| EC |
3.4.17.1 |
| Accepted name: |
carboxypeptidase A |
| Reaction: |
Release of a C-terminal amino acid, but little or no action with -Asp, -Glu, -Arg, -Lys or -Pro |
| Other name(s): |
carboxypolypeptidase; pancreatic carboxypeptidase A; tissue carboxypeptidase A |
| Comments: |
A zinc enzyme formed from procarboxypeptidase A. Isolated from cattle, pig and dogfish pancreas, and other sources including mast cells [3] and skeletal muscle [4]. Type example of peptidase family M14. |
| Links to other databases: |
BRENDA, EXPASY, Gene, GTD, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 11075-17-5 |
| References: |
| 1. |
Petra, P.H. Bovine procarboxypeptidase and carboxypeptidase A. Methods Enzymol. 19 (1970) 460–503. |
| 2. |
Reeck, G.R., Walsh, K.A. and Neurath, H. Isolation and characterization of carboxypeptidases A and B from activated pancreatic juice. Biochemistry 10 (1971) 4690–4698. [PMID: 5140186] |
| 3. |
Everitt, M.T. and Neurath, H. Rat peritoneal mast cell carboxypeptidase: localization, purification and enzymatic properties. FEBS Lett. 110 (1980) 292–296. [DOI] [PMID: 7371832] |
| 4. |
Bodwell, J.E. and Meyer, W.L. Purification and characterization of carboxypeptidase A from rat skeletal muscle. Biochemistry 20 (1981) 2767–2777. [PMID: 7018567] |
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| [EC 3.4.17.1 created 1961 as EC 3.4.2.1, transferred 1972 to EC 3.4.12.2, transferred 1978 to EC 3.4.17.1] |
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