Structure of Nampt/PBEF/visfatin, a mammalian NAD+ biosynthetic enzyme.
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.
Wang
Tao
T
Department of Biophysics and Biophysical Chemistry, Johns Hopkins University School of Medicine, 725 N. Wolfe St., Baltimore, Maryland 21205, USA.
Zhang
Xiangbin
X
Bheda
Poonam
P
Revollo
Javier R
JR
Imai
Shin-ichiro
S
Wolberger
Cynthia
C
D000818:Animals; D001665:Binding Sites; D003460:Crystallization; D016207:Cytokines / Q000737:chemistry* / Q000378:metabolism*; D051379:Mice; D008958:Models, Molecular; D009243:NAD / Q000096:biosynthesis*; D054409:Nicotinamide Phosphoribosyltransferase; D011487:Protein Conformation
D016207:Cytokines; D009243:NAD; D054409:Nicotinamide Phosphoribosyltransferase; C495867:nicotinamide phosphoribosyltransferase, mouse