Nicotinate-nucleotide adenylyltransferase (NadD)

Nicotinate-nucleotide adenylyltransferase (NadD) is an essential enzyme that catalyzes the transfer of an adenylyl group from ATP to nicotinate mononucleotide (NaMN), producing deamido-NAD+ as a key step in the biosynthesis of NAD+ and NADP+. This enzyme is highly conserved and indispensable for cellular metabolism, and in bacteria such as Mycobacterium tuberculosis, NadD has been validated as a promising target for antibiotic development due to its essentiality and unique mechanistic features relative to human orthologs. Inhibition of this enzyme impairs NAD production, leading to compromised bacterial survival, especially during stress or dormancy. Structural studies have identified unique features that can be exploited for the design of selective inhibitors.

Other names

ATP:nicotinate-ribonucleotide adenylyltransferasedeamido-NAD+ pyrophosphorylasenicotinate mononucleotide adenylyltransferasedeamidonicotinamide adenine dinucleotide pyrophosphorylaseNaMN-ATasenicotinic acid mononucleotide adenylyltransferase

Competitive inhibition (binding to substrate sites and interfering with enzyme catalysis; potential drugs act as inhibitors, blocking NAD biosynthesis)