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In permeabilized yeast cells 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase are studied during growth. It is shown that in yeast at least two fructose 2,6-bisphosphate degrading enzyme activities occur, differing in pH profile and in their substrate affinities. The activities of 6-phosphofructo-2-kinase and of fructose-2,6-bisphosphatases drop in the exponential and the transition phase while the activity of the alkaline phosphatases steadily increases. In the stationary phase the activities of 6-phosphofructo-2-kinase and of the low Km fructose-2,6-bisphosphatase increase again. Yeast 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase were purified and separated from each other. The purified 6-phosphofructo-2-kinase was found to exhibit a very high specific activity (1.3 U/mg). The enzyme is efficiently inhibited by ATP. The ATP inhibition is most pronounced at low concentrations of magnesium and fructose-6-phosphate. Phosphoenolpyruvate and sn-glycerol 3-phosphate are inhibitors of the enzyme. The high-affinity yeast fructose-2,6-bisphosphatase releases inorganic phosphate from the 2-position of fructose 2,6-bisphosphate. It displays hyperbolic kinetics towards fructose 2,6-bisphosphate (Km = 0.3 microM) and is strongly inhibited by fructose 6-phosphate. The inhibition is counteracted by sn-glycerol 3-phosphate. The enzyme is shown to be inactivated by cAMP-dependent phosphorylation and reactivated by the action of protein phosphatase 2A.
E Hofmann, and
A Bedri, and
R Kessler, and
M Kretschmer, and
W Schellenberger
May 1983,
The Journal of biological chemistry,
E Hofmann, and
A Bedri, and
R Kessler, and
M Kretschmer, and
W Schellenberger
June 1991,
The Biochemical journal,
E Hofmann, and
A Bedri, and
R Kessler, and
M Kretschmer, and
W Schellenberger
September 2006,
Current opinion in clinical nutrition and metabolic care,
E Hofmann, and
A Bedri, and
R Kessler, and
M Kretschmer, and
W Schellenberger
June 1990,
Nucleic acids research,
E Hofmann, and
A Bedri, and
R Kessler, and
M Kretschmer, and
W Schellenberger
January 1995,
Annual review of biochemistry,
E Hofmann, and
A Bedri, and
R Kessler, and
M Kretschmer, and
W Schellenberger
September 1987,
The Biochemical journal,
E Hofmann, and
A Bedri, and
R Kessler, and
M Kretschmer, and
W Schellenberger
November 1990,
Seikagaku. The Journal of Japanese Biochemical Society,
E Hofmann, and
A Bedri, and
R Kessler, and
M Kretschmer, and
W Schellenberger
October 1993,
Biochemistry,
E Hofmann, and
A Bedri, and
R Kessler, and
M Kretschmer, and
W Schellenberger
May 1985,
Archives of biochemistry and biophysics,
E Hofmann, and
A Bedri, and
R Kessler, and
M Kretschmer, and
W Schellenberger
July 2001,
The Journal of biological chemistry,
