| carboxypeptidase B1 (tissue) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | CPB1 | ||||||
| NCBI gene | 1360 | ||||||
| HGNC | 2299 | ||||||
| OMIM | 114852 | ||||||
| RefSeq | NM_001871 | ||||||
| UniProt | P15086 | ||||||
| Other data | |||||||
| EC number | 3.4.17.2 | ||||||
| Locus | Chr. 3 q24 | ||||||
| |||||||
| carboxypeptidase B2 (plasma) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | CPB2 | ||||||
| NCBI gene | 1361 | ||||||
| HGNC | 2300 | ||||||
| OMIM | 603101 | ||||||
| RefSeq | NM_016413 | ||||||
| UniProt | Q96IY4 | ||||||
| Other data | |||||||
| Locus | Chr. 13 q14.11 | ||||||
| |||||||
| carboxypeptidase B | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Carboxypeptidase B ( EC 3.4.17.2, protaminase, pancreatic carboxypeptidase B, tissue carboxypeptidase B, peptidyl-L-lysine [L-arginine]hydrolase) is a carboxypeptidase that preferentially cleaves off basic amino acids arginine and lysine from the C-terminus of a peptide. [1] [2] [3] [4] This enzyme is secreted by the pancreas, and it travels to the small intestine, where it aids in protein digestion. Plasma carboxypeptidase B (carboxypeptidase B2) is responsible for converting the C5a protein into C5a des-Arg, with one less amino acid.
References
- ^ Folk JE (1970). "Carboxypeptidase B (Porcine Pancreas)". Proteolytic Enzymes. Methods Enzymol. Vol. 19. pp. 504–508. doi: 10.1016/0076-6879(70)19036-7. ISBN 9780121818814.
- ^ Brodrick JW, Geokas MC, Largman C (December 1976). "Human carboxypeptidase B. II. Purification of the enzyme from pancreatic tissue and comparison with the enzymes present in pancreatic secretion". Biochimica et Biophysica Acta (BBA) - Enzymology. 452 (2): 468–81. doi: 10.1016/0005-2744(76)90197-2. PMID 1009123.
- ^ Butterworth J, Duncan JJ (September 1979). "Carboxypeptidase B activity of cultured skin fibroblasts and relationship to cystic fibrosis". Clinica Chimica Acta; International Journal of Clinical Chemistry. 97 (1): 39–43. doi: 10.1016/0009-8981(79)90023-8. PMID 40714.
- ^ Wallace EF, Evans CJ, Jurik SM, Mefford IN, Barchas JD (1982). "Carboxypeptidase B activity from adrenal medulla--is it involved in the processing of proenkephalin?". Life Sciences. 31 (16–17): 1793–6. doi: 10.1016/0024-3205(82)90212-0. PMID 6130442.
External links
- The MEROPS online database for peptidases and their inhibitors: M14.003
- Carboxypeptidase+B at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
| carboxypeptidase B1 (tissue) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | CPB1 | ||||||
| NCBI gene | 1360 | ||||||
| HGNC | 2299 | ||||||
| OMIM | 114852 | ||||||
| RefSeq | NM_001871 | ||||||
| UniProt | P15086 | ||||||
| Other data | |||||||
| EC number | 3.4.17.2 | ||||||
| Locus | Chr. 3 q24 | ||||||
| |||||||
| carboxypeptidase B2 (plasma) | |||||||
|---|---|---|---|---|---|---|---|
| Identifiers | |||||||
| Symbol | CPB2 | ||||||
| NCBI gene | 1361 | ||||||
| HGNC | 2300 | ||||||
| OMIM | 603101 | ||||||
| RefSeq | NM_016413 | ||||||
| UniProt | Q96IY4 | ||||||
| Other data | |||||||
| Locus | Chr. 13 q14.11 | ||||||
| |||||||
| carboxypeptidase B | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 3.4.17.2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Carboxypeptidase B ( EC 3.4.17.2, protaminase, pancreatic carboxypeptidase B, tissue carboxypeptidase B, peptidyl-L-lysine [L-arginine]hydrolase) is a carboxypeptidase that preferentially cleaves off basic amino acids arginine and lysine from the C-terminus of a peptide. [1] [2] [3] [4] This enzyme is secreted by the pancreas, and it travels to the small intestine, where it aids in protein digestion. Plasma carboxypeptidase B (carboxypeptidase B2) is responsible for converting the C5a protein into C5a des-Arg, with one less amino acid.
References
- ^ Folk JE (1970). "Carboxypeptidase B (Porcine Pancreas)". Proteolytic Enzymes. Methods Enzymol. Vol. 19. pp. 504–508. doi: 10.1016/0076-6879(70)19036-7. ISBN 9780121818814.
- ^ Brodrick JW, Geokas MC, Largman C (December 1976). "Human carboxypeptidase B. II. Purification of the enzyme from pancreatic tissue and comparison with the enzymes present in pancreatic secretion". Biochimica et Biophysica Acta (BBA) - Enzymology. 452 (2): 468–81. doi: 10.1016/0005-2744(76)90197-2. PMID 1009123.
- ^ Butterworth J, Duncan JJ (September 1979). "Carboxypeptidase B activity of cultured skin fibroblasts and relationship to cystic fibrosis". Clinica Chimica Acta; International Journal of Clinical Chemistry. 97 (1): 39–43. doi: 10.1016/0009-8981(79)90023-8. PMID 40714.
- ^ Wallace EF, Evans CJ, Jurik SM, Mefford IN, Barchas JD (1982). "Carboxypeptidase B activity from adrenal medulla--is it involved in the processing of proenkephalin?". Life Sciences. 31 (16–17): 1793–6. doi: 10.1016/0024-3205(82)90212-0. PMID 6130442.
External links
- The MEROPS online database for peptidases and their inhibitors: M14.003
- Carboxypeptidase+B at the U.S. National Library of Medicine Medical Subject Headings (MeSH)