The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics. Product formed (mmol/min) Substrate added (mmol/L) 217 0.8 325 433 4 488 647 1000 The Km for this enzyme is approximately: 4 mM. 2 mM. 1 mM. O 6 mM. 1000 mM.

Chemistry & Chemical Reactivity
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Chapter14: Chemical Kinetics: The Rates Of Chemical Reactions
Section: Chapter Questions
Problem 43PS: Compare the lock-and-key and induced-fit models for substrate binding to an enzyme.
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The following data were obtained in a study of an enzyme known to follow Michaelis-Menten
kinetics.
Product formed (mmol/min)
Substrate added (mmol/L)
217
0.8
325
2
433
4
488
6
647
1000
The Km for this enzyme is approximately:
4 mM.
2 mM.
1 mM.
6 mM.
1000 mM.
Transcribed Image Text:The following data were obtained in a study of an enzyme known to follow Michaelis-Menten kinetics. Product formed (mmol/min) Substrate added (mmol/L) 217 0.8 325 2 433 4 488 6 647 1000 The Km for this enzyme is approximately: 4 mM. 2 mM. 1 mM. 6 mM. 1000 mM.
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