Spinach leaf 6-phosphofructo-2-kinase. Isolation of a new enzyme form that undergoes ATP-dependent modification

Griffin H. Walker, Steven C. Huber

Research output: Contribution to journalArticle

Abstract

A novel form of 6-phosphofructo-2-kinase was partially purified from spinach (Spinacia oleracea L.) leaves. As isolated, the new enzyme form possessed little or no enzymatic activity. However, pretreatment with 2 mM Mg-ATP dramatically increased the activities of 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase. Activation only occurred in the presence of magnesium plus ATP; either alone was ineffective. The ATP activation was reversed by treatment with alkaline phosphatase and could be completely restored by subsequent incubation with Mg-ATP. Thus, protein phosphorylation appears to be the mechanism involved. This is the first evidence that higher plants contain an interconvertible form of the enzyme.

Original languageEnglish (US)
Pages (from-to)375-380
Number of pages6
JournalFEBS Letters
Volume213
Issue number2
DOIs
StatePublished - Mar 23 1987

Keywords

  • (Spinacia oleracea L.)
  • 6-phosphofructo-2-kinase
  • Fructose-2,6-bisphosphatase
  • P ATP
  • Regulation

ASJC Scopus subject areas

  • Biophysics
  • Structural Biology
  • Biochemistry
  • Molecular Biology
  • Genetics
  • Cell Biology

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