How many (i) transition states, and (ii) intermediates are associated with this mechanism:
Are the following statements correct descriptions of the steady state assumption used to derive the Michaelis-Menten equation?
The concentration of enzyme in an assay is much lower than the concentration of substrate.
The equilibrium between E, S, and ES is rapidly established.
The concentration of the ES complex does not change during the time frame where enzyme activity is being measured.
Product formed during the reaction does not react with E to reform ES at a significant rate
Which of the following statements are true about the catalytic efficiency of an enzyme following the simple kinetic scheme shown here?
a low Km and high kcat increase catalytic efficiency.
the theoretic upper limit to catalytic efficiency is diffusion controlled.
catalytic efficiency is a second order rate constant with a value close to k1 for a “perfect” enzyme.
The red line on the following reaction coordinate diagram is consistent with which kinetic mechanism?
An enzyme that follows Michaelis-Menten kinetics has a Vmax of 200.0 units and a Km of 0.100 mM. What will be the activity for this enzyme when the substrate concentration is 0.500 mM?
Algebraically solve the Michaelis-Menten equation for [S] to answer the following question: what concentration of substrate gives an initial rate of 1500 units for an enzyme that exhibits a Vmax of 10,000 units and a Km of 0.25 mM?
Kinetic analysis of a homodimeric enzyme of 150,000 molecular weight (that is the Mr of the dimer) catalyzing conversion of substrate S to product P provides the following kinetic constants: Vmax = 1000 units when 1 mg of enzyme is assayed. Assume each subunit contains an active site; i.e. there are two active sites per dimer. Calculate the turnover number for this enzyme. In units of s-1.
What forms of the enzyme do a competitive (C), noncompetitive (NC), and uncompetitive (UC) inhibitor bind to?
NC: E and ES.
UC: ES only.
Using information from the following graph of 1/v vs. 1[S] for a particular enzyme, determine the values of Vmax and Km
Vmax = 50
Km = 0.4
For the kinetic scheme shown below, which rate constants are first order?
k2, k-2, k3, k-3 , k4 ,k-1
Which statement(s) can be made with certainty about the following reaction:
the reaction is exergonic
The following graph shows a Lineweaver-Burke ( 1/v vs. 1/[S] ) plot (indicated by an arrow) for an enzymatic reaction transforming substrate S to product P. Which line could possibly represent a competitive inhibitor?
Which of the following strategies for rate acceleration apply to ALL enzyme-catalyzed reactions?
transition state stabilization
In general, the structure of the active site of an enzyme will be most complementary to: