You are studying the enzyme alcohol dehydrogenase that catalyzes the following r

Question

You are studying the enzyme alcohol dehydrogenase that catalyzes the following reaction: NAD+ + ethanol ? NADH + H+ + acetaldehyde A) You discover that mercury ion (Hg+) at a concentration of 1 mM inhibits the enzyme by 95%. You find by appropriate kinetic experiments that the enzyme's apparent Km for ethanol is the same in the presence and the absence of Hg+. What does this tell you about the kind of inhibition caused by Hg+? B) Explain how you, as a working biochemist, might discover whether or not this enzyme is allosterically regulated.

Explanation / Answer

Since binding of the inhibitor to the enzyme reduces its activity by 95% and does not affect the binding of substrate so it is Non-Competitive inhibition.

If there is a change in the conformation of substrate which can be either Tensed or Relaxed then we can say that it is allosterically regulated

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