Rapid Equilibrium bisubstrate systems complex

However, the primary double reciprocal plots of some rapid equilibrium systems are identical. In rapid equilibrium systems, in the presence of the products of reaction, the primary reciprocal plots are very characteristic and depend on the number and type of enzyme-substrate and enzyme-product complexes that can form. Therefore, in order to distinguish between different t5q>es, one must revert to product inhibition patterns that can easily distinguish between aU types of rapid equilibrium bisubstrate systems (Plowman, 1972 Segel, 1975) (Table 2). 

Fromm and Rudolph have discussed the practical limitations on interpreting product inhibition experiments. The table below illustrates the distinctive kinetic patterns observed with bisubstrate enzymes in the absence or presence of abortive complex formation. It should also be noted that the random mechanisms in this table (and in similar tables in other texts) are usually for rapid equilibrium random mechanism schemes. Steady-state random mechanisms will contain squared terms in the product concentrations in the overall rate expression. The presence of these terms would predict nonhnearity in product inhibition studies. This nonlin-earity might not be obvious under standard initial rate protocols, but products that would be competitive in rapid equilibrium systems might appear to be noncompetitive in steady-state random schemes , depending on the relative magnitude of those squared terms. See Abortive Complex... 

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