Regulation of nicotinate phosphoribosyltransferase in Brevibacterium ammoniagenes ATCC 6872

N. G. Dul'yaninova; E. M. Podlepa; V. P. Radina; V. Zh Tsyrenov; V. Ya Bykhovskii

Regulation of nicotinate phosphoribosyltransferase in Brevibacterium ammoniagenes ATCC 6872

N. G. Dul'yaninova, E. M. Podlepa, V. P. Radina, V. Zh Tsyrenov, V. Ya Bykhovskii

Research output: Contribution to journal › Article › peer-review

Abstract

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)
Pages (from-to)	13-17
Number of pages	5
Journal	Applied Biochemistry and Microbiology
Volume	33
Issue number	1
State	Published - Jan 1 1997
Externally published	Yes

ASJC Scopus subject areas

Biochemistry
Applied Microbiology and Biotechnology

Cite this

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abstract = "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.",

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AU - Dul'yaninova, N. G.

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AU - Radina, V. P.

AU - Tsyrenov, V. Zh

AU - Bykhovskii, V. Ya

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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, 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.

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, 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.

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Regulation of nicotinate phosphoribosyltransferase in Brevibacterium ammoniagenes ATCC 6872

Abstract

ASJC Scopus subject areas

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