Which One Of The Following Statements About The Mechanism Of Lysozyme Is False A The Enzyme Stabilizes A Distorted Hal 1 (54.7 KiB) Viewed 33 times
Which one of the following statements about the mechanism of lysozyme is FALSE? A) The enzyme stabilizes a distorted half-chair conformation for NAM that is thought to resemble the conformation of the transition state. B) The originally proposed Philips mechanism based on the crystal structure of an enzyme-inhibitor complex illustrates all aspects of catalysis. C) The mechanism involves formation of a positively charged carbocation/oxonium intermediate. D) Asp52 contributes to electrostatic and covalent catalysis.
If [Etotal] is increased 10-fold, what is the effect on the rate of an enzyme-catalyzed reaction that follows Michaelis-Menten kinetics? A) The rate will be increased 10-fold only when [S]<<KM. B) The rate will be unchanged at high substrate concentration. C) Vmax and KM will both be increased 10-fold. D) The rate will be increased 10-fold at all substrate concentrations.
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