Given an elementary step for a reaction, write the step’s rate equation. 3, 5, 7
Relate reaction velocity to enzyme concentration.
Describe when an enzyme will become saturated in terms of substrate concentration.
Understand the derivation of the Michaelis-Menten equation. 21
Relate Vmax to KM. 13, 15, 17, 27
Know what kcat is.
Justify the use of kcat and KM in the best measure of enzyme efficiency.
Know what a Lineweaver-Burk plot is. 23
State three cases where the Michaelis-Menten rate equation is not applicable.
Explain why all irreversible inhibitors are not suicide substrates.
Describe how a competitive inhibitor affects KM and Vmax.
Be able to calculate KI, given the equation
Recognize transition state analogs, and relate them to competitive inhibition. 35, 41
Relate the effect of mixed inhibitors and competitive inhibitors on KM and Vmax, and to enzyme binding sites. 43
Know that allosteric regulation includes positive and negative effectors. 49
Describe how feedback inhibition works.