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How does a noncomeptitive inhibitor affect an enzyme?
A noncompetitive inhibitor acts to decrease how fast the enzyme can act on substrates. It accomplishes this by lowering the maximum rate at which it can create products. Noncompetitive inhibitors do not alter the enzyme's Michaelis constant.
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How do competitive inhibitors affect enzyme efficiency?
Competitive inhibitors can be overpowered by introducing excess substrate, so they do not affect the maximum rate of the enzyme. They do, however, make it so that more substrate is required in order to get the enzyme working at half of its maximum rate. As a result, competitive inhibitors act by raising the Michaelis constant of enzymes.
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How is pepsinogen activated in the stomach?
Once in the stomach lumen, pepsinogen finds itself in a very acidic environment. The acidic environment cleaves an amino acid sequence from pepsinogen, turning it into the active enzyme pepsin. This type of activation causes pepsin to only activate in the stomach lumen where it is needed.
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