Abstract
ABSTRACT A new region for enzyme activity of inorganic pyrophosphate-dependent phosphofructokinase from Propionibacterium freudenreichii was detected at extremely high concentration (>0.5 mM) of pyrophosphate, where the maximum velocity increased about 3 times. At a relatively low concentration (<0.1 mM) 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.
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