Class of enzymes
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 |
---|
Search for |
---|
Structures | Swiss-model |
---|
Domains | InterPro |
---|
|
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 |
---|
Search for |
---|
Structures | Swiss-model |
---|
Domains | InterPro |
---|
|
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)
|
---|
Activity | |
---|
Regulation | |
---|
Classification | |
---|
Kinetics | |
---|
Types | |
---|
- Biology portal