Carboxypeptidase B

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.

carboxypeptidase B1 (tissue)
Identifiers
SymbolCPB1
NCBI gene1360
HGNC2299
OMIM114852
RefSeqNM_001871
UniProtP15086
Other data
EC number3.4.17.2
LocusChr. 3 q24
carboxypeptidase B2 (plasma)
Identifiers
SymbolCPB2
NCBI gene1361
HGNC2300
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

References
  1. Folk JE (1970). "Carboxypeptidase B (porcine pancreas)". Methods Enzymol. 19: 504–508. doi:10.1016/0076-6879(70)19036-7.
  2. 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.
  3. 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.
  4. 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.
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