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Deacetylation Assays to Unravel the Interplay between Sirtuins (SIRT2) and Specific Protein-substrates
Published on: February 27, 2016
Sirtuin chemical mechanisms.
1Department of Pharmacology, Weill Medical College of Cornell University, New York, NY 10065, USA. aas2004@med.cornell.edu
Biochimica Et Biophysica Acta
|February 6, 2010
Summary
Sirtuins are ancient enzymes that utilize NAD(+) to modify proteins and other molecules. This review explores their diverse chemical reactions and mechanisms, including deacetylation and roles in bacterial metabolism.
Area of Science:
- Biochemistry
- Enzymology
- Molecular Biology
Background:
- Sirtuins are evolutionarily conserved proteins found across all domains of life.
- These enzymes universally bind and activate NAD(+) to catalyze various reactions.
- Key sirtuin activity involves NAD(+)-dependent deacetylation of acetylated lysine residues.
Purpose of the Study:
- To provide a comprehensive overview of sirtuin enzymatic chemistries.
- To elucidate the diverse reaction mechanisms employed by sirtuins.
- To highlight the broad biological relevance of sirtuin-catalyzed reactions.
Main Methods:
- Literature review of sirtuin biochemical and mechanistic studies.
- Analysis of known sirtuin substrates and reaction products.
- Survey of different types of ADP-ribosylation reactions catalyzed by sirtuins.
Main Results:
- Sirtuins catalyze multiple forms of ADP-ribosylation beyond deacetylation.
- Observed reactions include protein ADP-ribosylation and NAD(+) solvolysis.
- Specific sirtuin activity involves ADP-ribosyltransfer in cobalamin biosynthesis.
Conclusions:
- Sirtuins exhibit a wider range of chemical activities than previously appreciated.
- Understanding these diverse mechanisms is crucial for deciphering sirtuin functions.
- Sirtuins play fundamental roles in cellular processes and metabolic pathways across life.
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