Nicotinate phosphoribosyltransferase

In enzymology, a nicotinate phosphoribosyltransferase is an enzyme that catalyzes the chemical reaction


 * nicotinate + 5-phospho-α- D -ribose 1-diphosphate + ATP + H2O $$\rightleftharpoons$$ nicotinate D -ribonucleotide + diphosphate + ADP + phosphate

Thus, the four substrates of this enzyme are nicotinate, 5-phospho-alpha-D-ribose 1-diphosphate, ATP, and H2O, whereas its four products are nicotinate D-ribonucleotide, diphosphate, ADP, and phosphate.

This enzyme belongs to the family of ligases, specifically those forming generic carbon-nitrogen bonds. The systematic name of this enzyme class is 5-phospho-alpha-D-ribose 1-diphosphate:nicotinate ligase (ADP, diphosphate-forming) .

Structural studies
As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes, , , , , , and.