This tolerance would explain why bogus molecules of slightly different size compared to the true substrate molecule can still be accomodated by the elastic active site. Small changes in temperature would distort the active site conformation but not so much that the active site could not still accomodate the substrate molecular size. PH changes which would also change the active site conformation but not so much that the active site could not flexibly accomodate the substrate molecule. Return to the top of the page. A number of things can happen to throw a monkey wrench into this remarkably efficient process.
Every enzyme has a temperature range of optimum activity.
Outside that temperature range the enzyme is rendered inactive and is said to be totally inhibited. When these forces are disturbed and changed, this causes a change in the secondary and tertiary levels of protein structure, and the active site is altered in its conformation beyond its ability to accomodate the substrate molecules it was intended to catalyze. Return to the top of the page. Effects on Enzyme Activity Changes in the pH or acidity of the environment can take place that would alter or totally inhibit the enzyme from catalyzing a reaction. This change in the pH will affect the polar and non-polar intramolecular attractive and repulsive forces and alter the shape of the enzyme and the active site as well to the point where the substrate molecule could no longer fit, and the chemical change would be inhibited from taking place as efficiently or not at all.