期刊
ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS
卷 700, 期 -, 页码 -出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.abb.2021.108773
关键词
Acyl-CoA synthetase; Fatty acid metabolism; Structure-function; Electron microscopy; Nanodisc; Enzyme kinetics
资金
- Van Andel Institute
This study characterized the mammalian ACSL1 protein and demonstrated its activity as a monomer through enzymatic assays, mutational analysis, and cryo-electron microscopy.
Fatty acids are essential cellular building blocks and a major energy source. Regardless of their metabolic fate, fatty acids first need to be activated by forming a thioester with a coenzyme A group. This reaction is carried out by acyl-CoA synthetases (ACSs), of which ACSL1 (long-chain acyl-CoA synthetase 1) is an important member. Two bacterial homologues of ACSL1 crystal structures have been solved previously. One is a soluble dimeric protein, and the other is a monomeric peripheral membrane protein. The mammalian ACSL1 is a membrane protein with an N-terminal transmembrane helix. To characterize the mammalian ACSL1, we purified the fulllength mouse ACSL1 and reconstituted it into lipid nanodiscs. Using enzymatic assays, mutational analysis, and cryo-electron microscopy, we show that mouse ACSL1 is active as a monomer.
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