The degree of steady-state rate equations for multi-subunit allosteric enzymes [proceedings].

There are several enormous simplifications which result immediately from the application of this concept in enzyme kinetics. It is no longer necessary to discuss in vague imprecise terms the relative size of rate constants to effect reduction or allow rapid equilibrium assumptions. The resultant itself takes care of that. I t is no longer necessary to work out a complete rate equation for a complex mechanism to see what the reduced function will look like. It is only necessary to calculate the distribution expressions for the leastand highest-substrate-degree pathways to the free enzyme and the highestsubstrate-populated nodes. Most important of all, we can now turn systematically to the task of the interpretation of product-inhibition effects in complex enzyme-catalysed reactions without recourse to the highly restrictive rapid-equilibrium assumptions.