A novel enzyme catalyzes the synthesis of activation factor from ATP and D-fructose-6-P.

E. Furuya, K. Uyeda

Research output: Contribution to journalArticle

45 Scopus citations

Abstract

We have recently discovered an activator for phosphofructokinase termed "activation factor" (Furuya, E., and Uyeda, K. (1980) Proc. Natl. Acad. Sci. U. S. A. 77, 5861-5864). In this paper, we investigated the enzyme responsible for its synthesis. We have found an enzyme from rat liver which catalyzes the formation of activation factor from fructose-6-P and ATP-Mg and it has been identified as fructose-2,6-P2. Fructose-1,6-P2, fructose-1-P, or fructose does not serve as a substrate. This enzyme has been partially purified and shown to be different from phosphofructokinase. Several lines of evidence indicate that the in vitro synthetic product is identical with chemically synthesized fructose-2,6-P2: (a) it is active in our assay for activation factor which is based on counteraction of ATP inhibition of phosphofructokinase; (b) it is acid labile as is fructose-2,6-P2; and (c) it shows the same mobility as synthetic fructose-2,6-P2 upon paper chromatography and the acid hydrolysis product has been identified as fructose-6-P. Thus, this new enzyme catalyzes the synthesis of the activation factor from fructose-6-P and ATP-Mg.

Original languageEnglish (US)
Pages (from-to)7109-7112
Number of pages4
JournalJournal of Biological Chemistry
Volume256
Issue number14
StatePublished - Jul 25 1981

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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