![alculate the value Vo if an enzyme has Km=5.4 x 104. V max=484M/min and [S] = 0.001M 2. Meutral sphingomyelinase 2 converts s](http://img.homeworklib.com/questions/9f96c980-e5af-11eb-a0f3-bba9ce8d962b.png?x-oss-process=image/resize,w_560)
Homework Answers
1) according to Michelis Menten equation
Vo=( Vmax X S)/ (Km+S)
Vo=(48uM/secx1000uM)/(5.4x10-4M+0.001M)
Vo= 48x103uM2/sec/15.4x10-4M
Vo=48x103uM2/sec/1540uM
Vo= 48000/1540 uM/sec
Vo=31.16 uM/sec
2) Vo= (Vmax X S )/ (Km+ S)
6um/sec= 35um/sec X 3x10-5M/(Km + 3X10-5 M)
Km + 3x10-5 M =17.5x 10-5M
Km=14.5x10-5M
Km=145uM
Hope it's clear..thanks
Add Answer to:
alculate the value Vo if an enzyme has Km=5.4 x 104. V max=484M/min and [S] =...
1. An enzyme has a km of 4.7 X 105M. If the Vmax of the preparation...
1. An enzyme has a km of 4.7 X 105M. If the Vmax of the preparation is 224M/min, what velocity would be observed in the presence of 2 X 10^M substrate and 5 X10+M a competitive inhibitor. Ki is 3 X 10^M. What is the degree of inhibition? (10pts)
Refer to the below Enzyme activity data (Table 4) to determine the following: (1.5 pts each) a) V...
Refer to the below Enzyme activity data (Table 4) to determine the following: (1.5 pts each) a) Vmax b) why is the velocity v constant at [S] greater than 2 x 10-3 M? c) what is the free [E] at [S] = 2 x 10-2 M? 2. SI (mol/L 2 x 10-l 2 x 10-2 2 x 10-3 2 x 104 5 x 10-4 1,3 x 10-5 ol/min 60.00 60.00 60.00 48.00 45.00 2.00 Table 4. Enzyme activity assay data...
The following data were recorded for the enzyme-catalyzed reaction. Substrate concentration (M) 6.25 x 100 7.50...
The following data were recorded for the enzyme-catalyzed reaction. Substrate concentration (M) 6.25 x 100 7.50 x 10 1.00 x 10-4 1.00 x 10-3 Reaction velocity (nM/min) 15 56 60 75 (1) Estimate Km and Vmax- (2) What would V be at S=2.5 x 10-5 ?
1. an enzyme is observed to approach an initial velocity of 0.1M/s as more and more...
1. an enzyme is observed to approach an initial velocity of
0.1M/s as more and more [S] is added to the reaction. additionally
when V0 is equal to 0.05 M/s [S] is equal to 0.6 M. based on this
information what is Vmax and Km?
2. If a psrticular enzyme has a Vmax of 0.4 M/s, and a Km of
20 mM, what is V0 wjen [S] = 0.8 M?
3. We have discussed which amino acids chymotrypsin cleaves
at,...
Interpret the data above 1. What is the aporoximate Km and Vmax (units matter) 2.Briefly explain...
Interpret the data above
1. What is the aporoximate Km and Vmax (units matter)
2.Briefly explain how you found each
3.if you used 0.020 microM enzyme in your studies, what is
kcat in units of s^-1? Show your work units matter
4. Does this enzyme appear to display cooperativity? Explain
how you came up to that conclusion.
Directions: Below are data from 4 separate experiments that you must analyze/evaluate. Using the information from all 4 experiments, you must then propose...
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...
e) y_3cos(x +4) +4 MaxMinAmp riod f y 5 cos 2n(x -0.5)+5 V.T Max Amp Min AC SİNE function has a maximu m value o...
e) y_3cos(x +4) +4 MaxMinAmp riod f y 5 cos 2n(x -0.5)+5 V.T Max Amp Min AC SİNE function has a maximu m value of 4, aminimum value of 2, a phase shift of 1 rad to the right, and a period of 4. Write an equation for the function and graph the function [KU, 6m] 2. Min _Armp period. P.S V.T. . Equation 3. Determine the equation for the following a) COSINE function Equation b) SINE function Equation 4....
Based on the document below, 1. Describe the hypothesis Chaudhuri et al ids attempting to evaluate;...
Based on the document below,
1. Describe the hypothesis Chaudhuri et al ids attempting to
evaluate; in other words, what is the goal of this paper? Why is he
writing it?
2. Does the data presented in the paper support the hypothesis
stated in the introduction? Explain.
3.According to Chaudhuri, what is the potential role of thew
alkaline phosphatase in the cleanup of industrial waste.
CHAUDHURI et al: KINETIC BEHAVIOUR OF CALF INTESTINAL ALP WITH PNPP 8.5, 9, 9.5, 10,...
82.6 642 6.40 - 57 5.4 R0.8 MAX 28.6 035 28.4 #51 3 45 ф100 R3 #8.5 M10 X 1.5-6H 45 4X 10.5 NOTE:...
82.6 642 6.40 - 57 5.4 R0.8 MAX 28.6 035 28.4 #51 3 45 ф100 R3 #8.5 M10 X 1.5-6H 45 4X 10.5 NOTE: ALL DIMS IN mm ーAX 90. GRAY IRON FIN. DIMS i02 UNFİN, DIMS 최 ANGLE ±0° 30' FLANGED HUB 31A059 2 Refer to drawing 31A059 to answer the following questions. the units of measurement in (a) inches, (b) millimeters, or (c) centimeters? 2. Is the section view a (a) half-section or a (b) full section? what...
1. An enzyme has a km of 4.7 X 105M. If the Vmax of the preparation is 224M/min, what velocity would be observed in the presence of 2 X 10^M substrate and 5 X10+M a competitive inhibitor. Ki is 3 X 10^M. What is the degree of inhibition? (10pts)
Refer to the below Enzyme activity data (Table 4) to determine the following: (1.5 pts each) a) Vmax b) why is the velocity v constant at [S] greater than 2 x 10-3 M? c) what is the free [E] at [S] = 2 x 10-2 M? 2. SI (mol/L 2 x 10-l 2 x 10-2 2 x 10-3 2 x 104 5 x 10-4 1,3 x 10-5 ol/min 60.00 60.00 60.00 48.00 45.00 2.00 Table 4. Enzyme activity assay data...
The following data were recorded for the enzyme-catalyzed reaction. Substrate concentration (M) 6.25 x 100 7.50 x 10 1.00 x 10-4 1.00 x 10-3 Reaction velocity (nM/min) 15 56 60 75 (1) Estimate Km and Vmax- (2) What would V be at S=2.5 x 10-5 ?
1. an enzyme is observed to approach an initial velocity of
0.1M/s as more and more [S] is added to the reaction. additionally
when V0 is equal to 0.05 M/s [S] is equal to 0.6 M. based on this
information what is Vmax and Km?
2. If a psrticular enzyme has a Vmax of 0.4 M/s, and a Km of
20 mM, what is V0 wjen [S] = 0.8 M?
3. We have discussed which amino acids chymotrypsin cleaves
at,...
Interpret the data above
1. What is the aporoximate Km and Vmax (units matter)
2.Briefly explain how you found each
3.if you used 0.020 microM enzyme in your studies, what is
kcat in units of s^-1? Show your work units matter
4. Does this enzyme appear to display cooperativity? Explain
how you came up to that conclusion.
Directions: Below are data from 4 separate experiments that you must analyze/evaluate. Using the information from all 4 experiments, you must then propose...
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...
e) y_3cos(x +4) +4 MaxMinAmp riod f y 5 cos 2n(x -0.5)+5 V.T Max Amp Min AC SİNE function has a maximu m value of 4, aminimum value of 2, a phase shift of 1 rad to the right, and a period of 4. Write an equation for the function and graph the function [KU, 6m] 2. Min _Armp period. P.S V.T. . Equation 3. Determine the equation for the following a) COSINE function Equation b) SINE function Equation 4....
Based on the document below,
1. Describe the hypothesis Chaudhuri et al ids attempting to
evaluate; in other words, what is the goal of this paper? Why is he
writing it?
2. Does the data presented in the paper support the hypothesis
stated in the introduction? Explain.
3.According to Chaudhuri, what is the potential role of thew
alkaline phosphatase in the cleanup of industrial waste.
CHAUDHURI et al: KINETIC BEHAVIOUR OF CALF INTESTINAL ALP WITH PNPP 8.5, 9, 9.5, 10,...
82.6 642 6.40 - 57 5.4 R0.8 MAX 28.6 035 28.4 #51 3 45 ф100 R3 #8.5 M10 X 1.5-6H 45 4X 10.5 NOTE: ALL DIMS IN mm ーAX 90. GRAY IRON FIN. DIMS i02 UNFİN, DIMS 최 ANGLE ±0° 30' FLANGED HUB 31A059 2 Refer to drawing 31A059 to answer the following questions. the units of measurement in (a) inches, (b) millimeters, or (c) centimeters? 2. Is the section view a (a) half-section or a (b) full section? what...
Most questions answered within 3 hours.
-
A fast food meal has 5660 kJ of energy. A person uses energy at
a rate...
asked 3 minutes ago -
The pKb for a generic amine(R-NH2)) in
aqueous solution is 6.30. What is its pKa?
asked 4 minutes ago -
The following reactions have the indicated equilibrium constants
at a particular temperature: N2(g) + O2(g) ⇌...
asked 7 minutes ago -
Please Help ASAP.
1Consider the below code which iterates over a linked
list of n nodes...
asked 23 minutes ago -
Determine the air to fuel ratio of:
Canadian natural gas, with 93.9% methane, 4.2% ethane, 0.3%...
asked 23 minutes ago -
A manufacturer of power tools claims that the average amount of
time required to assemble their...
asked 25 minutes ago -
"electron-withdrawing substituents on carbon encourage back
donation", then on the next page he says that "greater...
asked 37 minutes ago -
On December 31, 2016, the shareholders’ equity section of the
balance sheet of R & L...
asked 45 minutes ago -
16.7
At t=0s a small "upward" (positive y) pulse centered at x = 5.0
m is...
asked 58 minutes ago -
Twitter Users and News: A poll conducted in 2013 found that 52%
of U.S. adult Twitter...
asked 1 hour ago -
How
would I know whether a given amino acid has an ionizable group or
not? please...
asked 1 hour ago -
True or false?
True False The function of the enzyme acyl CoA
synthetase is the ATP-dependent coupling...
asked 1 hour ago