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• W2016017656 abstract "Sirtuins are nicotinamide adenine dinucleotide (NAD+)-dependent deacetylases that catalyze the deacetylation of proteins such as histones and p53. A sensitive and convenient fluorometric assay for evaluating the SIRT1 enzymatic activity was developed here. Specifically, the remaining NAD+ after the deacetylation was determined by converting NAD+ to a highly fluorescent cyclized α-adduct compound. By this assay, we found that nicotinamide, Cu2+, and Zn2+ antagonize the activity of SIRT1. Resveratrol stimulates the enzymatic activity specifically with 7-amino-4-methylcoumarin (AMC)-labeled acetylated peptide. Epigallocatechin galate (EGCG) inhibits SIRT1 activity with both AMC-labeled and unlabeled peptide. However, a combination of vitamin C with EGCG can reverse the inhibition of EGCG with the unlabeled peptide or stimulate the deacetylation of AMC-labeled peptide by SIRT1. The assay does not require any isotopic material and thus is biologically safe. It can be adapted to a 96-well microplate for high-throughput screening. Notably, the acetylated peptides with or without fluorescent labels may be used in the assay, which facilitates the substrate specificity study of SIRT1 activators or inhibitors in vitro." @default.
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• W2016017656 date "2009-12-01" @default.
• W2016017656 modified "2023-09-24" @default.
• W2016017656 title "A fluorometric assay of SIRT1 deacetylation activity through quantification of nicotinamide adenine dinucleotide" @default.
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• W2016017656 doi "https://doi.org/10.1016/j.ab.2009.08.011" @default.
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