Synonyms

EC Number Synonyms Comment Organism
5.3.3.1 DELTA5-3-ketosteroid isomerase
-
Pseudomonas putida
5.3.3.1 KSI
-
Pseudomonas putida