Abstract:
:Two molecular forms of pyrophosphate-dependent phosphofructokinase (PP(i)-PFK; pyrophosphate:D-fructose-6-phosphate 1-phosphotransferase; EC 2.7.1.90) have been found whose activity depends upon association and dissociation characteristics regulated by fructose 2,6-bisphosphate (Fru-2,6-P(2)). PP(i)-PFK was purified 200-fold from cotyledons of germinating pea seeds and found to exist in two interconvertible molecular forms. The two forms of PP(i)-PFK have sedimentation coefficients of 6.3 and 12.7 S during ultracentrifugation in sucrose density gradients and also differ both in sensitivity to the activator Fru-2,6-P(2) and in affinity for the substrate fructose 6-phosphate. The major component of enzyme activity is in the large form (12.7 S), but the small, less-active, form (6.3 S) predominates when the enzyme preparation is extracted and stored in buffer without Fru-2,6-P(2) and glycerol. Urea (1 M) or pyrophosphate (20 mM) treatment results in at least a 50% loss of activity in the glycolytic direction, whereas these treatments had much less influence on the gluconeogenic direction activity. Concomitant with the loss of glycolytic activity the enzyme dissociates into the small form. Fru-2,6-P(2) stabilizes the large form of the enzyme against the dissociating effects of pyrophosphate and prevents the inactivation in the glycolytic direction during either urea or pyrophosphate treatment. The small molecular form of the enzyme is converted into the large form in the presence of Fru-2,6-P(2). We propose that glycolytic and gluconeogenic hexose metabolism in plants includes a regulatory mechanism induced by Fru-2,6-P(2) that involves the interconversion of two molecular forms of PP(i)-PFK.
journal_name
Proc Natl Acad Sci U S Aauthors
Wu MX,Smyth DA,Black CCdoi
10.1073/pnas.81.16.5051subject
Has Abstractpub_date
1984-08-01 00:00:00pages
5051-5issue
16eissn
0027-8424issn
1091-6490journal_volume
81pub_type
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