Put the following steps in order to generate a MM Graph. Some steps may be unnecessary.
Michaelis Menten equation depicts the best known model for kinetics of enzyme catalyzed reaction.
Thus, at [S] = Km, Vo will be
equal to half of Vmax i.e, half of the enzyme molecules are bound
to substrate molecule.
When the reaction is at Keq, it is at steady state where rate of formation of Enzyme Substrate (ES) complex is equal to the rate of is equal to the rate of decomposition of ES.
Increasing [E], will affect Vmax of a reaction at a given substrate concentration. But is not applicable to MM kinetics as in MM equation it is assumed that [S] >> [E] .
Put the following steps in order to generate a MM Graph. Some steps may be unnecessary....
pls help
Question 7 5 pts Put the following steps in order to generate a MM Graph. Some steps may be unnecessary. Step 1 [Choose ] [Choose] Step 2 Keep measuring vo at different [S], till [S]n Measure vo at [S]1 Step 3 Keep measuring v0 at a given [S], till [E]n Keep measuring [P] at a given time at different [S], till [S]n Step 4 Plot vo vs [S] Measure [P] at a given time for [S]2 Measure v0...
Can someone please help with the steps for forming a
Michaelis-Menten graph? My professor said there are only 3 and step
4 is unnecessary.
Question 7 5 pts Put the following steps in order to generate a MM Graph. Some steps may be unnecessary. [ Choose ] Measure vo at [S]1 Keep measuring vO at a given [S], till [E]n Measure vo at [S]2 Measure [P] at a given time for [S12 Measure [P] at a given time for [S]1...
Which statement about enzyme catalysis is false? All of the active site amino acids are next to each other in the primary sequence. Enzymes speed up reactions by forming specific non-covalent bonds between the enzyme amino acids and the transition state molecule. Some enzymes require other molecules, called cofactors, to carry out chemical reactions. Generally, the most important amino acids for an enzyme's function are those in the active site. Question 6 1 pt When [S] is much more than...
A. Choose anly one correcet answer for each of the following questions (4 pts cach). AL Some and KM values are shown below for enzyme-substrate pairs. Which of the following enzymes is most efficient in converting the substrate into the product? b) kes.-4x10s s", KM-0.026 M d)k,,-5.7 x1o's", K-2x10s M c)人at-900 s", KM-2.5 × 10.5 M A2. Which of the following enzyme reaction mechanisms has multiple substrates? a) induced-fit e) Michaclis-Menton b) random sequential d) reversible covalent modification e) None...
biochemistry
if you could please help me answer the following questions!
741) (5 pts) Transition state theory relates the rate constant to the free energy of activation, AG. How can enzymes reduce the activation energy barrier? a) decrease the free energy of the product b) high affinity binding to the transition state c) increase the free energy of the substrate d) increase entropy upon release of product e) bind to the substrate with high affinity 2) (5 pts) Which is...
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 different experiment yields the following kinetic data Substrate] (mM)Vo (uM/min) no inhibitorVo (uM/min)+7 nM inhibitor 0.02 0.04 0.10 0.25 1.00 2.50 0.8 2.9 8.6 24 36 50 Plot the data for the kinetics of the enzyme (with and without the inhibitor) in a double reciprocal (Lineweaver-Burk) plot. Keep in mind that the x axis is 1/[S] and the y axis is 1/Vo. If you are using Excel you want to choose the (x,y) scatter plot (without a ne). You...
biochemistry
if you could please help me answer the following questions!
* 1. (5 pts) Which of the following is a catalytic mechanism utilize by enzymes? Multiple answers may be correct. Select all that are correct. 1. Acid-base a) acid-base catalysis d. metal-ion catalysis 12. Covalent b covalent catalysis e. transition state binding c. heterogeneou 3. Metalion . Proximin onentation, E 2. 76 pts) What is the "steady-state" assumption in the derivation of the s.clectrosch? Tynsin Michaelis-Menten equation? Sie binding...
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,...
ENSC 102-Problem Set #7 Due at the beginning of class on Friday, May 30 Answer each of the following questions in your own words and using your own calculations. For worked problems remember to explain any intermediate steps or assumptions, show all units, and box your final answers. For fu possible credit, make sure your finished work is legible, prepared on loose-leaf paper and shows your name and your lab instructor s name at the top of the first page...