Questions 8 and 9

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*e·Explain why an uncompetitive inhibitor lowers Vmax and appears to decrease KM 8. In the case of the competitive inhibitor, we said that both k, and KM are altered by that inhibitor. Since an uncompetitive inhibitor alters Ky, does that mean that an uncompetitive inhibitor changes the value of k,? 9. If you are studying a reaction that is operating under Michaelis-Menton kinetics and you double the concentration of enzyme, VMAx will double but Kw, will not change. Explain why the value of KM does not change in this instance. In other words, why is the value of Ky independent of enzyme concentration? xz