🧪 Enzymes

1-B   2-B   3-A   4-B  |  5 = low   6 = 37   7 = Km increases, Vmax unchanged   8 = Vmax decreases, Km unchanged   9 = Because competitive inhibitors compete for the same active site as the substrate, so enough substrate molecules statistically outcompete the inhibitor; non-competitive inhibitors bind a separate allosteric site, so no amount of substrate displaces them  |  10 = Each enzyme's active site has amino acid side chains whose shape and charge are optimised for a specific pH; pepsin's active site is stable and most active in the highly acidic stomach, while trypsin's active site is folded to work in the alkaline environment of the small intestine — outside their optimum range, both would denature or lose activity.