title: Dissecting the roles of the N- and C-flanking residues of acetyllysine substrates for SIRT1 activity.
abstract: SIRT1 specificity: The multispecific SIRT1 enzyme catalyzes the deacetylation of acetyllysine residues within protein targets. However, little is known regarding the molecular basis for SIRT1 substrate recognition. Kinetic analysis of SIRT1 with a panel of peptide substrates shows the high importance of the region N-flanking the target acetyllysine and its high conservation through evolution.
authors: Department of Life Sciences and the National Institute for Biotechnology in the Negev (NIBN), Ben-Gurion University of the Negev, Be'er Sheva 84105, Israel.
authors: Roman
authors: R
authors: Meledin
authors: Ashraf
authors: A
authors: Brik
authors: Amir
authors: A
authors: Aharoni
mesh_terms: D000595:Amino Acid Sequence; D003598:Cytoskeletal Proteins / Q000737:chemistry; D007700:Kinetics; D008239:Lysine / Q000737:chemistry*; D008969:Molecular Sequence Data; D010455:Peptides / Q000737:chemistry / Q000378:metabolism; D017434:Protein Structure, Tertiary; D056564:Sirtuin 1 / Q000737:chemistry / Q000378:metabolism*; D013379:Substrate Specificity; D016159:Tumor Suppressor Protein p53 / Q000737:chemistry
chemical_list: C088832:CCDC6 protein, human; D003598:Cytoskeletal Proteins; D010455:Peptides; D016159:Tumor Suppressor Protein p53; D056564:Sirtuin 1; D008239:Lysine