Ontology highlight
ABSTRACT:
SUBMITTER: Forwood JK
PROVIDER: S-EPMC1965522 | biostudies-literature | 2007 Jun
REPOSITORIES: biostudies-literature
Forwood Jade K JK Thakur Anil S AS Guncar Gregor G Marfori Mary M Mouradov Dmitri D Meng Weining W Robinson Jodie J Huber Thomas T Kellie Stuart S Martin Jennifer L JL Hume David A DA Kobe Bostjan B
Proceedings of the National Academy of Sciences of the United States of America 20070611 25
Acyl-CoA thioesterases (Acots) catalyze the hydrolysis of fatty acyl-CoA to free fatty acid and CoA and thereby regulate lipid metabolism and cellular signaling. We present a comprehensive structural and functional characterization of mouse acyl-CoA thioesterase 7 (Acot7). Whereas prokaryotic homologues possess a single thioesterase domain, mammalian Acot7 contains a pair of domains in tandem. We determined the crystal structures of both the N- and C-terminal domains of the mouse enzyme, and inf ...[more]