PRODUCT INHIBITION OF REVERSIBLE ENZYME-CATALYZED REACTIONS

Product inhibition studies of reversible reactions can give unusual ki netic patterns. A plot of rate versus substrate concentration may appe ar to be sigmoidal and the double reciprocal plot will show upward cur vature. This apparent positive cooperativity is due to the simultaneou s occurrence of both the forward and reverse reaction. By fitting the appropriate rate equation to the data it is possible to determine the maximum velocity and Michaelis constant for both forward and reverse r eaction from experiments conducted in one direction only.