Document Detail


Nicotinamide riboside and nicotinic acid riboside salvage in fungi and mammals. Quantitative basis for Urh1 and purine nucleoside phosphorylase function in NAD+ metabolism.
MedLine Citation:
PMID:  19001417     Owner:  NLM     Status:  MEDLINE    
Abstract/OtherAbstract:
NAD+ is a co-enzyme for hydride transfer enzymes and an essential substrate of ADP-ribose transfer enzymes and sirtuins, the type III protein lysine deacetylases related to yeast Sir2. Supplementation of yeast cells with nicotinamide riboside extends replicative lifespan and increases Sir2-dependent gene silencing by virtue of increasing net NAD+ synthesis. Nicotinamide riboside elevates NAD+ levels via the nicotinamide riboside kinase pathway and by a pathway initiated by splitting the nucleoside into a nicotinamide base followed by nicotinamide salvage. Genetic evidence has established that uridine hydrolase, purine nucleoside phosphorylase, and methylthioadenosine phosphorylase are required for Nrk-independent utilization of nicotinamide riboside in yeast. Here we show that mammalian purine nucleoside phosphorylase but not methylthioadenosine phosphorylase is responsible for mammalian nicotinamide riboside kinase-independent nicotinamide riboside utilization. We demonstrate that so-called uridine hydrolase is 100-fold more active as a nicotinamide riboside hydrolase than as a uridine hydrolase and that uridine hydrolase and mammalian purine nucleoside phosphorylase cleave nicotinic acid riboside, whereas the yeast phosphorylase has little activity on nicotinic acid riboside. Finally, we show that yeast nicotinic acid riboside utilization largely depends on uridine hydrolase and nicotinamide riboside kinase and that nicotinic acid riboside bioavailability is increased by ester modification.
Authors:
Peter Belenky; Kathryn C Christensen; Francesca Gazzaniga; Alexandre A Pletnev; Charles Brenner
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Publication Detail:
Type:  Journal Article; Research Support, N.I.H., Extramural; Research Support, Non-U.S. Gov't; Research Support, U.S. Gov't, Non-P.H.S.     Date:  2008-11-11
Journal Detail:
Title:  The Journal of biological chemistry     Volume:  284     ISSN:  0021-9258     ISO Abbreviation:  J. Biol. Chem.     Publication Date:  2009 Jan 
Date Detail:
Created Date:  2008-12-29     Completed Date:  2009-02-24     Revised Date:  2013-08-06    
Medline Journal Info:
Nlm Unique ID:  2985121R     Medline TA:  J Biol Chem     Country:  United States    
Other Details:
Languages:  eng     Pagination:  158-64     Citation Subset:  IM    
Affiliation:
Department of Genetics and Biochemistry, Dartmouth Medical School, Lebanon, New Hampshire 03756, USA.
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MeSH Terms
Descriptor/Qualifier:
Histone Deacetylases / genetics,  metabolism
Humans
NAD / genetics,  metabolism*
Niacinamide / genetics,  metabolism*
Phosphotransferases (Alcohol Group Acceptor) / genetics,  metabolism*
Purine-Nucleoside Phosphorylase / genetics,  metabolism*
Saccharomyces cerevisiae / genetics,  metabolism*
Silent Information Regulator Proteins, Saccharomyces cerevisiae / genetics,  metabolism
Sirtuin 2
Sirtuins / genetics,  metabolism
Grant Support
ID/Acronym/Agency:
T32 GM008704/GM/NIGMS NIH HHS; T32GM008704/GM/NIGMS NIH HHS
Chemical
Reg. No./Substance:
0/Silent Information Regulator Proteins, Saccharomyces cerevisiae; 53-84-9/NAD; 98-92-0/Niacinamide; EC 2.4.2.1/Purine-Nucleoside Phosphorylase; EC 2.4.2.28/5'-methylthioadenosine phosphorylase; EC 2.7.1.-/Phosphotransferases (Alcohol Group Acceptor); EC 2.7.1.-/nicotinamide riboside kinase; EC 3.5.1.-/SIR2 protein, S cerevisiae; EC 3.5.1.-/Sirtuin 2; EC 3.5.1.-/Sirtuins; EC 3.5.1.98/Histone Deacetylases
Comments/Corrections
Erratum In:
J Biol Chem. 2009 Mar 20;284(12):8208

From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine


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