Purification and Characterization of Pyrophosphate-Dependent Phosphofructokinase from Phosphate-Starved Brassica nigra Suspension Cells
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چکیده
منابع مشابه
Purification and Characterization of Pyrophosphate- Dependent Phosphofructokinase from Phosphate-Starved Brassica nigra Suspension CeIIs’
Previously, we reported that inorganic phosphate (Pi) deprivation of Brassica nigra suspension cells or seedlings leads to a progressive increase in the a$-subunit ratio of the inorganic pyrophosphate (PPibdependent phosphofructokinase (PFP) and that this coincides with a marked enhancement in the enzyme’s activity and sensitivity to i ts allosteric activator, fructose-2,6-bisphosphate (Fru-2,6...
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When Brassica nigra leaf petiole suspension cells were subjected to 7 days of inorganic phosphate (Pi) starvation the extractable activity of: (a) pyrophosphate:fructose 6-phosphate 1-phosphotransferase, nonphosphorylating NADP-glyceraldehyde 3-phosphate dehydrogenase, phosphoenolpyruvate phosphatase, and phosphoenolpyruvate carboxylase increased at least fivefold, (b) phosphorylating NAD-glyce...
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A pyrophosphate-dependent phosphofructokinase (pyrophosphate; D-fructose-6-phosphate-1-phosphotransferase) has been purified and characterized from extracts of Propionibacterium shermanii. The enzyme catalyzes the transfer of phosphate from pyrophosphate to fructose 6-phosphate to yield fructose-1,6-P2 and phosphate. This unique enzymatic activity was observed initially in Entamoeba histolytica...
متن کاملPurification and Characterization of Pyrophosphate-
Previously, we reported that inorganic phosphate (Pi) deprivation of Brassica nigra suspension cells or seedlings leads to a progressive increase in the a$-subunit ratio of the inorganic pyrophosphate (PPibdependent phosphofructokinase (PFP) and that this coincides with a marked enhancement in the enzyme’s activity and sensitivity to i ts allosteric activator, fructose-2,6-bisphosphate (Fru-2,6...
متن کاملPurification and Characterization of Phosphofructokinase from Rhodotorui~ Glutinis
Abstract: Fhosphofructokinase has been identified and purified from extracts of Rhodotorula glutinlus. Kinetic studies of the enzyme indicated high eooperativity with respect to fructose 6-phosphate. The kinetics for ATP shows no cooperativity as indicated by the hyperbolic behavior of the enzyme. The enzyme is inhibited by ADF. Citrate and phosphate have no effect on the enzyme activity. The r...
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ژورنال
عنوان ژورنال: Plant Physiology
سال: 1996
ISSN: 1532-2548,0032-0889
DOI: 10.1104/pp.112.1.343