Sirtuin
Silent information regulator 2 (Sir2) proteins, also known as sirtuins, are a family of nicotine adenine dinucleotide (NAD) dependent protein deacetylases in organisms ranging from bacteria to humans that are characterized by the presence of a unique and highly conserved catalytic domain of approximately 260 amino acids. Sirtuins are divided into 5 classes, including Class I (subclasses Ia, Ib and Ic), Class II, Class III, Class IV (subclasses IVa and IVb) and Class U (Gram-positive bacteria specific). The catalytic domain of sirtuins is comprised of two bilobed globular domains, the large domain containing the NAD-binding pocket and the small domain binding the acetyl-lysine substrate.
- A8242 SplitomicinSummary: inhibitor of Sir2p and fMLP-induced free radicals
- A8302 Tenovin-6Target: Sir2-like Family Deacetylases (Sirtuins)Summary: SIRT inhibitor and p53 activator
- A8567 Tenovin-3Summary: p53 activator
- B3272 InauhzinTarget: Sir2-like Family Deacetylases (Sirtuins)Summary: SIRT1 inhibitor
- B5971 Triacetyl ResveratrolSummary: Cell-permeable resveratrol prodrug
- B6063 SIRT1/2 Inhibitor IVSummary: SIRT1 and SIRT2 inhibitor
- B4713 AK-7Summary: selective and brain-permeable SIRT2 inhibitor
- B7323 AGK 2Summary: SIRT2 inhibitor, potent and selective
- B7594 SalermideSummary: SIRT1 and SIRT2 inhibitor
- A4180 SRT1720 HCl3 CitationTarget: Sir2-like Family Deacetylases (Sirtuins)Summary: SIRT1 activator