I. An enzyme is what type of organic compound? II. What four elements are part of this organic compound? В. А. ch I. Is this compound alive? II. Why or why not? С. What environmental factors affect the activity of an enzyme? I. Do you have any enzymes inside your body? II. If yes, tell me about your favorite one. D.
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- QUESTION 6 Which of the following statements are true about enzyme inhibitors? QUESTION 6 Which of the following statements are true about enzyme inhibitors? A. Competitive inhibitors cause the slope of the Lineweaver-Burk line to change but not the y-intercept. B. Noncompetitive inhibitors are a type of mixed inhibitors. C. Uncompetitive inhibitors result in an alpha equal to 1 and an alpha' not equal to 1. D. Noncompetitive inhibitors result in lines with increasing [I] to share the same x-intercept. all of the above E. All of the above are true.a) what happens if an enzyme is not made correctly? b) what is the function of the major RNA is it proteins synthesis? c) what is the primary source of all glucose, and why is it such an important monosaccharide?You need to include its molecular formula. d) when you react ammonia with a halogenated alkane will you get only one organic product? Why or why not? (do not talk about inorganic products) e) emulsifiers are pretty important compounds for daily life, externally and internally to us humans. Describes the two parts of an emulsifier molecule, and how most emulsifiers work and what they actually do. f) consider the ring structure of B-D glucose. it will give a positive test as a reducing sugar. Describe how that can happen in a pH=7 solution such as fehlings'?47. Which of the following is true under the following conditions: The enzyme concentration is 5 nM, the substrate concentration is 5 mM, and the KM is 5 mM. (1 nM = 10-9 M, 1 μM=10-6 M, 1 mM = 10-3 M) Group of answer choices Between 0% and 50% of active sites have substrate bound 0% of active sites have substrate bound 50% of active sites have substrate bound 100% of active sites have substrate bound Between 50% and 100% of active sites have substrate bound
- A biochemist discovers and purifies a new enzyme, generating the purification table below. (a) From the information given in the table, calculate the specific activity of the enzyme after each purification procedure.(b) Which of the purification procedures used for this enzyme is most effective (i.e., gives the greatest relative increase in purity)?(c) Which of the purification procedures is least effective?(d) Is there any indication based on the results shown in the table that the enzyme after step 6 is now pure? What else could be done to estimate the purity of the enzyme preparation?The image shows the rate of an enzyme reaction under conditions of no inhibition, competitive inhibition, and noncompetitive inhibition as reactions labeled uninhibited, A, and B. Which of the following best explains what has occurred in the enzyme reactions? Reaction B shows competitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows noncompetitive inhibition, where increased substrate competes with inhibitors for the active site. Reaction A shows competitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor. Reaction B shows noncompetitive inhibition, where increased substrate does not affect the enzyme’s binding with the inhibitor.Which feature of an enzyme, distinct from non-enzyme proteins, relates specifically to their catalytic activity? Question 2 options: Stereospecific High specificity Rate enhancement Ability to be regulated
- Given: Your professor gives you a vial of enzyme and a vial of substrate. The product of this reaction is fluorescent and you can measure the concentration of the product as a function of time. (answer a, b, and c)a) Your professor tells you to quantify how much product is being produced per minute at thebeginning of the experiment. What exactly are you measuring?b) On the same plot, show the kinetic curve for an increased quantity of enzyme. Assume a 2x concentration. Indicate Km and Vmax.c) You don’t have a computer hand. Sad. How can you plot the data such that you can get important Michaelis-Menten values?Essay: In your own words explain the following concept in not more than 5 sentences a. The lock and key model for enzyme activity b. Relationship of substrate and enzyme concentration to enzyme activity c. importance of blotting technology d. factors that can affect the donnan equilibriumwill UPVOTE!Kindly answer the following questions. What is an enzyme? How enzymes are being classified and enumerate its classification? How enzymes determine their substrate? What are the factors that affect enzyme activities?
- Which of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that applyWhich of the following statements about Km is false? The km for a substrate will vary depending on the conditions of the reaction The km is equal to ½ vmax The kcat of a reaction will vary as it is equal to Vmax/km Km reflects the stability of the enzyme-substrate complex Both B and C are false Both A and C are false Not sure if 5 or 6 is correct1. Make a Lineweaver-Burk plot and use the plot to complete the information in the table and the following questions. a. Is it possible for the enzyme to overcome the effect of the inhibitor in question from the chart. Explain. b. What prevents this enzyme from being an even more catalytically efficient enzyme? c. What do single molecule data indicate about the validity of ensemble data?d. What is the reason that humans are insensitive to sulfa drugs?