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Crystal structure and mechanistic implications of N2-(2-carboxyethyl)arginine synthase, the first enzyme in the clavulanic acid biosynthesis pathway.

Abstract:

The initial step in the biosynthesis of the clinically important beta-lactamase inhibitor clavulanic acid involves condensation of two primary metabolites, D-glyceraldehyde 3-phosphate and L-arginine, to give N2-(2-carboxyethyl)arginine, a beta-amino acid. This unusual N-C bond forming reaction is catalyzed by the thiamin diphosphate (ThP2)-dependent enzyme N2-(2-carboxyethyl)arginine synthase. Here we report the crystal structure of N2-(2-carboxyethyl)arginine synthase, complexed with ThP2 a...

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Publication status:
Published

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Publisher copy:
10.1074/jbc.m310803200

Authors


Caines, ME More by this author
Elkins, JM More by this author
Hewitson, KS More by this author
More by this author
Institution:
University of Oxford
Department:
Oxford, MPLS, Chemistry, Organic Chemistry
Journal:
The Journal of biological chemistry
Volume:
279
Issue:
7
Pages:
5685-5692
Publication date:
2004-02-05
DOI:
EISSN:
1083-351X
ISSN:
0021-9258
URN:
uuid:aae7ac78-1891-4b32-b36d-544ec6e05b88
Source identifiers:
32540
Local pid:
pubs:32540

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