The Enzyme Database

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EC 2.3.1.286     
Accepted name: protein acetyllysine N-acetyltransferase
Reaction: [protein]-N6-acetyl-L-lysine + NAD+ + H2O = [protein]-L-lysine + 2′′-O-acetyl-ADP-D-ribose + nicotinamide (overall reaction)
(1a) [protein]-N6-acetyl-L-lysine + NAD+ = [protein]-N6-[1,1-(5-adenosylyl-α-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide
(1b) [protein]-N6-[1,1-(5-adenosylyl-α-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O = [protein]-L-lysine + 2′′-O-acetyl-ADP-D-ribose
Other name(s): Sir2; protein lysine deacetylase; NAD+-dependent protein deacetylase
Systematic name: [protein]-N6-acetyl-L-lysine:NAD+ N-acetyltransferase (NAD+-hydrolysing; 2′′-O-acetyl-ADP-D-ribose-forming)
Comments: The enzyme, found in all domains of life, is involved in gene regulation by deacetylating proteins. Some of the 2′′-O-acetyl-ADP-D-ribose converts non-enzymically to 3′′-O-acetyl-ADP-D-ribose.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc
References:
1.  Landry, J., Slama, J.T. and Sternglanz, R. Role of NAD+ in the deacetylase activity of the SIR2-like proteins. Biochem. Biophys. Res. Commun. 278 (2000) 685–690. [PMID: 11095969]
2.  Sauve, A.A., Celic, I., Avalos, J., Deng, H., Boeke, J.D. and Schramm, V.L. Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions. Biochemistry 40 (2001) 15456–15463. [PMID: 11747420]
3.  Min, J., Landry, J., Sternglanz, R. and Xu, R.M. Crystal structure of a SIR2 homolog-NAD complex. Cell 105 (2001) 269–279. [PMID: 11336676]
4.  Jackson, M.D., Schmidt, M.T., Oppenheimer, N.J. and Denu, J.M. Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. J. Biol. Chem. 278 (2003) 50985–50998. [PMID: 14522996]
5.  Sauve, A.A., Wolberger, C., Schramm, V.L. and Boeke, J.D. The biochemistry of sirtuins. Annu. Rev. Biochem. 75 (2006) 435–465. [PMID: 16756498]
[EC 2.3.1.286 created 2019]
 
 


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