Ontology highlight
ABSTRACT:
SUBMITTER: Hallows WC
PROVIDER: S-EPMC3101115 | biostudies-literature | 2011 Jan
REPOSITORIES: biostudies-literature
Hallows William C WC Yu Wei W Smith Brian C BC Devries Mark K MK Ellinger James J JJ Someya Shinichi S Shortreed Michael R MR Prolla Tomas T Markley John L JL Smith Lloyd M LM Zhao Shimin S Guan Kun-Liang KL Denu John M JM
Molecular cell 20110101 2
Emerging evidence suggests that protein acetylation is a broad-ranging regulatory mechanism. Here we utilize acetyl-peptide arrays and metabolomic analyses to identify substrates of mitochondrial deacetylase Sirt3. We identified ornithine transcarbamoylase (OTC) from the urea cycle, and enzymes involved in β-oxidation. Metabolomic analyses of fasted mice lacking Sirt3 (sirt3(-/-)) revealed alterations in β-oxidation and the urea cycle. Biochemical analysis demonstrated that Sirt3 directly deacet ...[more]