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Allosteric activation and competitive inhibition of yeast phosphofructokinase by d-fructose

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Abstract

Purified phosphofructokinase from bakers yeast is activated by d-fructose in low concentrations (up to 1 mM) and inhibited by high concentrations. The stimulatory effect of d-fructose is similar, but smaller than that of AMP. In the presence of AMP (0.4 mM or higher) d-fructose does no longer stimulate, but its inhibitory effect persists (K I =8 mM). Its dualistic action on phosphofructokinase activity indicates that d-fructose might induce low frequency in glycolytic oscillations by direct interaction with the enzyme.

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Abbreviations

ALD:

fructosediphosphate aldolase (4.1.2.13)

ATPase:

ATP phosphohydrolase (3.6.1.3)

DAP:

dihydroxyacetonephosphate

F-6-P:

fructose-6-phosphate

FDP:

fructose-1,6-diphosphate

GAP:

glyceraldehydephosphate

GDH:

glycerol-3-phosphate dehydrogenase (1.1.1.8)

PEP:

phosphoenolpyruvate

PFK:

phosphofructokinase (2.7.1.11)

PK:

pyruvate kinase (2.7.1.40)

TIM:

triosephosphate isomerase (5.3.1.1.)

Tris:

trishydroxymethylaminomethan

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Betz, A., Röttger, U. & Kreuzberg, K.H. Allosteric activation and competitive inhibition of yeast phosphofructokinase by d-fructose. Arch. Microbiol. 103, 123–126 (1975). https://doi.org/10.1007/BF00436338

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  • DOI: https://doi.org/10.1007/BF00436338

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