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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
Peer review status:
Peer reviewed

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Publisher copy:
10.1016/j.jmb.2009.03.064

Authors


Kochan, Grazyna More by this author
Pilka, Ewa S More by this author
von Delft, Frank More by this author
Oppermann, Udo More by this author
Yue, Wyatt W More by this author
Publisher:
Elsevier Publisher's website
Journal:
Journal of Molecular Biology Journal website
Volume:
388
Issue:
5
Pages:
997-1008
Publication date:
2009
DOI:
ISSN:
1089-8638
URN:
uuid:0927071c-c511-4392-9055-67f0160a031c
Local pid:
SGC:19345228

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