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- Title
The catalytic triad of serine peptidases.
- Authors
Polgár, L
- 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.
- Publication
Cellular and molecular life sciences : CMLS, 2005, Vol 62, Issue 19-20, p2161
- ISSN
1420-682X
- Publication type
Journal Article
- DOI
10.1007/s00018-005-5160-x