Enzymes that are multimeric often display a cooperative response. Like that of the Hemoglobin response to oxygen binding as compared to myglobin's response. The higher the K M value, the lower the affinity of the enzyme for the substrate. V MAX is the maximum velocity, which is observed at high substrate concentrations. There is a theoretical maximum to how high the catalytic efficiency can be.
Diffusion is the physical processes by which they come into contact with one another.
This is called the diffusion-limited rate . When an enzyme catalyzes at this rate it is said to be catalytically perfect . Alteration of enzyme activity Inhibition Irreversible inhibition Covalent modification Usually of a group at the active site. The inhibitor competes for the same binding site as the substrate with a dissociation constant of K I . The inhibitor binds to a site on the enzyme that is distinct from subtrate binding site with a dissociation constant of K I .