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Carboxypeptidase B

Class of enzymes

Summary

Class of enzymes

Carboxypeptidase B (, 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. 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

(1970). "Proteolytic Enzymes".
(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.
(September 1979). "Carboxypeptidase B activity of cultured skin fibroblasts and relationship to cystic fibrosis". Clinica Chimica Acta; International Journal of Clinical Chemistry.
(1982). "Carboxypeptidase B activity from adrenal medulla--is it involved in the processing of proenkephalin?". Life Sciences.

Wikipedia Source

This article was imported from Wikipedia and is available under the Creative Commons Attribution-ShareAlike 4.0 License. Content has been adapted to SurfDoc format. Original contributors can be found on the article history page.

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