Sirtuin 3 (SIRT3) Antibody – Rabbit Polyclonal

This gene encodes a member of the sirtuin family of proteins, homologs to the yeast Sir2 protein. Members of the sirtuin family are characterized by a sirtuin core domain and grouped into four classes. The functions of human sirtuins have not yet been determined; however, yeast sirtuin proteins are known to regulate epigenetic gene silencing and suppress recombination of rDNA. Studies suggest that the human sirtuins may function as intracellular regulatory proteins with mono-ADP-ribosyltransferase activity. The protein encoded by this gene is included in class I of the sirtuin family. Two alternatively spliced transcript variants that encode different proteins have been described for this gene. [provided by RefSeq, Jul 2008]

SIRT3: a soluble mitochondrial NAD-dependent protein deacetylase. Can deacetylate and thereby activate a central metabolic regulator in the mitochondrial matrix, glutamate dehydrogenase. Mitochondrial proteins are hyperacetylated in SIRT3-deficient mice, but not in SIRT4 or SIRT5 deficient mice. SIRT3-deficient mice have no obvious metabolic phenotype, and the process of adaptive thermogenesis is normal. Can deacetylate and activate isocitrate dehydrogenase 2, an enzyme that participates in regulation of the citric acid cycle and the regeneration of antioxidants. Inhibited by nicotinamide, but not by trichostatin A. Its unprocessed form is enzymatically inactive. It is processed by mitochondrial processing peptidase (MPP) in the mitochondrial matrix to give an enzymatically active 28 kDa product.

Protein type: Deacetylase; EC 3.5.1.-; Mitochondrial

Chromosomal Location of Human Ortholog: 11p15.5

Cellular Component: mitochondrial matrix; mitochondrion

Molecular Function: enzyme binding; NAD+ ADP-ribosyltransferase activity; NAD-dependent histone deacetylase activity; protein binding; zinc ion binding

Biological Process: aerobic respiration; aging; histone deacetylation; mitochondrion organization; positive regulation of insulin secretion; protein ADP-ribosylation; protein deacetylation