The maximum catalytic rate of an enzyme is defined as the turnover number (also called kcat)and...
The maximum catalytic rate of an enzyme is defined as the turnover number (also called kcat)and is the maximum number of reactions a single active site can carry out per second for a given concentration of enzyme.
i.Would a competitive inhibitor reduce the turnover number for an enzyme?Why?
ii.Would an irreversible inhibitor reduce the turnover number for an enzyme?Why?
Homework Answers
Turnover number Kcat = Vmax / ETotal
Competitive inhibitor does not reduce the turnover number for an enzyme because Vmax is not change in competitive inhibitor and it becomes constant with presence or absence of inhibitor. So, Turnover number also become same in both the condition.
In irreversible inhibitor reduce the turnover number for an enzyme because Vmax is decrease. So turnover number also low compare to absence of inhibitor.
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The maximum catalytic rate of an enzyme is defined as the
turnover number (also called kcat)and...
help with these please The turnover number is defined as the maximum number of substrate molecules...
help with these please
The turnover number is defined as the maximum number of substrate molecules that can be converted into product molecules per unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily equal to the concentration of enzyme molecules, because some enzyme molecules have more than one active site. If the enzyme molecule has one active site, the turnover number is given by turnover number = - -=k2 (Rmax is often written as...
enzyme has a molar mass of 30 kilodatons. From this information, calculate Keat for this enzyme-catalyzed...
enzyme has a molar mass of 30 kilodatons. From this information, calculate Keat for this enzyme-catalyzed reaction both with and without inhibitor. Also explain from the data given on the graph which type of enzyme inhibition any is curring Series 1 - no inhibitor. Series 2 inhibitor present • Seriesi Series2 Linear (Series1) Linear (Series2) Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is:...
Determine the value of the turnover number of the enzyme catalase, given that Rmax (Vmax) for...
Determine the value of the turnover number of the enzyme catalase, given that Rmax (Vmax) for catalase is 41 mmol · L-1.5-1 and [E]t equals 3.6 nmol · L-1. Catalase has a single active site. turnover number: 8-1
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...
high and detecting one product at a time Question 77 The initial velocity of an enzyme...
high and detecting one product at a time Question 77 The initial velocity of an enzyme reaction (vo) describes A) The concentration of the enzyme at maximal velocity B) The concentration of substrate at maximal velocity C) The concentration of both at the start of the reaction D) The rate of the reaction when the substrate and enzyme are first med Question 78 What is the shape of a typical plot of initial rate vs substrate concentration tres kinetics? A)...
2. hypothesize the best conditions (pH and temperature) under which the enzyme chymotrypsin functions with an...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
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)
6) Whale insulin could be distinguished seralogically from pig insulin in spite of identical primary sequence....
6) Whale insulin could be distinguished seralogically from pig insulin in spite of identical primary sequence. This is because: A) They were folded at different temperatures in the different species. B) They were folded using different chaperone proteins. C) They were folded as larger precursor proteins with differing primary structure D) The antibodies used were made from denatured insulin 7) Enzymes are potent catalysts because they A) increase the equilibrium constants for the reactions they catalyze B) lower the activation...
41. An enzyme-substrate complex forms when substrate binds to an enzyme at the enzyme's site. 42....
41. An enzyme-substrate complex forms when substrate binds to an enzyme at the enzyme's site. 42. An inorganic ion such as zinc or manganese that is needed for an enzyme to function is acting as a 43. Competitive inhibition of enzymes occurs when: site A) catalytic B) allosterie C) operative B) cofactor C) apoenzyme D) holoenzyme A) coenzyme A) the inhibitor binds to the active site of the enzyme B) the inhibitor binds to the allosteric site of the enzyme...
12. Which of the following statements is true of enzyme catalysts? A B C To be...
12. Which of the following statements is true of enzyme catalysts? A B C To be effective, they must be present at the same concentration as their substrate. They can increase the equilibrium constant for a given reaction by a thousand-fold or more. They lower the activation energy for conversion of substrate to product. Their catalytic activity is independent of pH. They are generally equally active on D and L isomers of a given substrate. D E 13. In competitive...
help with these please
The turnover number is defined as the maximum number of substrate molecules that can be converted into product molecules per unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily equal to the concentration of enzyme molecules, because some enzyme molecules have more than one active site. If the enzyme molecule has one active site, the turnover number is given by turnover number = - -=k2 (Rmax is often written as...
enzyme has a molar mass of 30 kilodatons. From this information, calculate Keat for this enzyme-catalyzed reaction both with and without inhibitor. Also explain from the data given on the graph which type of enzyme inhibition any is curring Series 1 - no inhibitor. Series 2 inhibitor present • Seriesi Series2 Linear (Series1) Linear (Series2) Chapter 8. Enzyme Regulation and Inhibition 1. Competitive inhibitors are always of which type? a) allosteric b) irreversible c) reversible d) suicide 2. DIFP is:...
Determine the value of the turnover number of the enzyme catalase, given that Rmax (Vmax) for catalase is 41 mmol · L-1.5-1 and [E]t equals 3.6 nmol · L-1. Catalase has a single active site. turnover number: 8-1
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...
high and detecting one product at a time Question 77 The initial velocity of an enzyme reaction (vo) describes A) The concentration of the enzyme at maximal velocity B) The concentration of substrate at maximal velocity C) The concentration of both at the start of the reaction D) The rate of the reaction when the substrate and enzyme are first med Question 78 What is the shape of a typical plot of initial rate vs substrate concentration tres kinetics? A)...
2. hypothesize the best conditions (pH and temperature) under
which the enzyme chymotrypsin functions with an appropriate
reference. also, hypothesize what will occur in the presence of an
inhibitor and the type of inhibition.
EXPERIMENT 5: ENZYME ACTIVITY WITH a-CHYMOTRYPSIN Prelab Assignment 1. Prepare a flow chart, covering one half of the experimental work (either part A and C if your lab bench is on the window side of the lab or part B and D if your locker is...
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)
6) Whale insulin could be distinguished seralogically from pig insulin in spite of identical primary sequence. This is because: A) They were folded at different temperatures in the different species. B) They were folded using different chaperone proteins. C) They were folded as larger precursor proteins with differing primary structure D) The antibodies used were made from denatured insulin 7) Enzymes are potent catalysts because they A) increase the equilibrium constants for the reactions they catalyze B) lower the activation...
41. An enzyme-substrate complex forms when substrate binds to an enzyme at the enzyme's site. 42. An inorganic ion such as zinc or manganese that is needed for an enzyme to function is acting as a 43. Competitive inhibition of enzymes occurs when: site A) catalytic B) allosterie C) operative B) cofactor C) apoenzyme D) holoenzyme A) coenzyme A) the inhibitor binds to the active site of the enzyme B) the inhibitor binds to the allosteric site of the enzyme...
12. Which of the following statements is true of enzyme catalysts? A B C To be effective, they must be present at the same concentration as their substrate. They can increase the equilibrium constant for a given reaction by a thousand-fold or more. They lower the activation energy for conversion of substrate to product. Their catalytic activity is independent of pH. They are generally equally active on D and L isomers of a given substrate. D E 13. In competitive...
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