FFLD 11

Question 1

A progress curve for an enzyme catalysed reaction:
A. Follows the change in substrate or product concentration with time
B. Is linear until the reaction reaches completion
C. Measures the initial substrate of a reaction
D. Shows that enzyme is degraded as the reaction proceeds

Answer 1

A

Question 2

A high kM for an enzyme-substrate pair indicates a:
A. Fast reaction rate
B. Slow reaction rate
C. High affinity between enzyme and substrate
D. Low affinity between enzyme and substrate

Answer 2

D

Question 3

Select the correct statement
A. Monomeric proteins are usually allosteric enzymes
B. Proteases can cleave several different types of covalent bonds
C. Allosteric enzymes produce a hyperbolic curve on a reaction velocity vs. substrate concentration graph
D. The energy molecule ATP can act as an allosteric regulator

Answer 3

D

Question 4

Select the incorrect statement:
A. Allosteric enzymes display cooperativity and have two or more subunits
B. An allosteric activator of an allosteric enzymes shift the sigmoidal curve to the left (and makes the curve less S-shaped)
C. An allosteric inhibitor of an allosteric enzyme shifts the Sigmoidal curve to the right (and makes the curve more S-shaped)
D. Allosteric enzymes follow Michaelis-Menten kinetics

Answer 4

D

Question 5

For the Michaelis-Menten equation to work the following assumptions are made (select all correct answers)
A. The [S] does not change significantly at the very beginning of the reaction
B. No products are converted back to substrates
C. The E + S -> ES step is faster than the ES -> E + P step
D. [S]&raquo_space;»> [E]
E. The K1 and K-1 are equal
F. K2 is negligible

Answer 5

A, B, D and E