Q96EB6

SIRT1 also known as SIR2, SIR2L1, SIR2alpha is a member of the sirtuin family. SIRT1 possesses a conserved catalytic core composed of a large Rossmann-fold domain and a smaller zinc-binding domain, interconnected by a flexible linker region that is essential for NAD⁺-dependent deacetylase activity. This structural configuration allows SIRT1 to interact with a variety of substrates, including histones and transcription factors, thereby regulating key cellular processes such as gene expression, DNA repair, metabolism, and aging. The precise structure of SIRT1 is vital for function, as this determines substrate specificity, enzymatic efficiency, and interactions with regulatory proteins, making SIRT1 a pivotal target for studies investigating age-related diseases, cancer, and metabolic disorders.