Write the enzyme model for chymotrypsin acting on PNPA. Which step must be the slowest in order to see pre-steady state burst kinetics? Why did you not see a burst of product formation in the experiment described above?
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Q: kąk4 k2k1 E +S → ES → E + P (Vmax,f\ rax.f (Vmax,b [P] KM.f KM.b [S] [P] Vo 1+ KM.f Кмь KM,b ||
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- A student performed an enzyme inhibition reaction to experimentally determine the inhibitor constant of the EI complex using Dixion plot. i. The student setup two sets of experiments. Each set contained increasing concentrations of inhibitor, constant concentration of substrate and constant concentration of Alkaline phosphatase. ii. Set 1 contained lower concentration of substrate than set 2. iii. After mixing everything, he let the reaction happen for 15 minutes and measured the absorbance. iv. Then he plotted 1/v Vs 1/[I] - What error led to an unexpected graph? A) He is supposed to change the [S] within the set. B) He was not supposed to let the reaction happen for 15minutes before measuring the absorption C) He was not supposed to change the enzyme concentration within the set D) he made no errors E) his choice of X and Y axis are incorrectIn lab 4, you calculated cholesterol levels of a sample directly based on the absorbance ratio of the sample to standard. What assumption are we making for this calculation to be accurate? O All the cholesterol in the sample is unesterified (i.e. free cholesterol). There is a linear relationship between the cholesterol concentration of the sample and the absorbance of the sample. The enzymatic reaction goes to completion, i.e. all substrates are converted to products. The HDL and LDL in the sample have different absorption maxima as compared to the cholesterol.Given this, if you used 6g of vitamin Z powder to make 20 ml of solution, what is the % concentration of this solution? (I gave the image since I don't know if that info is needed to solve this question.)It also gives a follow-up, if you can help here too: You work in a lab as a summer student. One of your tasks is to make sure that there is enough cell culture medium containing antibiotics to grow bacteria. One day you realize that there is only 5 ml of 10% Antibiotic stock solution in the freezer. You decide to use it all to prepare the working culture medium with 0.01% antibiotic. In the lab there is plenty of growth medium without antibiotics. (Note: dilution in medium is like dilution in water). You remember the equation to make dilutions of stock solutions. You usually use this formula to calculate the required volume of a stock solution, but you realize it can apply here as well, even though the unknown is the final volume. So, you make that dilution. Given that each bacterial…
- Which of the following statement on the process of enzyme production is false? Select one: a. Agglomeration is sometimes used to increase solubility of enzyme powder b. After fermentation, intracellular enzymes can be directly extracted by filtration c. Spray drying can be used to dry the enzyme products into powder forms d. Chromatography is used to purify the enzyme producedLysozyme and benzonase are included in the lysis buffer, given that these are enzymes, one might not see bands for them on electrophoresis gel (SDS PAGE), why?Show the calculations required to make up 250mlof a stock solution of this chemical that will then be at the working concentration when 1 volume of this solution is added to 10 volumes of cell culture medium.
- In an experiment where you use different concentrations of avocado catalase to determine how that affects rate of the reaction with its substrate, hydrogen peroxide, why was the amount(concentration) of peroxide kept the same for all tubes? Why was the total volume of every tube 10cm?An enzyme catalyzes the reaction M-N. The enzyme is present at a concentration of 0.0000000022 M, and the Vmax is 0.0000028 Ms1. The Km for substrate is 5.5 µM. Calculate kcat-1. Which medium would you consider to be “complex” and which “defi ned”? Which is “rich” and which is “minimal”? Explain your answers. 2. Given that polyurethane is a huge polymer (MW >>100,000 Daltons), why is it important that thepolyurethanase is a secreted enzyme? If we assume that the polyurethane is the source of energy for the organism, how can material (carbon atoms) from it fi nd its way into the central metabolic pathways ofthis microbe? What is the “entry point”? What happens after its entry into the metabolic pathway?
- Use the data from the table below to answer the questions on an ezyme obtained from potato extract. The greater the absorbance value, the more product generated for each chemical reaction Table 1: Summary Data for Enzyme Catalyzed Reaction Product Formation Measured as Absorbance Tube Distilled Water Catechol PTU (Inhibitor) Potato Extract Results (Absorbance) 1 5.5 ml 0.5 ml -- --- 0.02 2 5 ml 0.5 ml --- 0.5 ml 0.68 3 4.5 ml 0.5 ml 0.5 ml 0.5 ml 0.04 4 4.5 ml 0.5 ml 1.0 ml 1.26 5 4.5 ml 1.0 ml 0.5 ml 1.22 a) Explain with respect to enzyme activity why test tube 1 produced very little absorbance: b) Explain with respect to enzyme activity why test tube 3 produced very little absorbance: c) Explain how to tubes 4 and 5 differ with respect to reaction conditions. d) Explain with respect to enzyme activity why tubes 4 and 5 have similar absorbance and why both have…The kinetics of this novel amylase were observed using lz in KI indicator to track the amount of starch at t-O min and t-1 min. They set up the following tubes and measured the absorbance after 1 minute of incubation. The reaction was stopped with HCl and 5 ml of Iz in KI indicator was added. One ml of each was used as sample in the spectrophotometer. Table 3. Calibration Curve Test tube Concentration of stock starch, mg/mL Volume of starch solution, ml Volume of distilled water, mL Volume of I, in Kl solution, mL Absorbance 1 10 0.0009 2 10 0.4 4.6 5 0.3306 3 10 0.8 4.2 5 0.5891 4 10 1.2 3.8 5 0.8409 15 10 1.6 3.4 1.0885 16 10 2.0 3.0 5 1.2572Consider the following enzyme cartoons or structures carefully. Note active sites, presence of cofactors, substrates, etc. and then answer the following questions with the applicable numbers 1, 2, 3, 4, None or All. More than one number may apply. 3. 2. 1. GO Substrate Enzyme Substrate Enzyme Pepsin Enolase a. Example(s) of an allosteric enzyme b. Example(s) of a proteolytic enzyme c. Example(s) of an enzyme(s) with cofactor(s) e. Example(s) of an enzyme(s) that could be impacted by an irreversible competitor. d. Example(s) of an enzyme(s) with a second site for feedback control. f. Enzyme(s) definitely composed of two or more protein chains.