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

Nat Struct Mol Biol. 2006 Jul;13(7):661-2. doi: 10.1038/nsmb1114. Epub 2006 Jun 18.

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.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Binding Sites
  • Crystallization
  • Cytokines / chemistry*
  • Cytokines / metabolism*
  • Mice
  • Models, Molecular
  • NAD / biosynthesis*
  • Nicotinamide Phosphoribosyltransferase
  • Protein Conformation

Substances

  • Cytokines
  • NAD
  • Nicotinamide Phosphoribosyltransferase
  • nicotinamide phosphoribosyltransferase, mouse

Associated data

  • PDB/2H3B
  • PDB/2H3D