Carboxypeptidase B

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carboxypeptidase B1 (tissue)
Identifiers
SymbolCPB1
Entrez1360
HUGO2299
OMIM114852
RefSeqNM_001871
UniProtP15086
Other data
EC number3.4.17.2
LocusChr. 3 q24
carboxypeptidase B2 (plasma)
Identifiers
SymbolCPB2
Entrez1361
HUGO2300
OMIM603101
RefSeqNM_016413
UniProtQ96IY4
Other data
LocusChr. 13 q14.11
carboxypeptidase B
Identifiers
EC number3.4.17.2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / 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 acts upon basic amino acids, such as arginine and lysine.[1][2][3][4] This serum enzyme is also responsible for rapidly metabolizing the C5a protein into C5a des-Arg, with one less amino acid.

References

  1. Folk, J.E. (1970). "Carboxypeptidase B (porcine pancreas)". Methods Enzymol. 19: 504–508. doi:10.1016/0076-6879(70)19036-7.
  2. Brodrick, J.W.; Geokas, M.C.; Largman, C. (1976). "Human carboxypeptidase B. II. Purification of the enzyme from pancreatic tissue and comparison with the enzymes present in pancreatic secretion". Biochim. Biophys. Acta. 452: 468–481. doi:10.1016/0005-2744(76)90197-2. PMID 1009123.
  3. Butterworth, J.; Duncan, J.J. (1979). "Carboxypeptidase B activity of cultured skin fibroblasts and relationship to cystic fibrosis". Clin. Chim. Acta. 97: 39–43. doi:10.1016/0009-8981(79)90023-8. PMID 40714.
  4. Wallace, E.F.; Evans, C.J.; Jurik, S.M.; Mefford, I.N.; Barchas, J.D. (1982). "Carboxypeptidase B activity from adrenal medulla. Is it involved in the processing of proenkephalin?". Life Sci. 31: 1793–1796. doi:10.1016/0024-3205(82)90212-0. PMID 6130442.

External links