Nicotinamide-nucleotide adenylyltransferase
In enzymology, a nicotinamide-nucleotide adenylyltransferase (EC 2.7.7.1) is an enzyme that catalyzes the chemical reaction
- ATP + nicotinamide ribonucleotide diphosphate + NAD+
Thus, the two substrates of this enzyme are ATP and nicotinamide ribonucleotide, whereas its two products are diphosphate and NAD+.
This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing nucleotide groups (nucleotidyltransferases). The systematic name of this enzyme class is ATP:nicotinamide-nucleotide adenylyltransferase. Other names in common use include NAD+ pyrophosphorylase, adenosine triphosphate-nicotinamide mononucleotide transadenylase, ATP:NMN adenylyltransferase, diphosphopyridine nucleotide pyrophosphorylase, nicotinamide adenine dinucleotide pyrophosphorylase, nicotinamide mononucleotide adenylyltransferase, and NMN adenylyltransferase. This enzyme participates in nicotinate and nicotinamide metabolism. The human version of this protein is NMNAT1.
Structural studies
As of late 2007, 11 structures have been solved for this class of enzymes, with PDB accession codes 1EJ2, 1GZU, 1HYB, 1KKU, 1KQN, 1KQO, 1KR2, 1M8F, 1M8G, 1M8J, and 1M8K.
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