1. The antibacterial activity of flavonoids was tested against the bacterial strain, Escherichia coli. The minimum inhibitory concentration at which 50% of the compounds were inhibited (MIC50) are presented in the table below for some of the compounds. Table 1: Antibacterial activity of flavonoids tested against E. coli Compound Kaempferol Quercetin Compound X Luteolin Tangeritin 5,6,7,4'- Tetramethoxyflavone Genistin Genistein MIC50 (μg/mL) 25.50 35.76 36.72 67.25 137.10 156.34 238.94 320.88 1.1 What subgroups of flavonoids do these belong to.

1. The antibacterial activity of flavonoids was tested against the bacterial strain, Escherichia coli. The minimum inhibitory concentration at which 50% of the compounds were inhibited (MIC50) are presented in the table below for some of the compounds. Table 1: Antibacterial activity of flavonoids tested against E. coli Compound Kaempferol Quercetin Compound X Luteolin Tangeritin 5,6,7,4'- Tetramethoxyflavone Genistin Genistein MIC50 (μg/mL) 25.50 35.76 36.72 67.25 137.10 156.34 238.94 320.88 1.1 What subgroups of flavonoids do these belong to.

Chemistry for Today: General, Organic, and Biochemistry

9th Edition

ISBN:9781305960060

Author:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Publisher:Spencer L. Seager, Michael R. Slabaugh, Maren S. Hansen

Chapter20: Enzymes

Section: Chapter Questions

Problem 20.52E

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Similar questions

8 The optimal temperature for the action of lactate dehydrogenase is 36°C. It is irreversibly inactivated at 85°C, but a yeast containing this enzyme can survive for months at —10°C. Explain how this can happen.
If we made a Lineweaver-Burk plot of an irreversible inhibitor, which type of reversible inhibition would it be most likely to resemble?
Draw the structures of the substrate (pNPP) and of the inhibitors (Pi and Phe). Consider them in the fully deprotonated states. What similarities can you detect between each inhibitor and the substrate?
Following data were obtained for an enzyme in the absence and presence of an inhibitor. What are the Km and Vmax values for the inhibited and uninhibited enzymes? What is the type of inhibitor?
A4 Your enzyme is inhibited by one of the compounds depicted above. The inhibitor for your specific protein is indicated via the PDB protein code shown.On the basis of the enzyme’s structure, its substrate and mechanism of action, predict what type of enzyme inhibition ( i.e., competitive or non-competitive) may occur and justify why you think this is the case . (Up to 50 words) TYPE NOT WRITE.
. Relation between Reaction Velocity and Substrate Concentration: MichaelisMenten Equation: At what substrate concentration would an enzyme with a kcat of 30.0s−1 and a Km of 0.0050 M operate at one-quarter of its maximum rate?
A. Given the information in the image, what type of inhibitor would Sulfanilamide be? B. Sketch out what a Lineweaver–Burk plot would look like for both the normal binding of the enzyme and one which has Sulfanilamide present.
How is the maximal rate of the enzyme changed in the presence of an inhibitor?
Is the inhibitor competitive, uncompetitive or non competitive and why?
Calculate the enzyme and specific activity of a reaction with 3 μM Hsp90 using the following information: The rate is measured in a spectrophotometer as 0.028 OD units/min in a 1 ml reaction volume. The absorbance was detected at 340nm and the extinction coefficient for NADH at this wavelength is 6200 L M- 1 min-1 and the molecular mass of Hsp90 is 82.7 kDa. The rate of NADH utilisation is equivalent to the rate of ATP utilised by Hsp90. Show all your calculations and the units for your answers. c) Calculate the turnover number for the reaction described in (b) above
The time that is required for an enzyme to convert one substrate molecule into one product molecule is _________ A. Km. B. 1/kcat. C. 1/Km. D. kcat. Which of the following does not apply to the concerted model for subunit behavior: A. Each subunit can exist in a relaxed (R) and taut (T) conformation. B. All subunits will be in either the R or the T conformation at the same time. C. Some subunits can be in the R state while others are in the T state. D. The presence of inhibitors will lead to more of the enzyme being in the T form E. The presence of activators will lead to more of the enzyme being in the R form
An orange juice is thermally processed for determining ascorbic acid degradation kinetics. After different temperature experiments, the following ascorbic acid concentration values were obtained: Ascorbic Acid (mg/L) Processing Time (second) 0 15 30 60 90 120 Temperature (oC) 75 558.3 546.5 535 526.5 519.6 508.6 85 608.6 595.2 587.4 572.7 557.5 542.3 95 612.6 601.5 588.2 546.1 521.8 509.5 According to the results; Determine ascorbic acid degradation order Derive the equations related to the degradation order (general equation and t1/2) Calculate k-values at the constant processing temperatures Calculate activation energy (Ea) of the degradation reaction Calculate half-life time of ascorbic acid for all processing (For better evaluation, add figures for the addressed questions, if necessary)