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Current Medicinal Chemistry

Editor-in-Chief

ISSN (Print): 0929-8673
ISSN (Online): 1875-533X

Structure and Function of Nicotinamide Mononucleotide Adenylyltransferase

Author(s): G. Magni, A. Amici, M. Emanuelli, G. Orsomando, N. Raffaelli and S. Ruggieri

Volume 11 , Issue 7 , 2004

Page: [873 - 885] Pages: 13

DOI: 10.2174/0929867043455666

Price: $65

Abstract

The enzyme nicotinamide mononucleotide adenylyltransferase (NMNAT), a member of the nucleotidyltransferase α / β phosphodiesterase superfamily, catalyzes the reaction NMN + ATP = NAD + PPi, representing the final step in the biosynthesis of NAD, a molecule playing a fundamental role as a cofactor in cellular redox reactions. NAD also serves as the substrate for reactions involved in important regulatory roles, such as protein covalent modifications, like ADP-ribosylation reactions, as well as Sir2 histone deacetylase, a recently discovered class of enzymes involved in the regulation of gene silencing. This overview describes the most recent findings on NMNATs from bacteria, archaea, yeast, animal and human sources, with detailed consideration of their major kinetic, molecular and structural features. On this regard, the different characteristics exhibited by the enzyme from the various species are highlighted. The possibility that NMNAT may represent an interesting candidate as a target for the rational design of selective chemotherapic agents has been suggested.

Keywords: nad homeostasis, pyridine nucleotides, structure biology, recombinant enzymes


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