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Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2.


ABSTRACT: We report that human acetyl-CoA synthetase 2 (AceCS2) is a mitochondrial matrix protein. AceCS2 is reversibly acetylated at Lys-642 in the active site of the enzyme. The mitochondrial sirtuin SIRT3 interacts with AceCS2 and deacetylates Lys-642 both in vitro and in vivo. Deacetylation of AceCS2 by SIRT3 activates the acetyl-CoA synthetase activity of AceCS2. This report identifies the first acetylated substrate protein of SIRT3. Our findings show that a mammalian sirtuin directly controls the activity of a metabolic enzyme by means of reversible lysine acetylation. Because the activity of a bacterial ortholog of AceCS2, called ACS, is controlled via deacetylation by a bacterial sirtuin protein, our observation highlights the conservation of a metabolic regulatory pathway from bacteria to humans.

SUBMITTER: Schwer B 

PROVIDER: S-EPMC1502439 | biostudies-literature | 2006 Jul

REPOSITORIES: biostudies-literature

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Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2.

Schwer Bjoern B   Bunkenborg Jakob J   Verdin Regis O RO   Andersen Jens S JS   Verdin Eric E  

Proceedings of the National Academy of Sciences of the United States of America 20060620 27


We report that human acetyl-CoA synthetase 2 (AceCS2) is a mitochondrial matrix protein. AceCS2 is reversibly acetylated at Lys-642 in the active site of the enzyme. The mitochondrial sirtuin SIRT3 interacts with AceCS2 and deacetylates Lys-642 both in vitro and in vivo. Deacetylation of AceCS2 by SIRT3 activates the acetyl-CoA synthetase activity of AceCS2. This report identifies the first acetylated substrate protein of SIRT3. Our findings show that a mammalian sirtuin directly controls the ac  ...[more]

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