Ontology highlight
ABSTRACT:
SUBMITTER: Bharathi SS
PROVIDER: S-EPMC3837126 | biostudies-literature | 2013 Nov
REPOSITORIES: biostudies-literature
Bharathi Sivakama S SS Zhang Yuxun Y Mohsen Al-Walid AW Uppala Radha R Balasubramani Manimalha M Schreiber Emanuel E Uechi Guy G Beck Megan E ME Rardin Matthew J MJ Vockley Jerry J Verdin Eric E Gibson Bradford W BW Hirschey Matthew D MD Goetzman Eric S ES
The Journal of biological chemistry 20131011 47
Long-chain acyl-CoA dehydrogenase (LCAD) is a key mitochondrial fatty acid oxidation enzyme. We previously demonstrated increased LCAD lysine acetylation in SIRT3 knockout mice concomitant with reduced LCAD activity and reduced fatty acid oxidation. To study the effects of acetylation on LCAD and determine sirtuin 3 (SIRT3) target sites, we chemically acetylated recombinant LCAD. Acetylation impeded substrate binding and reduced catalytic efficiency. Deacetylation with recombinant SIRT3 partiall ...[more]