Literature summary for 3.4.19.9 extracted from

Fujimoto, Z.; Kimura, K.
Crystal structure of bacteriophage phiNIT1 zinc peptidase PghP that hydrolyzes gamma-glutamyl linkage of bacterial poly-gamma-glutamate (2012), Proteins Struct. Funct. Bioinform., 80, 722-732.

Search for more literature for 3.4.19.9

Crystallization (Commentary)

Crystallization (Comment)	Organism
to 1.9 A resolution. A zinc-binding motif, His-Glu-His, is present at the C-terminal end of the beta-sheet. The enzyme has a catalytic center containing a zinc ion and an overall topology resembling mammalian carboxypeptidase A and related enzymes	Bacillus phage phiNIT1

Protein Variants

Protein Variants	Comment	Organism
E165A	mutant shows no poly-gamma-glutamate hydrolysis activity	Bacillus phage phiNIT1
E45A	mutant shows no poly-gamma-glutamate hydrolysis activity	Bacillus phage phiNIT1
H103A	mutant shows no poly-gamma-glutamate hydrolysis activity	Bacillus phage phiNIT1
H40A	mutant shows no poly-gamma-glutamate hydrolysis activity	Bacillus phage phiNIT1
H78A	mutant shows no poly-gamma-glutamate hydrolysis activity	Bacillus phage phiNIT1

Metals/Ions

Metals/Ions	Comment	Organism	Structure
Zn2+	a zinc-binding motif, His-Glu-His, is present at the C-terminal end of the beta-sheet. The enzyme has a catalytic center containing a zinc ion and an overall topology resembling mammalian carboxypeptidase A and related enzymes	Bacillus phage phiNIT1

Organism

Organism	UniProt	Comment	Textmining
Bacillus phage phiNIT1	Q852V1	-	-

Synonyms

Synonyms	Comment	Organism
PghP	-	Bacillus phage phiNIT1

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Release 2023.1 (January 2023)