Homework Answers
Answer
Option B is correct i.e " Between X and Y, the number of enzyme molecules is limiting".
Explanation
From point W to X, substrate concentration is increasing that leads to collision of substrate with active site of enzyme and forms Enzyme-substrate complex; as we know between these points enzyme (free active sites) is also excess.
From point X and Y, all the active sites of enzymes are occupied by substrates that further causes no increase or enhancement in rate of reaction is possible.
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6 The graph shows the effect of substrate concentration on the rate of an enzyme- controlled...
The graph below shows an enzyme- controlled reaction. The enzyme concentration is kept constant. At concentrations...
The graph below shows an enzyme- controlled reaction. The enzyme concentration is kept constant. At concentrations of substrate greater than X, which of the following statements is true? Rate of reaction 0 Concentration of substrate X The rate of reaction is limited by enzyme concentration. The rate of reaction tends towards zero. The substrate has an inhibitory effect. The products have an inhibitory effect.
Which of the diagrams illustrates the way in which the rate of an enzyme-controlled reaction depends...
Which of the diagrams illustrates the way in which the rate of an enzyme-controlled reaction depends on substrate concentration? * А B Rate of reaction MÚN Substrate concentration A B D When starch and amylase are mixed in the presence of iodine solution, the blue-black colour rapidly disappears. This is due to the formation of which molecule? * glucose O glycogen sucrose O maltose Which of the following enzyme groups can catalyse oxidation reactions? * O phosphorylases isomerases hydrolases dehydrogenases...
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...
The concentration of substrate X is low. What happens to the rate of the enzyme- catalyzed reaction if the concentr...
The concentration of substrate X is low. What happens to the rate of the enzyme- catalyzed reaction if the concentration of X is doubled? 15. What effect does an increase in the enzyme concentration have on the rate of an enzyme-catalyzed reaction? 16.
Review your knowledge of how enzyme activity is affected by substrate concentration by selecting the correct...
Review your knowledge of how enzyme activity is affected by substrate concentration by selecting the correct statements concerning enzyme activity at low substrate concentrations. Contact between enzyme and substrate is rare Velocity of the reaction increases Enzyme makes product rapidly Enzyme makes product slowly Enzyme is saturated with substrate
2. We can measure how fast the Product is formed at increasing levels of Substrate Concentration...
2. We can measure how fast the Product is formed at increasing levels of Substrate Concentration The rate of the reaction can be plotted below. This is called a Michaelis-Menten Graph and it shows several important features of the enzyme: a. What happens to the reaction rate as the amount of substrate is increased? reaction rate- b. Why does the graph level off at high levels of substrate concentration? substrate concentration
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point...
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point where the enzyme is working at its maximum rate (Vmax/2), and amount of substrate needed to bind half of the active sites (Km). Label these points on the graph. Vmax represents: Vm Vmax/2 represents: Reaction velocity v Vmax 2 Km represents: Kim Substrate concentration (5)
how do I draw graph for this? collisions between ernzyme and substrate is tion rate. Sketch...
how do I draw graph for this?
collisions between ernzyme and substrate is tion rate. Sketch this relationship on the axes in Figure 6.5 and label both axes. Lab Topic 6: Enaymes 6-5 expected to increase the reac- Figure 6.5. Eflect of temperature on Teaction rate But heat energy has another effect in addition to speeding up the move- ment of molecules. It can also disrupt the delicate attractions between the chemical side groups of amino acids, causing the enzyme...
For the following questions, multiple answers may apply. 1) Enzyme activity in cells is controlled by...
For the following questions, multiple answers may apply. 1) Enzyme activity in cells is controlled by which processes: a) covalent modifications b) modulation of expression levels c) feedback inhibition d) binding to allosteric effectors 2) Which of the following statements about the concept of “induced fit” are true (2pts): a) Substrate binding induces either global or local conformational change in the enzyme, which then brings catalytic groups into proper orientation. b) When a substrate binds to an enzyme, the enzyme...
Part A Insert non-labeled graph from page 150 replica created and inserted below Rate ofrece with...
Part A Insert non-labeled graph from page 150 replica created and inserted below Rate ofrece with competitive inhibitor Substrate concentration The graph shows the normal reaction rate of an enzyme and the reaction rate when a competitive inhibitor is present. Which description below explains the appearance of the graph? As the substrate concentration increases, the activity of the enzyme decreases As the enzyme concentration increased, the effect of the inhibitor was more pronounced As the onzyme concentration increased the effect...
The graph below shows an enzyme- controlled reaction. The enzyme concentration is kept constant. At concentrations of substrate greater than X, which of the following statements is true? Rate of reaction 0 Concentration of substrate X The rate of reaction is limited by enzyme concentration. The rate of reaction tends towards zero. The substrate has an inhibitory effect. The products have an inhibitory effect.
Which of the diagrams illustrates the way in which the rate of an enzyme-controlled reaction depends on substrate concentration? * А B Rate of reaction MÚN Substrate concentration A B D When starch and amylase are mixed in the presence of iodine solution, the blue-black colour rapidly disappears. This is due to the formation of which molecule? * glucose O glycogen sucrose O maltose Which of the following enzyme groups can catalyse oxidation reactions? * O phosphorylases isomerases hydrolases dehydrogenases...
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...
The concentration of substrate X is low. What happens to the rate of the enzyme- catalyzed reaction if the concentration of X is doubled? 15. What effect does an increase in the enzyme concentration have on the rate of an enzyme-catalyzed reaction? 16.
Review your knowledge of how enzyme activity is affected by substrate concentration by selecting the correct statements concerning enzyme activity at low substrate concentrations. Contact between enzyme and substrate is rare Velocity of the reaction increases Enzyme makes product rapidly Enzyme makes product slowly Enzyme is saturated with substrate
2. We can measure how fast the Product is formed at increasing levels of Substrate Concentration The rate of the reaction can be plotted below. This is called a Michaelis-Menten Graph and it shows several important features of the enzyme: a. What happens to the reaction rate as the amount of substrate is increased? reaction rate- b. Why does the graph level off at high levels of substrate concentration? substrate concentration
3. The Michaelis-Menten Graph also shows the theoretical maximum rate of the enzyme (Vmax), the point where the enzyme is working at its maximum rate (Vmax/2), and amount of substrate needed to bind half of the active sites (Km). Label these points on the graph. Vmax represents: Vm Vmax/2 represents: Reaction velocity v Vmax 2 Km represents: Kim Substrate concentration (5)
how do I draw graph for this?
collisions between ernzyme and substrate is tion rate. Sketch this relationship on the axes in Figure 6.5 and label both axes. Lab Topic 6: Enaymes 6-5 expected to increase the reac- Figure 6.5. Eflect of temperature on Teaction rate But heat energy has another effect in addition to speeding up the move- ment of molecules. It can also disrupt the delicate attractions between the chemical side groups of amino acids, causing the enzyme...
Part A Insert non-labeled graph from page 150 replica created and inserted below Rate ofrece with competitive inhibitor Substrate concentration The graph shows the normal reaction rate of an enzyme and the reaction rate when a competitive inhibitor is present. Which description below explains the appearance of the graph? As the substrate concentration increases, the activity of the enzyme decreases As the enzyme concentration increased, the effect of the inhibitor was more pronounced As the onzyme concentration increased the effect...
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