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

  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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