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Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A.

Abstract:

Acyl-CoA synthetases belong to the superfamily of adenylate-forming enzymes, and catalyze the two-step activation of fatty acids or carboxylate-containing xenobiotics. The carboxylate substrate first reacts with ATP to form an acyl-adenylate intermediate, which then reacts with CoA to produce an acyl-CoA ester. Here, we report the first crystal structure of a medium-chain acyl-CoA synthetase ACSM2A, in a series of substrate/product/cofactor complexes central to the catalytic mechanism. We obs...

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Publication status:
Published

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Publisher copy:
10.1016/j.jmb.2009.03.064

Authors


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Institution:
University of Oxford
Department:
Oxford, MSD, Clinical Medicine, Structural Genomics Consortium
Oppermann, U More by this author
Journal:
Journal of molecular biology
Volume:
388
Issue:
5
Pages:
997-1008
Publication date:
2009-05-05
DOI:
EISSN:
1089-8638
ISSN:
0022-2836
URN:
uuid:117080c8-c0bb-4b9a-bb06-5f6dc37d836d
Source identifiers:
34675
Local pid:
pubs:34675

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