Abstract
Sirtuins are ancient proteins widely distributed in all lifeforms of earth. These proteins are universally able to bind NAD(+), and activate it to effect ADP-ribosylation of cellular nucleophiles. The most commonly observed sirtuin reaction is the ADP-ribosylation of acetyllysine, which leads to NAD(+)-dependent deacetylation. Other types of ADP-ribosylation have also been observed, including protein ADP-ribosylation, NAD(+) solvolysis and ADP-ribosyltransfer to 5,6-dimethylbenzimidazole, a reaction involved in eubacterial cobalamin biosynthesis. This review broadly surveys the chemistries and chemical mechanisms of these enzymes.
Copyright 2010 Elsevier B.V. All rights reserved.
Publication types
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Research Support, N.I.H., Extramural
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Research Support, Non-U.S. Gov't
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Review
MeSH terms
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Acetylation
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Adenosine Diphosphate Ribose / metabolism
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Animals
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Benzimidazoles / metabolism
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Humans
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Imidoesters / metabolism
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Lysine / analogs & derivatives
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Lysine / metabolism
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Models, Biological
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Molecular Structure
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NAD / metabolism
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Niacinamide / metabolism
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Niacinamide / pharmacology
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Plasmodium falciparum / metabolism
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Saccharomyces cerevisiae / drug effects
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Saccharomyces cerevisiae / metabolism
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Sirtuins / antagonists & inhibitors
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Sirtuins / chemistry
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Sirtuins / metabolism*
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Trypanosoma brucei brucei / metabolism
Substances
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Benzimidazoles
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Imidoesters
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NAD
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N(alpha)-acetyllysine
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Adenosine Diphosphate Ribose
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Niacinamide
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5,6-dimethylbenzimidazole
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Sirtuins
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Lysine