Reference - Detail
| RRC ID | 3296 |
|---|---|
| Author | Schwer B, Bunkenborg J, Verdin RO, Andersen JS, Verdin E. |
| Title | Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2. |
| Journal | Proc Natl Acad Sci U S A |
| 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. |
| Volume | 103(27) |
| Pages | 10224-10229 |
| Published | 2006-7-5 |
| DOI | 10.1073/pnas.0603968103 |
| PII | 0603968103 |
| PMID | 16788062 |
| PMC | PMC1502439 |
| MeSH | Acetate-CoA Ligase / chemistry Acetate-CoA Ligase / genetics Acetate-CoA Ligase / metabolism* Acetylation Amino Acid Sequence Animals Binding Sites Cell Line Chlorocebus aethiops Conserved Sequence Humans Lysine / genetics Lysine / metabolism* Mitochondria / enzymology* Mitochondrial Proteins / genetics Mitochondrial Proteins / metabolism Molecular Sequence Data Sequence Alignment Sirtuin 3 Sirtuins / genetics Sirtuins / metabolism |
| IF | 9.412 |
| Times Cited | 499 |
| WOS Category | BIOCHEMISTRY & MOLECULAR BIOLOGY |
| Resource | |
| Prokaryotes E. coli | JW1106 |