_EC 3.4.11.27 archaeal arginyl aminopeptidase.

0 PDB entries

EC 3.-.-.- Hydrolases. [51,972 PDB entries] EC 3.4.-.- Acting on peptide bonds (peptidases). [15,920 PDB entries] EC 3.4.11.- Aminopeptidases. [590 PDB entries] EC 3.4.11.27 archaeal arginyl aminopeptidase. [-]

Reaction:		an N-terminal L-arginyl-L-aminoacyl-[protein] + H2O = an N-terminal L-alpha-aminoacyl-[protein] + L-arginine.
		N-terminal L-arginyl-L-aminoacyl-[protein] + H2O = N-terminal L-alpha-aminoacyl-[protein] + L-arginine Molecule diagrams generated from .mol files obtained from the KEGG ftp site.
Comments:		The enzyme from the archaeon Pyrococcus horikoshii OT3 is thermostable. In that enzyme Cys(100) is the nucleophile responsible for the proteolytic activity, while Tyr(120) regulates the catalytic conformation of Cys(100) through a hydrogen bond, thereby affecting enzyme activity. The activity with L-Arginine is 90-300 times higher than with other N-terminal amino acids. The enzyme shows low endopeptidase activity.
Links:		[IntEnz]   [ExPASy]   [KEGG]

There are no PDB entries in enzyme class E.C.3.4.11.27