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Literature summary extracted from

  • Niu, L.; Liu, X.; Shi, Y.
    [Reactivity and function of cysteine residues in imidase from Pseudomonas putida YZ-26] (2011), Wei Sheng Wu Xue Bao, 51, 776-782.
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
3.5.2.16 C108G 72% of wild-type activity. Like wild-type, mutant forms tetramers. It has a high binding ability for Zn2+ Pseudomonas putida
3.5.2.16 C7G complete loss of activity. Mutant is a mixture of monomers and oligomers and displays decreased binding of Zn2+ Pseudomonas putida
3.5.2.16 C7G/C108G complete loss of activity. Mutants is a multimer, with decreased binding ability for Zn2+ Pseudomonas putida

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.5.2.16 Zn2+ residue C7 is required or binding of Zn2+ and maintaining the stability of the enzyme Pseudomonas putida

Organism

EC Number Organism UniProt Comment Textmining
3.5.2.16 Pseudomonas putida Q4JG22
-
-
3.5.2.16 Pseudomonas putida YZ-26 Q4JG22
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.2.16 DL-5-hydantoin + H2O
-
Pseudomonas putida hydantoic acid monoamide
-
?
3.5.2.16 DL-5-hydantoin + H2O
-
Pseudomonas putida YZ-26 hydantoic acid monoamide
-
?

Synonyms

EC Number Synonyms Comment Organism
3.5.2.16 CIH
-
Pseudomonas putida
3.5.2.16 cyclic imide hydrolase
-
Pseudomonas putida