Biology:NMNAT3
Nicotinamide mononucleotide adenylyltransferase 3 (NMNAT3) is an enzyme that in humans is encoded by the NMNAT3 gene.[1] NMNAT3 is the third of three protein isoforms of nicotinamide-nucleotide adenylyltransferase (NMNAT) found in humans.[2] As with the other NMNATs, NMNAT3 is an enzyme that catalyzes nicotinamide adenine dinucleotide (NAD) synthesis.[2] NMNAT3 levels are highest in liver, heart, skeletal muscle, and erythrocytes.[2]
NMNAT3 is localized in mitochondria or cytoplasm, depending upon the cell type.[3][4][5] Knockdown of NMNAT3 gene expression in cell culture strongly reduces mitochondrial function.[4] NMNAT3 is essential for maintaining NAD in red blood cells.[4]
The catechin epigallocatechin gallate found in tea can activate NMNAT3 by more than 40%.[5]
As of 2017 mutations in the NMNAT3 gene have not been associated with any known disease.[2]
References
- ↑ "Molecular cloning, chromosomal localization, tissue mRNA levels, bacterial expression, and enzymatic properties of human NMN adenylyltransferase". J Biol Chem 276 (1): 406–12. Feb 2001. doi:10.1074/jbc.M008700200. PMID 11027696.
- ↑ 2.0 2.1 2.2 2.3 "NMNAT: It's an NAD + Synthase… It's a Chaperone… It's a Neuroprotector". Current Opinion in Genetics & Development 44: 156–162. 2017. doi:10.1016/j.gde.2017.03.014. PMID 28445802.
- ↑ "Location, Location, Location: Compartmentalization of NAD + Synthesis and Functions in Mammalian Cells". Trends in Biochemical Sciences 45 (10): 858–873. 2020. doi:10.1016/j.tibs.2020.05.010. PMID 32595066. PMC 7502477. https://www.jbc.org/content/294/52/19831.long.
- ↑ 4.0 4.1 4.2 "NAD Metabolism: Implications in Aging and Longevity". Ageing Research Reviews 47: 1–17. 2018. doi:10.1016/j.arr.2018.05.006. PMID 29883761.
- ↑ 5.0 5.1 "Therapeutic Potential of NAD-Boosting Molecules: The In Vivo Evidence". Cell Metabolism 27 (3): 529–547. 2018. doi:10.1016/j.cmet.2018.02.011. PMID 29514064.
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