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Nicotinate phosphoribosyltransferase

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

nicotinate + 5-phospho-α-<small>D</small>-ribose 1-diphosphate + ATP + H<sub>2</sub>O nicotinate <small>D</small>-ribonucleotide + diphosphate + ADP + phosphate

Thus, the four substrates of this enzyme are nicotinate, 5-phospho-alpha-D-ribose 1-diphosphate, ATP, and H<sub>2</sub>O, 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 .

References