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pubmed-article:16663839pubmed:abstractTextThe participation of pyrophosphate-dependent phosphofructokinase (PPi-PFK) in plant glycolysis was examined using extracts from pea seeds (Pisum sativum L. cv Alaska). Glycolysis starting with fructose 6-phosphate was measured under aerobic conditions as the accumulation of pyruvate. Pyruvate accumulated in a medium containing PPi and adenosine diphosphate at about two-thirds of the rate in a medium containing adenosine diphosphate and adenosine triphosphate (ATP). The PPi-dependent pyruvate accumulation had the same reactant requirements and sensitivity to glycolysis inhibitors, sodium fluoride, and iodoacetamide, as the well-established ATP-dependent glycolysis. Added fructose 2,6-bisphosphate stimulated both the PPi-dependent pyruvate accumulation and PPi-PFK activity whereas this modulator had no effect on ATP-dependent glycolysis or ATP-PFK. Collectively these results demonstrate a PPi-dependent glycolytic pathway in plants which is responsive to fructose 2,6-bisphosphate.lld:pubmed
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pubmed-article:16663839pubmed:issn0032-0889lld:pubmed
pubmed-article:16663839pubmed:authorpubmed-author:SmithT ATAlld:pubmed
pubmed-article:16663839pubmed:authorpubmed-author:WuM XMXlld:pubmed
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pubmed-article:16663839pubmed:pagination316-20lld:pubmed
pubmed-article:16663839pubmed:dateRevised2010-9-15lld:pubmed
pubmed-article:16663839pubmed:year1984lld:pubmed
pubmed-article:16663839pubmed:articleTitlePyrophosphate and fructose 2,6-bisphosphate effects on glycolysis in pea seed extracts.lld:pubmed
pubmed-article:16663839pubmed:affiliationBiochemistry Department, University of Georgia, Athens, Georgia 30602.lld:pubmed
pubmed-article:16663839pubmed:publicationTypeJournal Articlelld:pubmed
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