| EC |
3.4.17.2 |
| Accepted name: |
carboxypeptidase B |
| Reaction: |
Preferential release of a C-terminal lysine or arginine amino acid |
| Other name(s): |
protaminase; pancreatic carboxypeptidase B; tissue carboxypeptidase B; peptidyl-L-lysine [L-arginine]hydrolase |
| Comments: |
A zinc enzyme formed from procarboxypeptidase B. Isolated from cattle, pig and dogfish pancreas and other sources, including skin fibroblasts [3] and adrenal medulla [4]. In peptidase family M14 (carboxypeptidase A family). |
| Links to other databases: |
BRENDA, EXPASY, Gene, KEGG, MetaCyc, MEROPS, PDB, CAS registry number: 9025-24-5 |
| References: |
| 1. |
Folk, J.E. Carboxypeptidase B (porcine pancreas). Methods Enzymol. 19 (1970) 504–508. |
| 2. |
Brodrick, J.W., Geokas, M.C. and Largman, C. Human carboxypeptidase B. II. Purification of the enzyme from pancreatic tissue and comparison with the enzymes present in pancreatic secretion. Biochim. Biophys. Acta 452 (1976) 468–481. [DOI] [PMID: 1009123] |
| 3. |
Butterworth, J. and Duncan, J.J. Carboxypeptidase B activity of cultured skin fibroblasts and relationship to cystic fibrosis. Clin. Chim. Acta 97 (1979) 39–43. [DOI] [PMID: 40714] |
| 4. |
Wallace, E.F., Evans, C.J., Jurik, S.M., Mefford, I.N. and Barchas, J.D. Carboxypeptidase B activity from adrenal medulla. Is it involved in the processing of proenkephalin? Life Sci. 31 (1982) 1793–1796. [PMID: 6130442] |
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| [EC 3.4.17.2 created 1961 as EC 3.4.2.2, transferred 1972 to EC 3.4.12.3, transferred 1978 to EC 3.4.17.2] |
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