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Dissecting the Roles of the N‐ and C‐Flanking Residues of Acetyllysine Substrates for SIRT1 Activity
Author(s) -
Meledin Roman,
Brik Ashraf,
Aharoni Amir
Publication year - 2013
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.201200727
Subject(s) - chemistry , substrate (aquarium) , substrate specificity , acetylation , biochemistry , enzyme , computational biology , peptide , computer science , combinatorial chemistry , gene , biology , ecology
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.