![VO vs [S] 0.0000014 y -0.0698x2 +0.0006x- 2E-08 0.0000013 0.0000012 0.0000011 0.000001 0.0000009 vo 0.0000008 Series2 0.00000](http://img.homeworklib.com/questions/9059cb00-6e5d-11ea-a25c-e95514bcafac.png?x-oss-process=image/resize,w_560)
| What is the Vmax and Km on this graph for both lines? |
This is not the best plot for determining Vmax and KM. A Lineweaver-Burke plot would be better. But still, these values can be approximated from them
Vmax is the highest rate the reaction can reach. For the blue line, the value seems to be around 0.0000013 (you have not used units in your graph, but whichever are your units for rate). KM is defined as the substrate concentration that results in a rate the is half the Vmax. In this case, half of Vmax would be 0.00000065, and the concentration corresponding to that value is, apporximately, 0.0015 (concentration units are not given). Please bear in mind that this is a very wide approximation, because the x axis is not divided in many values.
For the orange curve, the Vmax seems to tend to 0.00000045 and KM would be the concentration of substrate corresponding to a rate of 0.000000225, which is approximately 0.003.
What is the Vmax and Km on this graph for both lines? VO vs [S] 0.0000014...
Show mathematically how a value for KM can be obtained from the v0 vs S0 graph when v0 = ½ Vmax
1. Show, using the Michaelis-Menten equation, that when [S] >>> Km, vo = Vmax. Show, using the M-M equation that when [S] <<<Km, vo =[S][Et]kcat/Km. 2. What is Vmax? Provide both a mathematical and written description of Vmax? How can Vmax be experimentally altered? How can we use Vmax to determine the turnover number (kcat) of an enzyme-catalyzed reaction? What is the major challenge of determining Vmax from an Michaelis-Menten plot?
Nobody has been able to solve the Km. The Vmax values are
correct. I believe I have my graph wrong. Can someone please help
me solve this.
Using the Lineweaver-Burk Equation 1/Vo Km/Vmax[S]1/Vmax) create a graph of both the Non-Inhibited data and Inhibited data below (on the same graph axes) and calculate the KM and VMax for each line. Vo (umol/L.min) Vo (Hmol/L-min) [Sol (umol/L) Non-Inhibited Data Inhibited Data .00e-06 13.9 7.60 .00e-06 18.0 9.90 ..10e- 05 10e-05 26.0 14.8...
The equation that describes the above Michaelis-Menten curve: Vo TS]+K Vmax [S] Michaelis-Menten Equation Lineweaver and Burke manipulated the Michaelis-Menten equation to yield: Ko V I S Vmax [S] Lineweaver-Burke Equation Linewenver Burke Equation If you plot 1/ V. vs. 1/[S], you get the following Lineweaver-Burke plot: 1/V. Slope = km/Vmax Intercept = -1/KM -Intercept = 1/Vmax 1/[S] Which is easier to calculate values for Km and Vmax, using the linear (y=mx+b) Lineweaver-Burke Plot or the Michaelis-Menten curve?
Kcat =30.0 s-1
Km= 0.005 M
Operating at 1/4 Vmax
What is [S] ?
The solutions manuel doesn't explain the problem well. Whete
does the 0.33 km come from?
For part 2 : Plug in [S]= 1/2 Km, 2 Km, and 10 Km
Where does the 1.5 Km come from?
Answer (a) Here we want to find the value of [S] when Vo = 0.25 V max. The Michaelis-Menten equation is V = Vmax[S]/(Km + [SD so V = Vmax...
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...
21. For the L-8 graph below, what is the Km and Vmax for this enzyme? ◆ Series! Linear (Series1) y=1229·4x + 2.9701 ﹁ -0.005 0.005 L-DOPA]
12. From the Lineweaver-Burk graph given: a. What are the Km and Vmax for the uninhibited case? b. What type of inhibition is occurring? c. Shown on the page after the Lineweaver-Burk plot are semi-qualitative sketches for three V vs. (S) plots. Which one of these most likely corresponds to this particular experiment (A,B or C)? Scani explain th Cant catimer IIIIIIIII IIIIIIIII - -- | - | IIIII We were unable to transcribe this image
please graph all 3 lines and explain the
vmax&km
How to: Lineweaver Burke 1. The following data was determined for an enzyme in the absence of an inhibitor and in the presence of two different inhibitors (V2 and V3). Determine the V. and K for the enzyme (1) Plot the data and determine the type of inhibition for each inhibitor (S) mm 1 V2 4.3 5.5 V1 12 20 29 2 relliate 150b
a. What is the Km and Vmax for PFK1 when treated with OmM (represents control for enzymatic activity) or with 5mM AMP Show work on the graph draw lines for Vmax and Km. Control: Vmax (AMP), 0.32 0.28 0.2 Km 0.24 0.20 (s)-FTY20 (20LM): 0.18 Vmax 0.12 0.08 0.04 Km 0.00 Fructose-6-phosphate (mM) b. Fructose-6-phosphate is the substrate of the reaction. Based on answer in "a", what type of regulation occurs with and what site on PFK1 is AMP likely...