Nicotinamide/nicotinic acid mononucleotide adenylyltransferase, new insights into an ancient enzyme

被引:84
作者
Zhai, Rong Grace [1 ]
Rizzi, Menico [2 ]
Garavaglia, Silvia [2 ]
机构
[1] Univ Miami, Miller Sch Med, Dept Mol & Cellular Pharmacol, Ctr Neurosci, Miami, FL 33136 USA
[2] Univ Piemonte Orientale, DiSCAFF, I-28100 Novara, Italy
关键词
(5-8) NAD; Crystal structures; Oligomeric assembly; Neuroprotection; Enzyme; Chemerical proteins; Protein-protein interaction; WALLERIAN DEGENERATION WLD(S); HUMAN NMN ADENYLYLTRANSFERASE; BIFUNCTIONAL NADR REGULATOR; DELAYS AXONAL DEGENERATION; CRYSTAL-STRUCTURE; ESCHERICHIA-COLI; HAEMOPHILUS-INFLUENZAE; SALMONELLA-TYPHIMURIUM; NMN/NAMN ADENYLYLTRANSFERASE; SACCHAROMYCES-CEREVISIAE;
D O I
10.1007/s00018-009-0047-x
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
070307 [化学生物学]; 071010 [生物化学与分子生物学];
摘要
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.
引用
收藏
页码:2805 / 2818
页数:14
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