Carboxypeptidases


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Related to Carboxypeptidases: Carboxypeptidase B

Carboxypeptidases

 

an enzyme group of the hydrolase class (carboxypeptidase-A, carboxypeptidase-B, and yeast car-boxypeptidase) that catalyze the stepped hydrolysis of polypeptides from the C-end, that is, from the amino acid that contains a free carboxyl group (—COOH). The molecular weight of car-boxypeptidases exceeds 34, 000. Carboxypeptidase-A is most active on aromatic amino acids; carboxypeptidase-B, on lysine or arginene; and yeast carboxypeptidase, on glycine or lysine. In addition, carboxypeptidases have esterase activity (the ability to split ether bonds). Carboxypeptidase-A enters the duodenum from the pancreas where it is produced in the form of inactive procarboxypeptidase-A, which becomes carboxypeptidase-A, primarily under the influence of trypsin.

REFERENCES

Dixon, M., and E. Webb. Fermenty. Moscow, 1966. (Translated from English.)
Mosolov, V. V. Proteoliticheskie fermenty. Moscow, 1971.
References in periodicals archive ?
Aspartic protease, [beta]-galactosidase, peroxidase and serine carboxypeptidase were detected in three Ephedra species.
Furthermore, amidation of the C-terminus is not sufficient to suppress any carboxypeptidase activity (28).
A number of enzymes, including [Beta]-lactamases, carboxypeptidases, and squalene epoxidase, are under current study to develop inhibitors which may be useful medicinal agents and to gain insights into mechanisms of catalysis.
Many preformed mediators are involved in an anaphylactic reaction, including histamine, tryptase, chymase, mast cell carboxypeptidases, platelet activating factor and others.
Other enzymes which can transform mycotoxins include proteases, carboxypeptidases, and lactonohydrolyases (EFSA, 2009).
Carboxypeptidases from A to Z: implications in embryonic development and Wnt binding.
Families of overlapping peptides have been observed in many studies, suggesting the release of peptides from larger parent proteins by endoproteolytic cleavage followed by variable trimming of released peptides by aminopeptidases and carboxypeptidases (70, 74-79).
The proteolytic processing of peptides in the circulation by amino- and carboxypeptidases is well known, and it should not be surprising that the identified molecules represent modified and/or truncated forms of C3a.
A kinetic spectrophotometric method for the determination of basic carboxypeptidases was described using furyl-acrolyl peptides (42).
Basic carboxypeptidases are a group of enzymes that cleave a single basic amino acid, lysine or arginine, from the COOH terminus of peptides and proteins.