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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 |
BRENDA | 3.4.17.10 |
EC2PDB | 3.4.17.10 |
ExplorEnz | 3.4.17.10 |
PRIAM enzyme-specific profiles | 3.4.17.10 |
KEGG Ligand Database for Enzyme Nomenclature | 3.4.17.10 |
IUBMB Enzyme Nomenclature | 3.4.17.10 |
IntEnz | 3.4.17.10 |
MEDLINE | Find literature relating to 3.4.17.10 |
MetaCyc | 3.4.17.10 |
Rhea expert-curated reactions | 3.4.17.10 |
UniProtKB/Swiss-Prot |
|
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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.-.-.-