Pre Midterm Flashcards
(14 cards)
Inhibitors can regulate ____ activity.
Enzyme
What is EI and how is it created?
Unproductive complex: created when an inhibitor and substrate are competing for an enzyme.
T or F: Competitive inhibitors use different binding sites than the substrate.
False: They are competitive because they share a binding site.
What happens to the KM value of an enzyme when a competitive inhibitor is present?
It increases. This is because the reaction will require more substrate to reach half Vmax.
T or F: Competitive inhibitors can be overcome with enough substrate.
True. Enough substrate will get the enzyme up to Vmax.
What is the difference between a Michaelis-Menten graph and a Lineweaver-Burk graph?
Lineweaver-Burk will be linear, because the equation is the reciprocal of Michaelis-Menten.
What is EIS and how is it formed?
The product of a non-competitive inhibitor. The inhibitor binds to E and ES, as well as the substrate.
If EI and EIS both have different Ki values, what type of inhibition is it?
Mixed inhibition. EI and EIS will have the same Ki in non-competitive.
T or F: The Vmax decreases with non-competitive inhibition.
True. Vmax changes with non-competitive, but doesn’t with competitive.
Which group of amino acids are very non-polar?
F(Phe), A(Ala), M(Met), I(Ile), L(Leu) and V(Val).
Which two amino acids have sulfur?
M(Met) and C(Cys)
How are molecules separated using the TLC method?
Molecules are separated based on polarity.
Which seven amino acid side chains can be charged?
D(Asp), E(Glu), H(His), K(Lys), R(Arg), C(Cys) and Y(Tyr)
What will the charge of C(Cys) be in its protonated form?
It will be neutral. Deprotonated will be -1.
