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KINETIC MECHANISM OF PYROPHOSPHATE‐DEPENDENT PHOSPHOFRUCTOKINASE FROM PROPIONIBACTERIUM FREUDENREICHII AT EXTREMELY HIGH CONCENTRATION (> 0.5 m M ) OF PYROPHOSPHATE
Author(s) -
CHO YONGKWEON
Publication year - 1992
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1992.tb00435.x
Subject(s) - pyrophosphate , propionibacterium freudenreichii , phosphofructokinase , chemistry , pi , kinetics , ping pong , biochemistry , enzyme , biophysics , biology , glycolysis , thermodynamics , physics , quantum mechanics , fermentation , yield (engineering)
A new region for enzyme activity of inorganic pyrophosphate‐dependent phosphofructokinase from Propionibacterium freudenreichii was detected at extremely high concentration (>0.5 m M) of pyrophosphate, where the maximum velocity increased about 3 times. At a relatively low concentration (<0.1 m M) of pyrophosphate, the kinetic mechanism is rapid equilibrium random sequential with E:F6P:Pi, E:MgPPi:Pi and E:FBP:MgPPI being dead‐end complexes. However, the data from initial velocity and product inhibition patterns at extremely high concentration of pyrophosphate are consistent with a ping‐pong mechanism with E:MgPPi:Pi as a dead‐end complex, where MgPPi binds first.