Open Access
The NMN/NaMN adenylyltransferase (NMNAT) protein family
Corinna Lau1,Marc Niere1,Mathias Ziegler1
Department of Molecular Biology, University of Bergen, Thormohlensgate 55, N-5008 Bergen, Norway
DOI: 10.2741/3252 Volume 14 Issue 2, pp.410-431
Published: 01 January 2009
(This article belongs to the Special Issue ADP-riboseNAD metabolism)

NAD biosynthesis has become of considerable interest owing to the important signaling functions of the pyridine nucleotides which have been recognized over the past years. The formation of the dinucleotides from ATP and the mononucleotide of niacin (either nicotinamide or nicotinic acid) constitute the critical step in NAD generation which is catalyzed by NMN/NaMN adenylyltransferases, NMNATs. Recent research has established the molecular, catalytic and structural properties of NMNATs from many organisms. Detailed studies, particularly of the human NMNATs, have revealed distinct isoform-specific characteristics relating to enzyme kinetics and substrate specificity, oligomeric assembly as well as subcellular and tissue distribution. Moreover, direct functional relationships between NMNATs and major NAD-mediated signaling processes have been discovered suggesting that at least some of these proteins might play more than just an enzymatic role. Several investigations have also pointed to a critical role of NMNATs in pathological states such as cancer and neurodegeneration. This article intends to provide a comprehensive overview of the family of NMNATs and highlights some of the recently identified functional roles of these enzymes.

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Corinna Lau, Marc Niere, Mathias Ziegler. The NMN/NaMN adenylyltransferase (NMNAT) protein family. Frontiers in Bioscience-Landmark. 2009. 14(2); 410-431.