Enzyme kinetics models and common biochemistry lab techniques tested on the MCAT.
40 cards · basic cards · AI-written, checked twice. Edit anything.
- What is an enzyme?
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A biological catalyst that speeds up a reaction without being consumed- What is the active site of an enzyme?
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The region where substrate binds and the reaction is catalyzed- What is the Michaelis-Menten equation?
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v = Vmax[S] / (Km + [S])- What does Km represent in enzyme kinetics?
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The substrate concentration at which reaction velocity is half of Vmax- What does Vmax represent in enzyme kinetics?
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The maximum reaction velocity when the enzyme is fully saturated with substrate- How does a low Km value relate to substrate affinity?
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A low Km indicates high affinity between enzyme and substrate- What is a Lineweaver-Burk plot?
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A double reciprocal plot of 1/v versus 1/[S] used to analyze enzyme kinetics- What does the y-intercept of a Lineweaver-Burk plot equal?
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1/Vmax- What does the x-intercept of a Lineweaver-Burk plot equal?
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-1/Km- Where does a competitive inhibitor bind?
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The active site, competing directly with the substrate- How does a competitive inhibitor affect apparent Km?
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It increases the apparent Km- How does a competitive inhibitor affect Vmax?
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Vmax stays the same- How can competitive inhibition be overcome?
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By increasing substrate concentration- Where does a noncompetitive inhibitor bind?
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An allosteric site, not the active site- How does a noncompetitive inhibitor affect Vmax?
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It decreases Vmax
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