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PMID: 16783373 Published · ppublish English Journal Article Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't

Structure of Nampt/PBEF/visfatin, a mammalian NAD+ biosynthetic enzyme.

Nature structural & molecular biology ·Vol. 13 ·No. 7 ·2006-07-00 ·Pages 661-2

Wang T, Zhang X, Bheda P, Revollo JR, Imai S, Wolberger C

Abstract

Nicotinamide phosphoribosyltransferase (Nampt) synthesizes nicotinamide mononucleotide (NMN) from nicotinamide in a mammalian NAD+ biosynthetic pathway and is required for SirT1 activity in vivo. Nampt has also been presumed to be a cytokine (PBEF) or a hormone (visfatin). The crystal structure of Nampt in the presence and absence of NMN shows that Nampt is a dimeric type II phosphoribosyltransferase and provides insights into the enzymatic mechanism.

MeSH Terms
Animals Binding Sites Crystallization Cytokines/chemistry,metabolism Mice Models, Molecular NAD/biosynthesis Nicotinamide Phosphoribosyltransferase Protein Conformation
Chemicals
Cytokines NAD Nicotinamide Phosphoribosyltransferase nicotinamide phosphoribosyltransferase, mouse
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Wang Tao
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, Maryland 21205, USA.
Zhang Xiangbin
Bheda Poonam
Revollo Javier R
Imai Shin-ichiro
Wolberger Cynthia
Article Info
Journal
Nature structural & molecular biology
Abbr.
Nat Struct Mol Biol
ISSN
1545-9993
Published
2006-07-00
Epub
2006-00-18
Pages
661-2
Language
English
Region
United States
NLM ID
101186374
Subset
IM
Grants
NIDDK NIH HHS · P30 DK056341 · United States
NIDDK NIH HHS · P30 DK056341-06 · United States
NIGMS NIH HHS · Y1-GM-1104 · United States
NCI NIH HHS · Y1-CO-1020 · United States
Databases
PDB
Corrections
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