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 journalArticle

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 languageEnglish (US)
Pages (from-to)13-17
Number of pages5
JournalApplied Biochemistry and Microbiology
Volume33
Issue number1
StatePublished - Jan 1 1997
Externally publishedYes

ASJC Scopus subject areas

  • Biochemistry
  • Applied Microbiology and Biotechnology

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