Nicotinamide mononucleotide adenylyltransferase (NMNAT)

Nicotinamide mononucleotide adenylyltransferase (NMNAT) is a family of highly conserved enzymes that catalyze the formation of nicotinamide adenine dinucleotide (NAD) from nicotinamide mononucleotide (NMN) and ATP, a key step in NAD biosynthesis pathways in all living organisms[2][4]. NMNAT exists in multiple isoforms, such as NMNAT1 (nuclear), NMNAT2 (cytoplasmic, especially in neurons), and NMNAT3 (mitochondrial). These enzymes are critical for maintaining cellular NAD levels, supporting energy metabolism, DNA repair, and cell survival. Mutations in NMNAT1 are linked to Leber’s congenital amaurosis (LCA9), a form of inherited retinal degeneration[1]. NMNAT activity also confers neuroprotection, and pharmacological modulation is investigated for cancer, neurodegenerative diseases, and metabolic disorders[2][5]. Drugs like EGCG have been found to enhance NMNAT2 activity[3]. NMNATs are considered important therapeutic targets due to their central metabolic roles and involvement in pathophysiological conditions.

Other names

NMNAT1NMNAT2NMNAT3nicotinamide-nucleotide adenylyltransferasenicotinate-nucleotide adenylyltransferaseNaMN adenylyltransferasePNAT1LCA9SHILCA

Enzyme inhibition, Enzyme activation, modulation of NAD+ synthesis, neuroprotection