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Structure and function of nicotinamide mononucleotide adenylyltransferase
G Magni1, A Amici, M Emanuelli
1Istituto di Biotecnologie Biochimiche, Università Politecnica delle Marche, Ancona, Italy. magnig@univpm.it
Current Medicinal Chemistry
|April 14, 2004
Summary
Nicotinamide mononucleotide adenylyltransferases (NMNATs) catalyze the final step in NAD biosynthesis. This review highlights NMNAT features across species and their potential as drug targets.
Area of Science:
- Biochemistry
- Molecular Biology
- Enzymology
Background:
- Nicotinamide mononucleotide adenylyltransferase (NMNAT) is crucial for NAD biosynthesis, a vital cofactor in cellular redox and regulatory processes.
- NAD is essential for ADP-ribosylation and Sir2 histone deacetylase activity, impacting gene silencing.
Purpose of the Study:
- To provide an overview of recent findings on NMNATs from diverse species.
- To detail the kinetic, molecular, and structural characteristics of NMNATs.
- To highlight interspecies variations in NMNAT features.
Main Methods:
- Literature review of NMNAT research.
- Comparative analysis of NMNAT properties across bacteria, archaea, yeast, and animals.
- Focus on kinetic, molecular, and structural data.
Main Results:
- NMNATs exhibit diverse characteristics across different species.
- Detailed kinetic, molecular, and structural features of NMNATs are presented.
- Interspecies variations in NMNAT properties are highlighted.
Conclusions:
- NMNATs are key enzymes with diverse features across the tree of life.
- Understanding NMNATs' structure-function relationships is crucial.
- NMNATs represent potential targets for chemotherapeutic agent development.