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Structural analyses on intermediates in serine protease catalysis.

Abstract:

Although the subject of many studies, detailed structural information on aspects of the catalytic cycle of serine proteases is lacking. Crystallographic analyses were performed in which an acyl-enzyme complex, formed from elastase and a peptide, was reacted with a series of nucleophilic dipeptides. Multiple analyses led to electron density maps consistent with the formation of a tetrahedral species. In certain cases, apparent peptide bond formation at the active site was observed, and the ele...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m600495200

Authors


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Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Wilmouth, RC More by this author
Journal:
The Journal of biological chemistry
Volume:
281
Issue:
33
Pages:
24024-24035
Publication date:
2006-08-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:132f70bf-77a7-4812-8225-db5e9eb05cbf
Source identifiers:
40101
Local pid:
pubs:40101

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