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In enzymology, a nicotinate phosphoribosyltransferase () is an enzyme that catalyzes the chemical reaction :nicotinate + 5-phospho-alpha-D-ribose 1-diphosphate + ATP + H2O 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) . Other names in common use include niacin ribonucleotidase, nicotinic acid mononucleotide glycohydrolase, nicotinic acid mononucleotide pyrophosphorylase, and nicotinic acid phosphoribosyltransferase. This enzyme participates in nicotinate and nicotinamide metabolism. ==Structural studies== As of late 2007, 7 structures have been solved for this class of enzymes, with PDB accession codes , , , , , , and . 抄文引用元・出典: フリー百科事典『 ウィキペディア（Wikipedia）』 ■ウィキペディアで「Nicotinate phosphoribosyltransferase」の詳細全文を読む スポンサード リンク
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