BENG 130. Enzymatic Reaction Kinetics - Practice Problems
Solutions - Provided by Prof. Huang
1. Catalytic Strategy of Enzymes – Physical and Chemical Basis
Enzymes, in general, have very high substrate specificity and catalytic efficiency. The catalytic
power is the result of the lowering of the activation energy barrier or the energy of the transition
state complex by the enzymes.
List the main structural characteristics and physical forces that give rise to the high catalytic
specificity and power of enzymes.
Main point: Application of the transition state theory and the concept of molecular driving
forces/energies to enzyme-catalyzed biochemical reactions.
For solutions: See Page P6 in lecture notes/slides (on enzymatic reaction kinetics)
2. Enzyme Reaction Kinetics – The Michaelis-Menten Equation
a. What are the two assumptions made in the derivation of the Michaelis-Menten
kinetics/equation?
b. Enzyme-catalyzed reaction of a substrate S into product P can be described as two reversible
reactions in serial as follows:
k1 k2
S + E ES E + P
k-1 k-2
If (k-1 + k2,) >> k1 and k2 >> k-2 , steady-state approximation can be applied to [ES] and the
reaction can be simplified to:
k1 k2
S + E ES E + P
k-1
Derive the following rate equation (try to see if you can derive it in a few minutes).
d [ P] [S ]
v vmax
dt [S ] K M
vmax k2 [ E ]0 kcat [ E ]0 ;
(maximum rate is achieved when all enzyme molecules are saturated with substrate and utilized)
[ E ]0 Total concentration of enzyme;
k1 k2
KM , the so-called Michaelis constant.
k1
Purposes: know how to derive the rate law for enzyme reaction (the Michaelis-Menten equation),
the concepts of maximum rate, KM, and kcat (= k2, catalytic rate constant).
Solutions: See Page P9 in lecture notes/slides (on enzymatic reaction kinetics)
This study source was downloaded by 100000899194722 from CourseHero.com on 05-30-2025 16:05:53 GMT -05:00
https://www.coursehero.com/file/13900162/Solutions-to-Practice-Problems-for-Enzyme-Reaction-Kinetics/
Solutions - Provided by Prof. Huang
1. Catalytic Strategy of Enzymes – Physical and Chemical Basis
Enzymes, in general, have very high substrate specificity and catalytic efficiency. The catalytic
power is the result of the lowering of the activation energy barrier or the energy of the transition
state complex by the enzymes.
List the main structural characteristics and physical forces that give rise to the high catalytic
specificity and power of enzymes.
Main point: Application of the transition state theory and the concept of molecular driving
forces/energies to enzyme-catalyzed biochemical reactions.
For solutions: See Page P6 in lecture notes/slides (on enzymatic reaction kinetics)
2. Enzyme Reaction Kinetics – The Michaelis-Menten Equation
a. What are the two assumptions made in the derivation of the Michaelis-Menten
kinetics/equation?
b. Enzyme-catalyzed reaction of a substrate S into product P can be described as two reversible
reactions in serial as follows:
k1 k2
S + E ES E + P
k-1 k-2
If (k-1 + k2,) >> k1 and k2 >> k-2 , steady-state approximation can be applied to [ES] and the
reaction can be simplified to:
k1 k2
S + E ES E + P
k-1
Derive the following rate equation (try to see if you can derive it in a few minutes).
d [ P] [S ]
v vmax
dt [S ] K M
vmax k2 [ E ]0 kcat [ E ]0 ;
(maximum rate is achieved when all enzyme molecules are saturated with substrate and utilized)
[ E ]0 Total concentration of enzyme;
k1 k2
KM , the so-called Michaelis constant.
k1
Purposes: know how to derive the rate law for enzyme reaction (the Michaelis-Menten equation),
the concepts of maximum rate, KM, and kcat (= k2, catalytic rate constant).
Solutions: See Page P9 in lecture notes/slides (on enzymatic reaction kinetics)
This study source was downloaded by 100000899194722 from CourseHero.com on 05-30-2025 16:05:53 GMT -05:00
https://www.coursehero.com/file/13900162/Solutions-to-Practice-Problems-for-Enzyme-Reaction-Kinetics/
