11) What is the specificity constant (or enzymatic efficiency) of the 56 kDa enzyme, fumarase? It...
11) What is the specificity constant (or enzymatic efficiency) of the 56 kDa enzyme, fumarase? It has a Kcat of 9x103 (s-1), a Km of 3x10-7 (M), and you plan to use it at a concentration of 200 nM.
A) 1.6x108 (M-1 S-1)
B) 3x1010(M-1 S-1) This is the correct answer, why?
C) 1.5x10-2 (M-1 S-1)
D) 0.0018 (M-1 S-1)
E) 3.3x10-11 (M-1 S-1)
Homework Answers
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11) What is the specificity constant (or enzymatic efficiency)
of the 56 kDa enzyme, fumarase? It...
Please provide the correct answer Problem 36.16 11 of 14 > Part A The enzyme fumarase...
Please provide the correct
answer
Problem 36.16 11 of 14 > Part A The enzyme fumarase catalyzes the hydrolysis of fumarate: Fumarate(aq) + H2O(1) L - malate(aq). The turnover number for this enzyme is 2.5 x 10 s-4, and the Michaelis constant is 4.2 x 10" M. What is the rate of fumarate conversion if the initial enzyme concentration is 1.0x10-6 M and the fumarate concentration is 1.0x10-4 M ? Express your answer with the appropriate units. Ro = Value...
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a...
To determine the kinetic characteristics of an enzyme you used 1 nmol/L of enzyme in a series of assays where you measured the rate of reactions as you varied the concentration of substrate in each assay (Table A). Estimate from a Michaelis-Menten plot approximate values for Vmax, KM, Kcat, and the specificity constant for this enzyme and substrate. (The only information that is given is this paragraph and the table below). Table 1: [S] (μM) v (μmol/L/min) 0 0 5...
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...
please help!! please please "Looking at table 6-8 on Enzyme Reactions from the lecture, which achieves...
please help!! please please
"Looking at table 6-8 on Enzyme Reactions from the lecture,
which achieves an excellent specificity constant with a very
favorable kcat (insert answer here) , which with a
favorable Km (insert answer here) , and which with
moderate values for each (insert answer here) ?
(pick from acetyl cholinesterase, B-lactamase, and catalase)"
Question 2: "The units of Vmax are (insert answer
here) and the units of Km are (insert answer
here) (pick from M, M-1, M/s, s/M...
Please answer all of those questions 7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bo...
Please answer all of those questions
7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...
1) An experiment is run with enzyme E at a constant concentration of 1.00 nM. The...
1) An experiment is run with enzyme E at a constant concentration of 1.00 nM. The following data set was generated: Initial rate v, [SJ, μΜ μΜ/min 2.0 2.9 3.0 3.8 4.0 4.4 5.0 5.0 5.4 6.0 7.0 5.8 8.0 6.2 9.0 6.4 6.7 10.0 From these data, determine Vmax, KM, kcat and the turnover number. In a second series of experiment, the reaction was studied in the presence of 10mM of inhibitor A. The new data set is shown...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A↽−−⇀B. For substrate A,...
For her undergraduate project, Jessica studied an enzyme that catalyzes the reaction A↽−−⇀B. For substrate A, she determined that ?m=2.5 μM and ?cat=35 min−1. 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 Michaelis–Menten kinetics. 1)...
You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD...
You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD Previously, you determined that kcat = 400 s and Km = 10 M for your sample of happyase. Further research shows that this happyase sample was actually contaminated with a reversible inhibitor called ANGER. When ANGER is fully removed from the happyase preparation and [Eltotalis 4 nM, the measured Vmax is increased to 4.8 umes-1 and the measured Km is now 15 MM. Use...
a. what are the values of Vmax and Km in the abscence if the inhibitor what...
a. what are the values of Vmax and Km in the abscence if the
inhibitor what are the values of Vmax and Km in the presence of the
inhibitor?
b. what type of inhibition is it?
c. what is the dissociation constant (Ki) of the
inhibition?
