Literature summary for 3.5.2.16 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.

Search for more literature for 3.5.2.16

Protein Variants

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

Metals/Ions

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

Organism

Organism	UniProt	Comment	Textmining
Pseudomonas putida	Q4JG22	-	-
Pseudomonas putida YZ-26	Q4JG22	-	-

Substrates and Products (Substrate)

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

Synonyms

Synonyms	Comment	Organism
CIH	-	Pseudomonas putida
cyclic imide hydrolase	-	Pseudomonas putida

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Release 2023.1 (January 2023)