PubMed:16788062 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PubMed/sourceid/16788062","sourcedb":"PubMed","sourceid":"16788062","source_url":"http://www.ncbi.nlm.nih.gov/pubmed/16788062","text":"Reversible lysine acetylation controls the activity of the mitochondrial enzyme acetyl-CoA synthetase 2.\nWe 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.","tracks":[{"project":"LocText","denotations":[{"id":"T1","span":{"begin":59,"end":72},"obj":"go:GO:0005739"},{"id":"T2","span":{"begin":80,"end":103},"obj":"uniprot:Q9NUB1"},{"id":"T3","span":{"begin":120,"end":125},"obj":"taxonomy:9606"},{"id":"T4","span":{"begin":126,"end":149},"obj":"uniprot:Q9NUB1"},{"id":"T5","span":{"begin":151,"end":157},"obj":"uniprot:Q9NUB1"},{"id":"T6","span":{"begin":164,"end":184},"obj":"go:GO:0005759"},{"id":"T7","span":{"begin":194,"end":200},"obj":"uniprot:Q9NUB1"},{"id":"T8","span":{"begin":275,"end":288},"obj":"go:GO:0005739"},{"id":"T9","span":{"begin":297,"end":302},"obj":"uniprot:Q9NTG7"},{"id":"T10","span":{"begin":318,"end":324},"obj":"uniprot:Q9NUB1"},{"id":"T11","span":{"begin":394,"end":400},"obj":"uniprot:Q9NUB1"},{"id":"T12","span":{"begin":404,"end":409},"obj":"uniprot:Q9NTG7"},{"id":"T13","span":{"begin":458,"end":464},"obj":"uniprot:Q9NUB1"},{"id":"T14","span":{"begin":531,"end":536},"obj":"uniprot:Q9NTG7"},{"id":"T15","span":{"begin":725,"end":731},"obj":"uniprot:Q9NUB1"},{"id":"T16","span":{"begin":740,"end":743},"obj":"uniprot:uniprot:"},{"id":"T17","span":{"begin":904,"end":910},"obj":"taxonomy:9606"}],"relations":[{"id":"R1","pred":"localizeTo","subj":"T2","obj":"T1"},{"id":"R2","pred":"localizeTo","subj":"T4","obj":"T6"},{"id":"R3","pred":"localizeTo","subj":"T5","obj":"T6"},{"id":"R4","pred":"localizeTo","subj":"T9","obj":"T8"}],"namespaces":[{"prefix":"uniprot","uri":"http://identifiers.org/uniprot/"},{"prefix":"taxonomy","uri":"http://identifiers.org/taxonomy/"},{"prefix":"go","uri":"http://identifiers.org/go/"}],"attributes":[{"subj":"T1","pred":"source","obj":"LocText"},{"subj":"T2","pred":"source","obj":"LocText"},{"subj":"T3","pred":"source","obj":"LocText"},{"subj":"T4","pred":"source","obj":"LocText"},{"subj":"T5","pred":"source","obj":"LocText"},{"subj":"T6","pred":"source","obj":"LocText"},{"subj":"T7","pred":"source","obj":"LocText"},{"subj":"T8","pred":"source","obj":"LocText"},{"subj":"T9","pred":"source","obj":"LocText"},{"subj":"T10","pred":"source","obj":"LocText"},{"subj":"T11","pred":"source","obj":"LocText"},{"subj":"T12","pred":"source","obj":"LocText"},{"subj":"T13","pred":"source","obj":"LocText"},{"subj":"T14","pred":"source","obj":"LocText"},{"subj":"T15","pred":"source","obj":"LocText"},{"subj":"T16","pred":"source","obj":"LocText"},{"subj":"T17","pred":"source","obj":"LocText"}]},{"project":"PubmedHPO","denotations":[{"id":"T1","span":{"begin":164,"end":177},"obj":"HP_0001427"},{"id":"T2","span":{"begin":275,"end":288},"obj":"HP_0001427"}],"attributes":[{"subj":"T1","pred":"source","obj":"PubmedHPO"},{"subj":"T2","pred":"source","obj":"PubmedHPO"}]}],"config":{"attribute types":[{"pred":"source","value type":"selection","values":[{"id":"LocText","color":"#eceb93","default":true},{"id":"PubmedHPO","color":"#d193ec"}]}]}}