Competitive inhibition is characterized by the inhibitor binding to the active site of the enzyme, thereby preventing the substrate from binding. This leads to an increase in the apparent Km (higher substrate concentration required for half-maximal velocity) but does not affect the Vmax (maximum reaction velocity, which can still be reached if substrate concentration is sufficiently high).
Among the following select the correct statements : In reversible competitive enzyme inhibition - (i) The inhibitor bears structural resemblance to substrate. - (ii) Both K and Vmax are increased. - (iii) The inhibitor does not bear structural resemblance to substrate. - (iv) K is increased whereas Vmax remains unchanged.
Asked in Food Safety Officer 2022 · Topic: Cell (Cytoplasm and Cytosol: Composition and Functions)
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