Usually, an enzyme molecule has only one active site, and the active site fits with one specific type of substrate. An active site contains a binding site that binds the substrate and orients it for catalysis. Residues in the binding site form hydrogen bonds, hydrophobic interactions, or temporary covalent interactions (van der Waals) with the substrate to make an enzyme-substrate complex.
The decreased volume only disrupts the equilibrium if the moles of gaseous products and moles of gaseous reactants are unequal. If there are an equal number of moles of gaseous substances on both sides of the arrow, the change in volume has an equal effect on the concentrations of reactants and of products.
When the velocity decreases as the fluid leaves the orifice the pressure increases and tends to return to its original level. All of the pressure loss is not recovered because of friction and turbulence losses in the stream. The pressure drop across the orifice (P in Fig. 1) increases when the rate of flow increases. When there is no flow there is no differential. The differential pressure is proportional to the square of the velocity, it therefore follows that if all other factors remain constant, then the differential is proportional to the square of the rate of flow.