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

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

doi:10.1038/nsmb1114

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

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

School of Medicine

Research output: Contribution to journal › Article › peer-review

193 Scopus citations

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.

Original language	English (US)
Pages (from-to)	661-662
Number of pages	2
Journal	Nature Structural and Molecular Biology
Volume	13
Issue number	7
DOIs	https://doi.org/10.1038/nsmb1114
State	Published - Jul 2006

ASJC Scopus subject areas

Structural Biology
Molecular Biology

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

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.",

author = "Tao Wang and Xiangbin Zhang and Poonam Bheda and Revollo, {Javier R.} and Imai, {Shin Ichiro} and Cynthia Wolberger",

note = "Funding Information: We thank the staff at GM/CA-CAT at the Advanced Photon Source, which is funded in part by the US National Cancer Institute (Y1-CO-1020) and the US National Institute of General Medical Sciences (Y1-GM-1104). J.R.R. is a fellow supported by the Lucille P. Markey Special Emphasis Pathway in Human Pathology. S.I. is an Ellison Medical Foundation Scholar in Aging.",

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T1 - Structure of Nampt/PBEF/visfatin, a mammalian NAD+ biosynthetic enzyme

AU - Wang, Tao

AU - Zhang, Xiangbin

AU - Bheda, Poonam

AU - Revollo, Javier R.

AU - Imai, Shin Ichiro

AU - Wolberger, Cynthia

N1 - Funding Information: We thank the staff at GM/CA-CAT at the Advanced Photon Source, which is funded in part by the US National Cancer Institute (Y1-CO-1020) and the US National Institute of General Medical Sciences (Y1-GM-1104). J.R.R. is a fellow supported by the Lucille P. Markey Special Emphasis Pathway in Human Pathology. S.I. is an Ellison Medical Foundation Scholar in Aging.

PY - 2006/7

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N2 - 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.

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

Abstract

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