- 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...
Expand abstract - Publication status:
- Published
- Peer review status:
- Peer reviewed
- Publisher copy:
- 10.1016/j.jmb.2009.03.064
-
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- 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
- Language:
- English
- Subjects:
- Copyright holder:
- Wellcome Trust and Elsevier Ltd
- Copyright date:
- 2009
- Notes:
- Copyright © 2009 Elsevier Ltd.
Journal article
Structural snapshots for the conformation-dependent catalysis by human medium-chain acyl-coenzyme A synthetase ACSM2A
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