4.5 Article

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

Journal

NATURE STRUCTURAL & MOLECULAR BIOLOGY
Volume 13, Issue 7, Pages 661-662

Publisher

NATURE PUBLISHING GROUP
DOI: 10.1038/nsmb1114

Keywords

-

Funding

  1. NCI NIH HHS [Y1-CO-1020] Funding Source: Medline
  2. NIDDK NIH HHS [P30 DK056341-06, P30 DK056341] Funding Source: Medline
  3. NIGMS NIH HHS [Y1-GM-1104] Funding Source: Medline

Ask authors/readers for more resources

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.

Authors

I am an author on this paper
Click your name to claim this paper and add it to your profile.

Reviews

Primary Rating

4.5
Not enough ratings

Secondary Ratings

Novelty
-
Significance
-
Scientific rigor
-
Rate this paper

Recommended

No Data Available
No Data Available