Lecture 2

Question 1

High complementary interactions between S and E

Answer 1

energetically favorable
hydrophobic-hydrophobic, H-bond, favorable coulombic interactions

Question 2

substrate binding involves conformation change in E (induced fit)

Answer 2

free enzyme differs from bound enzyme, optimal recognition of substrates, brings catalytically important residue to right position, can induce residues distant to binding sites

Question 3

substrate binding is often a small region

Answer 3

true

Question 4

Km

Answer 4

Vmax/2, affinity for substrate binding, higher Km = lower affinity for S binding

Question 5

Vmax

Answer 5

max rate of the reaction

Question 6

competitive inhibitor

Answer 6

same Vmax if S is increased, but Km is increased
can flood with S to reach Vmax

Question 7

uncompetitive inhibitor

Answer 7

Bind to ES complex and decrease total number of functional enzymes
Vmax and Km decreased

Question 8

noncompetitve inhibitor

Answer 8

similar to dropping E
same Km, but lower Vmax