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

@article{Wang2006StructureON,
  title={Structure of Nampt/PBEF/visfatin, a mammalian NAD+ biosynthetic enzyme},
  author={Tao Wang and Xiangbin Zhang and Poonam Bheda and Javier R. Revollo and Shin‐ichiro Imai and Cynthia Wolberger},
  journal={Nature Structural \&Molecular Biology},
  year={2006},
  volume={13},
  pages={661-662}
}
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. 
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Nicotinamide Phosphoribosyltransferase Inhibitors
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TLDR
This review discusses the importance of different salvage pathways involved in metabolising the vitamin B3 class of NAD+ precursor molecules, with a particular focus on the recently identified nicotinamide riboside kinase (NRK) pathway at both a tissue-specific and systemic level. Expand
Nicotinamide phosphoribosyltransferase purification using SUMO expression system.
TLDR
Successful NAMPT expression using the pET-SUMO expression vector in E. coli strain SHuffle containing a hexa-His tag for purification is reported and NamPT solubilization in n-dodecyl-β-d-maltopyranoside (DDM) detergent in monomeric form is reported, thus enhancing the opportunity for further structural and functional investigations. Expand
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