Document Detail


The catalytic triad of serine peptidases.
MedLine Citation:
PMID:  16003488     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
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.
Authors:
L Polgár
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Publication Detail:
Type:  Journal Article; Research Support, Non-U.S. Gov't; Review    
Journal Detail:
Title:  Cellular and molecular life sciences : CMLS     Volume:  62     ISSN:  1420-682X     ISO Abbreviation:  Cell. Mol. Life Sci.     Publication Date:  2005 Oct 
Date Detail:
Created Date:  2005-10-19     Completed Date:  2005-12-14     Revised Date:  2007-08-13    
Medline Journal Info:
Nlm Unique ID:  9705402     Medline TA:  Cell Mol Life Sci     Country:  Switzerland    
Other Details:
Languages:  eng     Pagination:  2161-72     Citation Subset:  IM    
Affiliation:
Institute of Enzymology, Biological Research Center, Hungarian Academy of Sciences, P.O. Box 7, 1518, Budapest 112, Hungary. polgar@enzim.hu
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MeSH Terms
Descriptor/Qualifier:
Amino Acids / chemistry,  genetics
Animals
Anions / chemistry
Binding Sites
Catalysis
Protein Conformation
Protein Engineering
Serine Endopeptidases / chemistry*,  classification*,  genetics
Grant Support
ID/Acronym/Agency:
//Wellcome Trust
Chemical
Reg. No./Substance:
0/Amino Acids; 0/Anions; EC 3.4.21.-/Serine Endopeptidases

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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