Islet fructose 6-phosphate, 2-kinase:Fructose 2,6-bisphosphatase: Isozymic form, expression, and characterization

Toshiharu Sakurai, John H. Johnson, Kosaku Uyeda

Research output: Contribution to journalArticle

13 Scopus citations

Abstract

Polymerase chain reaction analysis of the mRNA isolated from rat islets demonstrated that the major isozyme of Fructose 6-P,2-kinase:Fructose 2,6-bisphosphatase was the heart type enzyme, and that the liver type enzyme was not detectable. The islet enzyme was expressed in Escherichia coli and purified to homogeneity. The islet enzyme showed the highest Fructose 6-P,2-kinase activity (478 milliunits/mg) compared to the other isozymes and Fructose 2,6-Pase activity (39 milliunits/mg). Fructose 6-P,2-kinase showed KmF6P = 17 μM, which is within the range of in vivo Fru 6-P concentrations in islets. 6-P-Gluconate was a potent inhibitor of Fructose 2,6-Pase. The data suggest that Fructose 6-P,2-kinase activity of the bifunctional enzyme was high and Fructose 2,6-Pase activity was inhibited under physiological variations of blood glucose concentration.

Original languageEnglish (US)
Pages (from-to)159-163
Number of pages5
JournalBiochemical and Biophysical Research Communications
Volume218
Issue number1
DOIs
StatePublished - Jan 5 1996

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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