Cellular and Molecular Life Sciences CMLS

, Volume 62, Issue 19, pp 2161–2172

The catalytic triad of serine peptidases

Review

DOI: 10.1007/s00018-005-5160-x

Cite this article as:
Polgár, L. Cell. Mol. Life Sci. (2005) 62: 2161. doi:10.1007/s00018-005-5160-x

Abstract.

The catalytic action of serine peptidases depends on the interplay of a nucleophile, a general base and an acid. In the classic trypsin and subtilisin families this catalytic triad is composed of serine, histidine and aspartic acid residues and exhibits similar spatial arrangements, but the order of the residues in the amino acid sequence is different. By now several new families have been discovered, in which the nucleophile-base-acid pattern is generally conserved, but the individual components can vary. The variations illustrate how different groups and different protein structures achieve the same reaction.

Key words.

Mechanisms of peptidase actionβ-lactamasecytomegalovirusNtp-hydrolysesoxyanion binding site

Copyright information

© Birkhäuser Verlag, Basel 2005

Authors and Affiliations

  1. 1.Institute of Enzymology, Biological Research CenterHungarian Academy of SciencesBudapest 112Hungary