Homework Answers
1. The value of Km is 0.20 mM. Here mM is the unit.
Km is the substrate concentration at which the rate of reaction is half maximum.
The V max is 1.0 mM/sec. Here mM/ sec is the unit.
2.
Rate of ES formation
3. The type of inhibition is Non-competitive inhibition. Because even when the substrate concentration is very high compared to inhibitor, the product formation has not reached maximum with inhibitor.
Non-competitive inhibition.
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The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed react...
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. S Where v is the velocity or rate, Vmax is the maximum velocity, Km is the +IST Michaelis- Menten constant, and I5 s the substrate concentration. K + S v (uM/min) a) A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (Vo) at different substrate concentrations ([S]) 300 Vmax 250 1/2 Vmax First, move the line labeled "Vmax to a...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. T...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
3) For the simplified representation of an enzyme-catalyzed reaction shown below, the statement “ES is in...
3) For the simplified representation of an enzyme-catalyzed
reaction shown below, the statement “ES is in steady-state” means
that:
A) k2 is very slow.
B) k1= k2.
C) k1= k-1.
D) k1[E][S] = k-1[ES] + k2[ES].
E) k1[E][S] = k-1[ES].
3) For the simplified representation of an enzyme-catalyzed reaction shown below, the statement “ES is in steady-state" means that: k, k, E+S <> ES Z E +P - k1 A) k2 is very slow. B) Kı= k2. C) K1= k-1....
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A B. For substrate...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A B. For substrate A, she determined 30 min that Km 3.0 HM and kcat Jessica graduated and her project has been passed on to you. Unfortunately, Jessica was so busy that she sometimes forgot to record all of the details of an assay in her lab notebook. Your mentor suggests that you try to back calculate some of the missing concentration values. Assume that the enzyme follows...
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Values for an Enzyme and a substrate are: Km=4 uM and kcat=20/min. For an experiment where...
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le glucose Suusti dle! 6. The Vmax and KM values for an unusual hexokinase found in...
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Consider the data collected for an enzyme-catalyzed reaction [S] (mM) vo (mM s1 0.25 2.00 0.50...
Consider the data collected for an enzyme-catalyzed reaction [S] (mM) vo (mM s1 0.25 2.00 0.50 3.33 1.00 5.00 2.00 6.67 Determine Vmax and K,,m for this reaction. mM s- Vmax mM
Initial rates of an enzyme-catalyzed reaction for various substrate concentrations are listed in the table below....
Initial rates of an enzyme-catalyzed reaction for various substrate concentrations are listed in the table below. From this data determine Km and Vm S(M)v (HM/min) 4.1x103 9.5x104 5.2x104 1.03x104 4.9x10-5 1.06x10 5.1x10-6 173 125 106 80 67 43
The Michaelis-Menten equation is often used to describe the kinetic characteristics of an enzyme-catalyzed reaction. S Where v is the velocity or rate, Vmax is the maximum velocity, Km is the +IST Michaelis- Menten constant, and I5 s the substrate concentration. K + S v (uM/min) a) A graph of the Michaelis-Menten equation is a plot of a reaction's initial velocity (Vo) at different substrate concentrations ([S]) 300 Vmax 250 1/2 Vmax First, move the line labeled "Vmax to a...
CHEM3250 Assignment-Enzyme Inhibition Consider the data below for an enzyme catalyzed reaction. The rate of the reaction has been determined with and without an inhibitor. A total concentration of enzyme of 20 uM was used in the experiment. SHOW WORK AND UNITS!!! Without Inhibitor With Inhibitor [substrate] (mM)Rate of formation of te of formation of product product (mM/min) mM/min) 6.67 5.25 0.49 7.04 38.91 1.0 2.2 6.9 41.8 44.0 1.5 3.5 1 a) On the same graph, plot the data...
3) For the simplified representation of an enzyme-catalyzed
reaction shown below, the statement “ES is in steady-state” means
that:
A) k2 is very slow.
B) k1= k2.
C) k1= k-1.
D) k1[E][S] = k-1[ES] + k2[ES].
E) k1[E][S] = k-1[ES].
3) For the simplified representation of an enzyme-catalyzed reaction shown below, the statement “ES is in steady-state" means that: k, k, E+S <> ES Z E +P - k1 A) k2 is very slow. B) Kı= k2. C) K1= k-1....
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A B. For substrate A, she determined 30 min that Km 3.0 HM and kcat Jessica graduated and her project has been passed on to you. Unfortunately, Jessica was so busy that she sometimes forgot to record all of the details of an assay in her lab notebook. Your mentor suggests that you try to back calculate some of the missing concentration values. Assume that the enzyme follows...
le glucose Suusti dle! 6. The Vmax and KM values for an unusual hexokinase found in Trypansoma cruzi (the causative agent of Chagas disease) are shown in the presence and absence of a bisphonate inhibitor (structure shown). Without inhibitor With inhibitor KM (MM) Vmax (umol. min . mL-1) 90 0.30 125 0.12 antio- try to con OH 120 Po- O=P-0-16MMUZ 0- A bisphonate compound a. What type of inhibitor is bisphonate? b. The parasite hexokinase, unlike the mammalian enzyme, is...
Consider the data collected for an enzyme-catalyzed reaction [S] (mM) vo (mM s1 0.25 2.00 0.50 3.33 1.00 5.00 2.00 6.67 Determine Vmax and K,,m for this reaction. mM s- Vmax mM
Initial rates of an enzyme-catalyzed reaction for various substrate concentrations are listed in the table below. From this data determine Km and Vm S(M)v (HM/min) 4.1x103 9.5x104 5.2x104 1.03x104 4.9x10-5 1.06x10 5.1x10-6 173 125 106 80 67 43
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