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