Product inhibition of reversible enzyme-catalysed reactions.

Product inhibition studies of reversible reactions can give unusual kinetic patterns. A plot of rate versus substrate concentration may appear to be sigmoidal and the double reciprocal plot will show upward curvature. This apparent positive cooperativity is due to the simultaneous 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 reaction from experiments conducted in one direction only.