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Carboxypeptidases

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Proteases New Perspectives

Part of the book series: MCBU Molecular and Cell Biology Updates ((MCBU))

Abstract

Carboxypeptidases catalyze the hydrolysis of peptide bonds at the C-terminus of peptides and proteins. This hydrolysis may be a step in the degradation of some substrate molecules or may result in the maturation of others. As for every type of protease, the physiological effect of the hydrolytic action is thus varied and also site- and organism-dependent. Moreover, the car-boxypeptidase action may be carried out by at least two different kinds of enzymes with different catalytic mechanisms. In one case, metallocarboxypeptidases possess a tightly bound Zn2+ atom which is directly involved in catalysis; on the other hand, the serine-carboxypeptidases contain an active Ser residue at the active centre which belongs to the Ser/His/Asp triad characteristic of serine proteinases.

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  1. Departament de Bioquímica i Biologia Molecular, Facultat de Ciències, and Institut de Biologia Fonamental, Universitat Autònoma de Barcelona, E-08193, Bellaterra, Spain

    Josep Vendrell & Francesc X. Avilés

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  1. Josep Vendrell
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  1. Jozef Stefan Institute, Jamova 39, 1000, Ljubljana, Slovenia

    Vito Turk

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Vendrell, J., Avilés, F.X. (1999). Carboxypeptidases. In: Turk, V. (eds) Proteases New Perspectives. MCBU Molecular and Cell Biology Updates. Birkhäuser, Basel. https://doi.org/10.1007/978-3-0348-8737-3_2

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  • DOI: https://doi.org/10.1007/978-3-0348-8737-3_2

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