2.3.1.286	evolution	Phno is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides	757557	
2.3.1.286	evolution	YfiQ is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides	757557	
2.3.1.286	evolution	Yiac is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides	757557	
2.3.1.286	evolution	YjaB is a member of the Gcn5-related N-acetyltransferase (GNAT) family. GNATs acetylate a broad range of substrates, including antibiotics, polyamines, amino acids, nucleotides, tRNAs, proteins, and peptides	757557	
2.3.1.286	malfunction	NAD+-dependent SIRT1 deactivation has a key role on ischemia-reperfusion-induced apoptosis	739745	
2.3.1.286	malfunction	SIRT1 depletion by RNA interference attenuates capsaicin-induced apoptosis in A-549 cancer cells and autophagy in MRC-5 cells	738438	
2.3.1.286	metabolism	acetylation of Lys413 decreases catalysis and SIRT3 reactivates isocitrate dehydrogenase 2 upon deacetylation. SIRT3-dependent deacetylation of isocitrate dehydrogenase 2 suppresses cellular stress by reactive oxygen species (ROS). Acetylation of Lys413 is regulated by SIRT3 in response to calorie and glucose restriction	729982	
2.3.1.286	metabolism	caloric restriction can extend life-span by inducing SIRT1 expression and promoting the long-term survival of irreplaceable cells	730962	
2.3.1.286	metabolism	isoform SIRT3 levels modulate mitochondrial protein folding	738661	
2.3.1.286	metabolism	Sir2 is involved in the regulation of p53 function via deacetylation	729560