The reversible Michaelis–Menten law, as with many enzymatic rate laws, can be decomposed into a capacity term, a thermodynamic term, and an enzyme saturation level. This is more easily seen when we write the reversible rate law as:
where  is the capacity term,  the thermodynamic term and 
the saturation term. The separation can be even better appreciated if we look at the elasticity coefficient . According to elasticity algebra, the elasticity of a product is the sum of the sub-term elasticities, that is:
Hence the elasticity of the reversible Michaelis–Menten rate law can easily be shown to be:
Since the capacity term is a constant, the first elasticity is zero. The thermodynamic term can be easily shown to be:
where  is the disequilibrium ratio and equals  and  the mass–action ratio
The saturation term becomes: