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?
- A biological catalyst that speeds up a reaction without being consumed
- What is the active site of an enzyme?
- The region where substrate binds and the reaction is catalyzed
- What is the Michaelis-Menten equation?
- v = Vmax[S] / (Km + [S])
- What does Km represent in enzyme kinetics?
- The substrate concentration at which reaction velocity is half of Vmax
- What does Vmax represent in enzyme kinetics?
- The maximum reaction velocity when the enzyme is fully saturated with substrate
- How does a low Km value relate to substrate affinity?
- A low Km indicates high affinity between enzyme and substrate
- What is a Lineweaver-Burk plot?
- 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?
- 1/Vmax
- What does the x-intercept of a Lineweaver-Burk plot equal?
- -1/Km
- Where does a competitive inhibitor bind?
- The active site, competing directly with the substrate
- How does a competitive inhibitor affect apparent Km?
- It increases the apparent Km
- How does a competitive inhibitor affect Vmax?
- Vmax stays the same
- How can competitive inhibition be overcome?
- By increasing substrate concentration
- Where does a noncompetitive inhibitor bind?
- An allosteric site, not the active site
- How does a noncompetitive inhibitor affect Vmax?
- It decreases Vmax