EC Number |
General Information |
Reference |
---|
2.3.1.286 | metabolism |
SIRT1 modulates DNA repair activity, which can be regulated by the acetylation status of repair protein Ku70 following DNA damage |
729683 |
2.3.1.286 | metabolism |
the deacetylation of [histone H4]-N6-acetyl-L-lysine16 by Sirt2 may be pivotal to the formation of condensed chromatin |
729802 |
2.3.1.286 | metabolism |
the enzyme can regulate flux and anapleurosis of this central metabolic cycle |
730205 |
2.3.1.286 | more |
the enzyme's key residues are F138, N119, D82, and A83. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism |
757557 |
2.3.1.286 | more |
the enzyme's key residues are Y115, E103, R69, and F70. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism |
757557 |
2.3.1.286 | more |
the enzyme's key residues are Y117, N105, H72, and N73. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism |
757557 |
2.3.1.286 | more |
the enzyme's key residues are Y128, S116, E78, and I79. Sequence and structural comparison of Escherichia coli KAT proteins and their key catalytic residues, structure homology modelling, overview. Acetyltransferases acetylate their substrates using a general acid/base chemical mechanism |
757557 |
2.3.1.286 | physiological function |
acetylation of heat shock protein 10 by isoform SIRT3 enhances medium-chain acyl-CoA dehydrogenase folding, enzyme activity, and fat oxidation |
738661 |
2.3.1.286 | physiological function |
enzyme expression is crucial for the survival of the cell |
737969 |
2.3.1.286 | physiological function |
heterochromatin assembly requires the SIR proteins Sir3, the primary structural component of SIR heterochromatin, and the Sir2-4 complex, responsible for the targeted recruitment of SIR proteins and the deacetylation of lysine 16 of histone H4 |
752056 |