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aidan aidan
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11 years ago
Why does Km increases in competitive inhibition?
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11 years ago
Because when there is a competitive inhibitor present (i.e. a substance which competes with the 'correct' substrate for a place within the enzyme active site), that means that the reaction proceeds more slowly (at a lower rate) for any given substrate concentration.

More substrate is required to successfully 'saturate' the enzyme present, and minimise the effect of the inhibitor, i.e. the Michaelis-Menten curve gets less steep, and reaches an asymptote (Vmax) at a point further towards towards the right hand side of the graph (at a higher substrate concentration).

Since Km is the substrate concentration at half-Vmax, Km also gets shifted to the right, i.e. it increases.
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