Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme |
| |
Authors: | Rong Grace Zhai Menico Rizzi Silvia Garavaglia |
| |
Institution: | (1) Department of Molecular and Cellular Pharmacology, Neuroscience Center, Miller School of Medicine, University of Miami, Miami, FL 33136, USA;(2) DiSCAFF, University of Piemonte Orientale “A. Avogadro”, Via Bovio, 6, 28100 Novara, Italy |
| |
Abstract: | Nicotinamide/nicotinic acid mononucleotide adenylyltransferase (NMNAT) has long been known as the master enzyme in NAD biosynthesis
in living organisms. A burst of investigations on NMNAT, going beyond enzymology, have paralleled increasing discoveries of
key roles played by NAD homeostasis in a number or patho-physiological conditions. The availability of in-depth kinetics and
structural enzymology analyses carried out on NMNATs from different organisms offer a powerful tool for uncovering fascinating
evolutionary relationships. On the other hand, additional functions featuring NMNAT have emerged from investigations aimed
at unraveling the molecular mechanisms responsible for complex biological phenomena such as neurodegeneration. NMNAT appears
to be a multifunctional protein that sits both at the core of central metabolism and at a crossroads of multiple cellular
processes. The resultant wealth of biochemical data has built a robust framework upon which design of NMNAT activators, inhibitors
or enzyme variants of potential medical interest can be based. |
| |
Keywords: | (5– 8) NAD Crystal structures Oligomeric assembly Neuroprotection Enzyme Chimerical proteins Protein– protein interaction |
本文献已被 SpringerLink 等数据库收录! |
|