Following is the - complete Answer -&- Explanation: for the first three sub-parts ( i.e. Sub- part : 1 to 3 ), of the given:
Question: in...typed & image format...
Answer:
Explanation:
Following is the complete: Explanation: for the above: Answer...
Following is the given: data set: slightly modified for building Lineweaver Burk plot: prepared by using MS Excel, presented....here, in....image format...
Where:
We know the following : Michaelis Menten equation:
1/ Vo = Km / Vmaxx ( 1/ [S] ) + 1/Vmax------------------------Equation - 1
Where:
Now, if we plot: 1/Vo vs. 1/[S] , according to Equation - 1, we will be getting the following : i.e.
Following is the graph: of 1/Vo vs. 1/[S] , prepared using MS Excel...presented in ...image format...
Linear Equation of the TrendLine: y = 2.696x + 8.151 -----------------------Equation - 2
We get:
Therefore:
Interpret the data above 1. What is the aporoximate Km and Vmax (units matter) 2.Briefly explain...
1-The unmutated form of your protein has a Km of 25 µM and a Vmax of 43 mM/s. The enzyme kinetic data for your enzyme with the amino acid substitution should now be displayed in the table above. Based on these data, explain the effect of amino acid substitution on the Km and Vmax for the mutated protein. (Up to 50 words) You are not expected to draw a Lineweaver-Burk plot, however a quick sketch of a Vi vs [S]...
2.) a. Given the following equation and using the Lineweaver-Burk equation find the Vmax and Km O y=7x+2.5 for enzyme A (in mM and s). b. Suppose you want to compare similar enzymes A (above Kcat=500) with enzyme B (Km=2.0, Kcat=450) to find out which enzyme has a higher catalytic efficiency; which enzyme has the higher catalytic efficiency?
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...
Given the following data (generated from a series of assays), what is the Km and Vmax for this enzyme? Include units and be careful of significant figures. [S], μM V(μM/min) 10.0 32.4 25.0 66.3 50.0 102 150.0 160 300.0 185
The value of Km for the shown data for a hexokinase-catalyzed reaction is with the unit of . The value of Vmax for. the same reaction is with the unit of . Be sure to give the values with the correct number of significant figures. You might have to construct a kinetic plot. For units, choose one answer from (uM, 1/ UM, HM/second, uM x second, mM, 1/mM, second, 1/second, mM/second, mM x second) vo (mM/sec) Glucose concentration (mm) 0.10...
10.What type of inhibitor is this? How do you know? (2) 11.For your assigned inhibitor 1, what are the apparent Km & Vmax? (NOTE: apparent Km& Vmax are just the Km & Vmax in presence of inhibitor, at a given concentration.) (2) Kinetics experiments were performed on PGI. Enzyme activity (initial velocity, Vo) was measured at varying concentrations of Glucose-6-phosphate (G6P). The enzyme concentration used in all experiments was 1.5 μM. 12.What will be the reaction rate with 0.500 mM...
1. The following kinetic data was generated for the Hst enzyme. The overall reaction for this enzyme is: OH ОН + NH3 NH2 All reactions are carried out in a final reaction volume of 2 mL with 0.1ug of purified Hst protein present at pH 7.8. The Hst protein has a molecular weight of 90 kDa based on estimates from gel filtration column chromatography and a molecular weight of 45 kDa based on estimates from denaturing SDS PAGE gel electrophoresis....
The key factor that controls the initial rate of an enzyme catalysed reaction (Vo) is the concentration of the substrate of the reaction ([S]). In Damon's Michaelis-Menten experiment, the highest concentration of substrate used was 500 UM. What do you think will happen to the reaction velocity if higher concentrations of substrate were used? Select one: a. Vo will reach a plateau at higher (S) values O b. Vo will increase exponentially as (S) is increased O c. Vo will...
need help with this question You set up an experiment to assess kinetic rate constants for enzyme X with substrates A and B. You use 10 M enzyme in all experiments. You may use excel or any other program to help you answer questions about enzyme X. Use the following set of data to answer the following questions: [A] AM Vo (uM/s) 500 MB 2.2 4.3 Vo (uM/s) 50 MB 0.8 0.5 - 9.8 11.6 13 al NONS 13.5 17....
12)Show work step by step 13)Show work step by step Below is BoX 6-1 if needed Applying the Michaelis-Menten Equation IV An enzyme is found that catalyzes the reaction X= Y Researchers find that the Kyn for the substrate A is 4 pm, and the keat is 20 min . (a) In an experiment, (X) = 6 mm, and the initial velocity, V, was 480 nm min!. What was the (E) used in the experiment? (b) In another experiment, (E)...