| Entry |
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| Name |
protein acetyllysine N-acetyltransferase;
Sir2;
protein lysine deacetylase;
NAD+-dependent protein deacetylase
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| Class |
Transferases;
Acyltransferases;
Transferring groups other than aminoacyl groups
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| Sysname |
[protein]-N6-acetyl-L-lysine:NAD+ N-acetyltransferase (NAD+-hydrolysing; 2''-O-acetyl-ADP-D-ribose-forming)
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| Reaction(IUBMB) |
[protein]-N6-acetyl-L-lysine + NAD+ + H2O = [protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose + nicotinamide (overall reaction) [RN: R10634];
(1a) [protein]-N6-acetyl-L-lysine + NAD+ = [protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + nicotinamide;
(1b) [protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine + H2O = [protein]-L-lysine + 2''-O-acetyl-ADP-D-ribose
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| Reaction(KEGG) |
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| Substrate |
[protein]-N6-acetyl-L-lysine [CPD: C20743];
NAD+ [CPD: C00003];
H2O [CPD: C00001];
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine
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| Product |
[protein]-L-lysine [CPD: C02188];
2''-O-acetyl-ADP-D-ribose;
nicotinamide [CPD: C00153];
[protein]-N6-[1,1-(5-adenosylyl-alpha-D-ribose-1,2-di-O-yl)ethyl]-L-lysine
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| Comment |
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.
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| History |
EC 2.3.1.286 created 2019
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| Pathway |
| ec00760 | Nicotinate and nicotinamide metabolism |
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| Orthology |
| K11121 | NAD+-dependent protein deacetylase SIR2 |
| K11411 | NAD+-dependent protein deacetylase sirtuin 1 |
| K11412 | NAD+-dependent protein deacetylase sirtuin 2 |
| K11413 | NAD+-dependent protein deacetylase sirtuin 3 |
| K11414 | NAD+-dependent protein deacetylase sirtuin 4 |
| K11415 | NAD+-dependent protein deacetylase sirtuin 5 |
| K11416 | NAD+-dependent protein deacetylase sirtuin 6 |
| K11417 | NAD+-dependent protein deacetylase sirtuin 7 |
| K12410 | NAD-dependent deacetylase |
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| Genes |
» show all
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| Reference |
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| Authors |
Landry J, Slama JT, Sternglanz R |
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| Title |
Role of NAD(+) in the deacetylase activity of the SIR2-like proteins. |
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| Journal |
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| Reference |
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| Authors |
Sauve AA, Celic I, Avalos J, Deng H, Boeke JD, Schramm VL |
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| Title |
Chemistry of gene silencing: the mechanism of NAD+-dependent deacetylation reactions. |
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| Journal |
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| Reference |
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| Authors |
Min J, Landry J, Sternglanz R, Xu RM |
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| Title |
Crystal structure of a SIR2 homolog-NAD complex. |
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| Journal |
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| Sequence |
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| Reference |
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| Authors |
Jackson MD, Schmidt MT, Oppenheimer NJ, Denu JM |
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| Title |
Mechanism of nicotinamide inhibition and transglycosidation by Sir2 histone/protein deacetylases. |
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| Journal |
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| Reference |
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| Authors |
Sauve AA, Wolberger C, Schramm VL, Boeke JD |
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| Title |
The biochemistry of sirtuins. |
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| Journal |
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| Other DBs |
| ExPASy - ENZYME nomenclature database: | 2.3.1.286 |
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