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ENZYME

ENZYME entry: EC 3.4.17.10

Accepted Name
carboxypeptidase E
Alternative Name(s)
carboxypeptidase H
enkephalin convertase
Reaction catalysed
Release of C-terminal arginine or lysine residues from polypeptides
Comment(s)
  • Activated by Co(2+).
  • Inhibited by 1,10-phenanthroline and other chelating agents.
  • pH optimum 5.6.
  • Located in storage granules of secretory cells, and active in processing of protein hormones and bioactive peptides.
  • Distinct from EC 3.4.17.2 and EC 3.4.17.3.
  • Belongs to peptidase family M14.
Cross-references
BRENDA3.4.17.10
EC2PDB3.4.17.10
ExplorEnz3.4.17.10
PRIAM enzyme-specific profiles3.4.17.10
KEGG Ligand Database for Enzyme Nomenclature3.4.17.10
IUBMB Enzyme Nomenclature3.4.17.10
IntEnz3.4.17.10
MEDLINEFind literature relating to 3.4.17.10
MetaCyc3.4.17.10
Rhea expert-curated reactions3.4.17.10
UniProtKB/Swiss-Prot
P04836, CBPE_BOVINO17754, CBPE_CAEELP16870, CBPE_HUMAN
P37892, CBPE_LOPAMQ4R4M3, CBPE_MACFAQ00493, CBPE_MOUSE
A5A6K7, CBPE_PANTRP15087, CBPE_RAT

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All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.17.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.4.-.-
All ENZYME / UniProtKB/Swiss-Prot entries corresponding to 3.-.-.-