NMNAT1 Protein, Human (sf9, His)

The NMNAT1 protein assumes a pivotal role in cellular processes as it catalyzes the formation of NAD(+) from nicotinamide mononucleotide (NMN) and ATP. Moreover, it exhibits comparable efficiency in utilizing the deamidated form, nicotinic acid mononucleotide (NaMN), as a substrate and can employ triazofurin monophosphate (TrMP) in the same capacity. Additionally, NMNAT1 catalyzes the reverse reaction, the pyrophosphorolytic cleavage of NAD(+), with a preference for NAD(+) and NaAD as substrates, displaying lesser efficiency in degrading NADH, nicotinic acid adenine dinucleotide phosphate (NHD), and nicotinamide guanine dinucleotide (NGD). Beyond its role in NAD(+) biosynthesis, NMNAT1 is involved in nuclear ATP generation, collaborating with PARP1, PARG, and NUDT5, a process essential for energy-demanding chromatin remodeling events. Furthermore, it serves as a cofactor for glutamate and aspartate ADP-ribosylation, directing PARP1 catalytic activity to histone residues. Notably, NMNAT1's enzymatic activity fails to cleave phosphorylated dinucleotides NADP(+), NADPH, and NaADP(+). Functionally, NMNAT1 plays a crucial role in protecting against axonal degeneration in response to mechanical or toxic insults.