Nicotinate phosphoribosyltransferase from Brevibacterium ammoniagenes ATCC 6872 (500-fold purification) was inhibited by the reaction products (nicotinic acid mononucleotide, pyrophosphate and ADP). Deamido NAD and NAD also had inhibitory effects. Nicotinamide, nicotinamide mononucleotide adenine, adenosine, polyadenylic acid, adenosine 5′-tetraphosphate, ribose 5-phosphate, nucleoside monophosphates, flavin mononucleotide, flavin adenine dinucleotide, or NADP did not affect the enzyme activity. CTP, ITP, GTP, and UTP could substitute ATP in this reaction. However, the affinity of the enzyme for the above-listed nucleoside triphosphates was lower than the affinity for ATP.
|Original language||English (US)|
|Number of pages||2|
|Journal||Prikladnaya Biokhimiya i Mikrobiologiya|
|State||Published - Dec 1 1997|
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