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

Tao Wang, Xiangbin Zhang, Poonam Bheda, Javier R. Revollo, Shin Ichiro Imai, Cynthia Wolberger

Research output: Contribution to journalArticle


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.

Original languageEnglish (US)
Pages (from-to)661-662
Number of pages2
JournalNature Structural and Molecular Biology
Issue number7
StatePublished - Jul 1 2006

ASJC Scopus subject areas

  • Structural Biology
  • Molecular Biology

Fingerprint Dive into the research topics of 'Structure of Nampt/PBEF/visfatin, a mammalian NAD<sup>+</sup> biosynthetic enzyme'. Together they form a unique fingerprint.

  • Cite this