The sirtuin family of enzymes are able to catalyze the Nε-acyl-lysine deacylation reaction on
histone and non-histone protein substrates. Over the past years since the discovery of its …

The protein acetylation of either the α-amino groups of amino-terminal residues or of internal
lysine or cysteine residues is one of the major posttranslational protein modifications that …

The sirtuin family of intracellular enzymes are able to catalyze a unique β-nicotinamide
adenine dinucleotide (β-NAD+)-dependent N ε-acyl-lysine deacylation reaction on histone …

Acylation of lysine is an important protein modification regulating diverse biological
processes. It was recently demonstrated that members of the human Sirtuin family are …

Since the discovery in 2000 that the yeast sirtuin called “Sir2” catalyzes NAD+ dependent
histone deacetylation, a wave of research has focused on evaluating the biochemical and …

Protein lysine posttranslational modification by an increasing number of different acyl groups
is becoming appreciated as a regulatory mechanism in cellular biology. Sirtuins are class III …

Sirtuins are a family of NAD+-dependent protein deacetylases widely distributed in all phyla
of life. Accumulating evidence indicates that sirtuins are important regulators of organism life …

Sirtuins are NAD-dependent deacylases. Previous studies have established two important
enzymatic intermediates in sirtuin-catalyzed deacylation, an alkylamidate intermediate I …

The β-NAD+-dependent N ε-acyl-lysine deacylation reaction catalyzed by sirtuin family
members has been increasingly demonstrated to be important in regulating multiple crucial …

Sirtuins are NAD+-dependent enzymes universally present in all organisms, where they play
central roles in regulating numerous biological processes. Although early studies showed …