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, and NADP did not affect the enzyme activity. CTP, ITP, GTP, and UTP could substitute for 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||5|
|Journal||Applied Biochemistry and Microbiology|
|State||Published - Jan 1 1997|
ASJC Scopus subject areas
- Applied Microbiology and Biotechnology