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ENZYME

ENZYME entry: EC 3.4.11.27

PURL: https://purl.expasy.org/enzyme/EC/3.4.11.27
Accepted Name
archaeal arginyl aminopeptidase
Reaction catalysed
an N-terminal L-arginyl-L-aminoacyl-[protein] + H2O = an N-terminal L-alpha-aminoacyl-[protein] + L-arginine
Comment(s)
  • 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.
Cross-references
BRENDA3.4.11.27
EC2PDB3.4.11.27
ExplorEnz3.4.11.27
KEGG Ligand Database for Enzyme Nomenclature3.4.11.27
IUBMB Enzyme Nomenclature3.4.11.27
MEDLINEFind literature relating to 3.4.11.27
MetaCyc3.4.11.27
Rhea expert-curated reactions3.4.11.27

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.11.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-