Enzyme activity will be high when substrate concentration is equal to KM b. below KM ...
- Enzyme activity will be high when substrate concentration is
- equal to KM b. below KM c. above KM d. none of the above
- Metalloproteases mostly use the element
- Cu b. Fe c. Zn d. Mn
Homework Answers
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Enzyme activity will be high when substrate concentration is
equal to KM b. below
KM ...
What is the consequence of a high Km value of an enzyme?
What is the consequence of a high Km value of an enzyme? High concentration of the substrate is needed for the maximal enzyme activity. The enzyme is present in a large concentration in the cell. Moderate concentration of the substrate will be enough for maximal enzyme activity. This enzyme has high maximal velocity.
What is substrate concentration, expressed as a multiple of Km, when an enzyme reaction is observed...
What is substrate concentration, expressed as a multiple of Km, when an enzyme reaction is observed to have an initial rate Vo = 0.75 Vmax. Select one: O a. [S] = 0.33 x km O b. [S] = 0.25 km O c. [S] = 0.75 x Km O d. [S] = 0.3 x km O e. [S] = 0.5 x km Check Next page ime Jump to...
Which of the following statements are corrects? When the substrate concentration is equal to KM, the...
Which of the following statements are corrects? When the substrate concentration is equal to KM, the reaction rate is half of its maximal value The value of KM is proportional to the concentration of the ES complex Inhibitors are molecules capable of decreasing the enzyme activity Uncompetitive inhibitors have no effect on Vmax fill in the blanks The respiratory chain is a set of_______complexes whose role is to transport _______ from reduced co-factors to dioxygen. The (entry from previous blank)...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
At what substrate concentration would an enzyme with a kcat of 30.0 sec-1 and a Km...
At what substrate concentration would an enzyme with a kcat of 30.0 sec-1 and a Km of 0.0030 M have an initial velocity that is 25% of the maximum velocity? a. 0.0010M b 0.0090 M c. 0.0015 M d. 0.0060 M e.Cannot be determined
6. An enzyme with a km of 0.06mmol/L hydrolyzed a substrate of a concentration 0.03 mmol/L....
6. An enzyme with a km of 0.06mmol/L hydrolyzed a substrate of a concentration 0.03 mmol/L. The initial velocity ws 0.0015 mmol/L.min!. Calculate the substrate concentration which gives an initial velocity of 0.003 mmol/L. min-1 7. Urease hydrolyzed urea at [s]=0.03mmol/L with a km of 0.06 mmol/L. The initial velocity observed was 1.5X10-3 mmol/L.min Calculate the initial velocity of the enzyme reaction when using [s]=0.12mmol/L
Can you infinitely infrease the substrate concentration to increase enzyme activity in a closed system such...
Can
you infinitely infrease the substrate concentration to increase
enzyme activity in a closed system such as a batch culture?
Can you infinitely increase the substrate concentration to increase enzyme activity in a closed system such as a batch culture? Yes Your answer B NO
If the substrate concentration is varied with a fixed concentration of enzyme, it is observed that...
If the substrate concentration is varied with a fixed concentration of enzyme, it is observed that at low substrate concentrations that overall order while at high substrate concentrations, the reaction will be overall order. Select one: a. first; second b. first; third order c. first; zero d. second; second e. second; pseudo first order
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but...
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but eventually reaches a maximum value, even though the concentration of substrate continues to increase. Which of the following best explains why? O As substrate concentration increases, the substrates preferentially bind with each other instead of the active site of the enzyme, and no additional catalysis occurs. As substrate concentration increases, the active sites of all the enzyme molecules become occupied with substrate molecules, and...
For each of the following enzyme regulation mechanisms/situations below, list whether it will: A. Always decrease activity V B. Always increase activity V C. May increase or decrease activity V D. May...
For each of the following enzyme regulation mechanisms/situations below, list whether it will: A. Always decrease activity V B. Always increase activity V C. May increase or decrease activity V D. May decrease or possibly have minimal effect on activity V E. Will definitely have no significant effect on activity V 1. Competitive Inhibitor with [I] > Ki and [S] < Km 2. Noncompetitive inhibitor with [I] > Ki and [S] < Km 3. Phosphorylation of Enzyme 4. Product Inhibition...
What is substrate concentration, expressed as a multiple of Km, when an enzyme reaction is observed to have an initial rate Vo = 0.75 Vmax. Select one: O a. [S] = 0.33 x km O b. [S] = 0.25 km O c. [S] = 0.75 x Km O d. [S] = 0.3 x km O e. [S] = 0.5 x km Check Next page ime Jump to...
3. Why is an allosteric enzyme more sensitive to substrate concentration around Km values than a Michaelis-Menten enzyme with the same Vmax? 4. Explain how pH and temperature influence enzyme activity. ( A Lineweaver-Burk (double reciprocal) plot was used to compare the effects of three different reversible inhibitors (A, B and C) on an enzyme. The plot of 1/V vs 1/[S] for the enzyme with no inhibitor is shown in a solid black line. The plot of 1/V vs 1/[S]...
6. An enzyme with a km of 0.06mmol/L hydrolyzed a substrate of a concentration 0.03 mmol/L. The initial velocity ws 0.0015 mmol/L.min!. Calculate the substrate concentration which gives an initial velocity of 0.003 mmol/L. min-1 7. Urease hydrolyzed urea at [s]=0.03mmol/L with a km of 0.06 mmol/L. The initial velocity observed was 1.5X10-3 mmol/L.min Calculate the initial velocity of the enzyme reaction when using [s]=0.12mmol/L
Can
you infinitely infrease the substrate concentration to increase
enzyme activity in a closed system such as a batch culture?
Can you infinitely increase the substrate concentration to increase enzyme activity in a closed system such as a batch culture? Yes Your answer B NO
If the substrate concentration is varied with a fixed concentration of enzyme, it is observed that at low substrate concentrations that overall order while at high substrate concentrations, the reaction will be overall order. Select one: a. first; second b. first; third order c. first; zero d. second; second e. second; pseudo first order
The rate of an enzyme-catalyzed reaction initially increases with an increase in the substrate concentration, but eventually reaches a maximum value, even though the concentration of substrate continues to increase. Which of the following best explains why? O As substrate concentration increases, the substrates preferentially bind with each other instead of the active site of the enzyme, and no additional catalysis occurs. As substrate concentration increases, the active sites of all the enzyme molecules become occupied with substrate molecules, and...
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