Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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- For the following problem indicate the values for each part of the equation and solve for the unknownvalue:Peter adds 200 μL of bacteria to a tube containing 2 mLs of nutrient broth and then adds 300 μL of acertain disinfectant. The final concentration of the disinfectant in this tube after adding it is 5%.C1=C2=V1=V2=arrow_forwardSUBSTRATE CONCENTRATION [S] µM INITIAL VELOCITY V0 s-1 10 0.13 25 0.27 50 0.45 100 0.65 150 0.77 200 0.85 300 0.94 500 1.03 (i) a) Construct an empty table with the following column headings: Substrate concentration [S] and initial velocity (Vi) where [S] has the unit µM, and Vi has the unit mM/s. (ii) The table provided is the enzyme kinetic data for your mutated enzyme, whereby Vi was expressed using the unit ∆A(405 nm)/s. Using the standard curve, express Vi with the unit mM/s rather than ∆A(405 nm)/s. Place your answer in the table above alongside the appropriate [S]. Hint: To answer this question you need to use this standard curve equation=0.0419x (The slope of the line is= 0.0419) (iii) 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, what is Vmax? Km? and…arrow_forwardYou are given a pure protein sample to characterize and provided the following information: Its molar extinction coefficient, ε280, is 0.25 liters micromole-1 cm-1 in both the folded and unfolded form Its ΔGo for unfolding is 1.5 kcal/mol at 37o (where RT = 0.59 kcal/mole) A) Using a 0.5 cm pathlength cell, you measure the absorbance at 280 nm of a 20-fold dilution of your pure protein in solution (by this, we mean that 50 ul of the protein sample was diluted to a final volume of 1 ml) and find A280 = 0.40. What is the original concentration of the protein before dilution? B) What is the concentration of the unfolded form of the protein in your sample?arrow_forward
- o NB4: Why do you think you first had to make the 1 mM solution instead of working directly from the stock solution?arrow_forwardWhat is the optimal substrate concentration for the enzymatic reaction presented in the Lineweaver-Burk plot below? a. -0.3211 units/mL b. –3.114 units/mL c. None of these values represent the optimal substrate concentration shown in the Lineweaver-Burk plot d. 3.114 units/mL e. 0.3211 units/mLarrow_forwardIn a typical enzyme-catalyzed reaction, what are the relative concentrations of reactants and products as compared to the enzyme concentration?arrow_forward
- graph the data from the table after taking recipocals of [S], V without inhibitor and V with inhibitor. It should be Lineweaver - Burke. use graph paper or excel. however upload graph and answers as 1 document as jpeg, pdf, or word. there should be 2 lines on 1 graph and both lines should cross the Y axis and hit the X axis (negative X axis). label both axes, determine Km and Vmax (show work) in the presence and absence of inhibitor State type of inhibition and if inhibitor resembles the substrate or not. can more substrate relieve the inhibition? [S] (UM) 3 10 30 5 90 Velocity (umol minute-¹) No inhibitor 10.4 14.5 22.5 33.8 40.5 Inhibitor 4.1 6.4 11.3 22.6 33.8arrow_forwardThe fosfomycin disc (200/50) also contains glucose-6-phosphate (G-6-P). Which ONE of the following best describes why this is the case? Select one: A. G-6-P increases the solubility of fosfomycin B. G-6-P is used to promote active transport of fosfomycin into the bacterial cell C. G-6-P is used in the formulation to correct glucose deficiencies promoted by fosfomycin D. G-6-P stabilises fosfomycin from spontaneous hydrolysis in aqueous solution E. G-6-P is an inhibitor of FosA that inactivates fosfomycinarrow_forward1. Ifa Lineweaver-Burk plot gave a line with an equation of y=0.25 x +0.34, what are the values of KM and Vmax if the substrate concentration is in mM and the velocity in mM/s?arrow_forward
- What if all the data above was the same EXCEPT with the change of G & X? Their new data is below. Would base X still be T? G & X [G] = 0.0447315M [X] = 0.0447315M [GX] = 0.0026845M 1.3416arrow_forwardWhen the yeast cells have completely re-hydrated, measure out 1.8 mL of well-mixed yeast suspension (0.2% yeast) into each of two new 15 mL centrifuge tubes. Add 200 μL of a 10% (w/v) Sodium Azide*** in YGM solution to one of the 15 mL tubes with yeast suspension. Add 200 μl of YGM to the other 15 mL tube of yeast suspension for your Control. Let both tubes incubate at room temperature for 30 min, vortexing every ~5 minutes What is the % concentration of azide in this sample during metabolic inhibition?What is the % concentration of yeast in this sample during metabolic inhibition?arrow_forwardIf the enzyme lactase has a Vo of 0.40 mM per minute when [S] = 1.25 mM, and a Vo of 1.0 mM per minute when [S] = 5.0 mM, what is its Vmax, Km and the slope on a linewver-burk plot?arrow_forward
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