When an enzyme is mixed with a large excess of the substrate, the enzyme-substrate intermediate builds up in a fast initial transient. Then the reaction achieves a steady-state kinetics in which enzyme substrate intermediates remains approximately constant over time and the reaction rate changes relatively slowly.Then the enzyme substrate complex convert into enzyme and product.

Hi Nina,

The enzyme in question may follow different routes depending on the type of interaction it may have with its substrate. In most of the cases, Michaelis - Menten equation is followed as per the assumption. But cooperative binding may alter the kinetics.