Carboxypeptidase B

carboxypeptidase B2 (plasma)
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
Structures
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Structures	Swiss-model
Domains	InterPro

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Structures	Swiss-model
Domains	InterPro

carboxypeptidase B1 (tissue)
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
Structures
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Structures	Swiss-model
Domains	InterPro

carboxypeptidase B

Identifiers

Databases

PDB structures

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PMC	articles
PubMed	articles
NCBI	proteins

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)

[1] 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.

[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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v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)