TY - JOUR
T1 - Regulation of Nicotinate Phosphoribosyltransferase in Brevibacterium ammoniagenes ATCC 6872
AU - Dul'yaninova, N. G.
AU - Podlepa, E. M.
AU - Radina, V. P.
AU - Tsyrenov, V. Zh
AU - Bykhovskii, V. Ya
PY - 1997/12/1
Y1 - 1997/12/1
N2 - 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.
AB - 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.
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M3 - Article
AN - SCOPUS:0345910559
SN - 0555-1099
VL - 33
SP - 22
EP - 23
JO - Prikladnaya Biokhimiya i Mikrobiologiya
JF - Prikladnaya Biokhimiya i Mikrobiologiya
IS - 1
ER -