Direct evidence that pyrophosphate: Fructose‐6‐phosphate phosphotransferase can act as a glycolytic enzyme in plants

FEBS Letters

Dancer, Jane¹  Hatzfeld, Wolf-Dieter¹  Stitt, Mark¹ 

[1] Lehrstuhl für Pflanzenphysiologie, 8580 Bayreuth, FRG

关键词: Pyrophosphate: fructose-6-phosphate phosphotransferase;    Pyrophosphate;    Fructose-2;    6-biphosphate;    Glycolysis;    (Plant);    ACES;    2-[(2-amino-2-oxoethyl)amino]ethanesulfonic acid;    CCCP;    carbonyl cyanide m-chlorophenyl-hydrazone;    Fru1;    6/2;    6P2;    fructose 1;    6-/2;    6-bisphosphate;    Fru/G1c6P;    fructose/glucose 6-phosphate;    PEP;    phosphoenolpyruvate;    PFP;    pyrophosphate: fructose-6-phosphate phosphotransferase;    PGA;    3-phosphoglycerate;    Pi;    inorganic phosphate;    PPi;    inorganic pyrophosphate;   

DOI  :  10.1016/0014-5793(89)81042-7

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Experiments were carried out to provide direct evidence that pyrophosphate: fructose-6-phosphate phosphotransferase (PFP) can operate as a glycolytic enzyme in some circumstances. A large increase in the rate of glycolysis was produced by adding uncoupler and alkalinising the medium of heterotrophic Chenopodium rubrum cells. Initially, a marked decrease in phosphoenolpyruvate, 3-phosphoglycerate and hexose phosphates occurred, but no change in fructose 2,6-bisphosphate or inorganic pyrophosphate was observed. However, a gradual increase in the rate of O₂ uptake during the subsequent 5 min was accompanied by an increase in fructose 2,6-bisphosphate and a decrease in pyrophosphate, providing evidence that activation of PFP contributes to the increase in rate of glycolysis. This was accompanied by partial recovery of the adenine nucleotide energy status.

【 授权许可】

Unknown