***d. graph a linear scatter plot including equation.
Homework (CHE 407) The initial velocity for an enzyme-catalyzed reaction is measured at various initial substrate concentration [S]o, in the absence and in the presence of...
C370S19HW3 Name Please attach your plots to this sheet and turn in your work on Monday June 3 The enzyme urease...
C370S19HW3 Name Please attach your plots to this sheet and turn in your work on Monday June 3 The enzyme urease catalyzes the hydrolysis of urea. 1. (3) Write the reaction catalyzed by Urea below: 2. (2) Of the 7 classes of Enzymes, which type is urease? 3. The rate of this reaction was determined for a series of solutions in which the concentration of urea was changed while maintaining a fixed urease concentration of 3.0 HM. The following data...
Please provide the correct
answer
Problem 36.16 11 of 14 > Part A The enzyme fumarase catalyzes the hydrolysis of fumarate: Fumarate(aq) + H2O(1) L - malate(aq). The turnover number for this enzyme is 2.5 x 10 s-4, and the Michaelis constant is 4.2 x 10" M. What is the rate of fumarate conversion if the initial enzyme concentration is 1.0x10-6 M and the fumarate concentration is 1.0x10-4 M ? Express your answer with the appropriate units. Ro = Value...
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...
please help!! please please
"Looking at table 6-8 on Enzyme Reactions from the lecture,
which achieves an excellent specificity constant with a very
favorable kcat (insert answer here) , which with a
favorable Km (insert answer here) , and which with
moderate values for each (insert answer here) ?
(pick from acetyl cholinesterase, B-lactamase, and catalase)"
Question 2: "The units of Vmax are (insert answer
here) and the units of Km are (insert answer
here) (pick from M, M-1, M/s, s/M...
Please answer all of those questions
7. Which of the followings is correct about the mechanisms of enzymatic reactions? General acid-base mechanism b. Metal elements mediated mechanism a. Covalent bonding mediated mechanism d. All above c. e. None a bove Which of the followings is correct about the meaning of the constant (Km) of Michaelis-Menten equation of enzyme catalyzed reactions? a. The constant and Michaelis-Menten equation is applicable only to the stage of reaction immediately after mixing of substrate(s) with...
1) An experiment is run with enzyme E at a constant concentration of 1.00 nM. The following data set was generated: Initial rate v, [SJ, μΜ μΜ/min 2.0 2.9 3.0 3.8 4.0 4.4 5.0 5.0 5.4 6.0 7.0 5.8 8.0 6.2 9.0 6.4 6.7 10.0 From these data, determine Vmax, KM, kcat and the turnover number. In a second series of experiment, the reaction was studied in the presence of 10mM of inhibitor A. The new data set is shown...
You are still interested in the enzyme happyase, which catalyzes the following reaction: HAPPY = SAD Previously, you determined that kcat = 400 s and Km = 10 M for your sample of happyase. Further research shows that this happyase sample was actually contaminated with a reversible inhibitor called ANGER. When ANGER is fully removed from the happyase preparation and [Eltotalis 4 nM, the measured Vmax is increased to 4.8 umes-1 and the measured Km is now 15 MM. Use...
a. what are the values of Vmax and Km in the abscence if the
inhibitor what are the values of Vmax and Km in the presence of the
inhibitor?
b. what type of inhibition is it?
c. what is the dissociation constant (Ki) of the
inhibition?
***d. graph a linear scatter plot including equation.
Homework (CHE 407) The initial velocity for an enzyme-catalyzed reaction is measured at various initial substrate concentration [S]o, in the absence and in the presence of...
C370S19HW3 Name Please attach your plots to this sheet and turn in your work on Monday June 3 The enzyme urease catalyzes the hydrolysis of urea. 1. (3) Write the reaction catalyzed by Urea below: 2. (2) Of the 7 classes of Enzymes, which type is urease? 3. The rate of this reaction was determined for a series of solutions in which the concentration of urea was changed while maintaining a fixed urease concentration of 3.0 HM. The following data...
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