Reaction Velocity (mm/sec)Mano!!L[11LIM3MFOSubstrate Concentration (M)1.INWhich statement is true?KMANALM4VThe graph above displays the kinetic profiles of the same enzyme catalyzing two different substrates.The red curve displays the higher turnover number (kcat).Thered curve displays higher affinity between substrate and enzyme.The blue curve displays competitive inhibition.The red curve displays higher cooperativity,

Answered: Image /qna-images/answer/24e00825-7950-4243-943f-50b201288862.jpg

Reaction Velocity (mm/sec) 1111111 Substrate Concentration (mm) The graph above displays the kinetic profiles of the sam Which statement is true? The red curve displays the higher turnover numb The red curve displays higher affinity between sm The blue curve displays competitive inhibition. The red curve displays higher cooperativity,

Reaction Velocity (mm/sec) 1111111 Substrate Concentration (mm) The graph above displays the kinetic profiles of the sam Which statement is true? The red curve displays the higher turnover numb The red curve displays higher affinity between sm The blue curve displays competitive inhibition. The red curve displays higher cooperativity,

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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The substrate dissociation constant, Ks, is k-1/k1. What do large values of this constant mean? That the formation of product will be fast Strong binding between enzyme and substrate that the reaction is unimolecular Weak binding between enzyme and substrate
Select the energy diagram or diagrams that illustrate reactions in which the second step is rate determining. A Free Energy C Free Energy Reaction A Reaction B Reaction C Reaction D Reaction Coordinate B Reaction Coordinate Free Energy Reaction Energy Diagrams Reaction Coordinate D Free M=MM Energy Reaction Coordinate
What is the relative activite and the degree of inhibition caused by a competitive inhibitor when [S] = Km and [I]=ki?
Predict the substrate and the activity (function) for a and b. For c and d, indicate the type of activity (class of enzyme) only. a) Maltase = b) Alcohol dehydrogenase c) CO2 H2C C. CH3 H3C H- H-N- CH- H,O H,N CH- OH CH CH, d) H,N CH OH
Match each enzyme class to the type of reactions catalyzed. Enzyme Class Type of Reactions Catalyzed reactions involving the transfer of a functional group from one molecule to another energetically unfavorable reactions that require ATP to form new bonds oxidation-reduction reactions reactions that eliminate or form a double bond hydrolysis reactions isomerization reactions Answer Bank hydrolase lyase ligase oxidoreductase isomerase transferase
6. What is the instantaneous reaction rate for an enzyme system? k = 0.087 1/h; enzyme concentration = 0.02 M; substrate concentration = 0.05 M; and Km concentration = 0.01 M? Answer should be in units of mM/h
H₂N Combination of two or more protein units 7. Which type of cross-link involves interactions between two cysteine amino acids? 8. Which type of cross-link would form between the following amino acids? Η Ο || H₂N-C-C-OH T CH₂ C=O NH₂ Η Ο LL H₂N-C-C-OH T CH₂ OH 9. To what main enzyme class do the nzym that catalyze the following reaction belong? (oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases) HO | || I c-c-N-C-COO + H₂O IT HR₂ R₁ H 1 This bond is cleaved H H₂N-C-COOⓇ I R₂ Wilter navy q H I H₂N-C-C00 1 R₁ •Qisulfide 10. Briefly explain the Lock and Key enzyme model.
How does changing the concentration of enzyme at a fixed concentration of substrate affect the rate of decomposition of H2O2?
29. In chymotrypsin both histidine and serine are important amino acids in the catalytic reaction. Below is an image showing one step of the reaction. Describe what is happening and the roles histidine and serine are playing. In your answer be sure to use correct terms in describing the type of enzyme mechanism being done each amino acid. His Asp 102 H₂C CH₂ Ser (195) CH₂ 4 Asp 102 H₂C CH₂ His 57 New N-terminus of cleaved polypeptide R chain Ser 195 CH₂
13. Isoenzyme assays can be used for medical diagnostic purposes because a. damaged tissue produces a different isoenzyme than undamaged tissue b. different tissues produce different isometric forms of the same enzyme C. different isoenzymes react with different substrates d. damaged tissue produces nonfunctioning isoenzymes
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 1.3 Would myricetin have higher or lower antibacterial activity compared to quercetin? Justify your answer by using the results provided.
vo(pM/min) 100 90 80 70 60 50 40 30, 20 10 0 What is V max for this enzyme ? Enzyme concentration 0.1 µM 5 10 15 20 A. 100 mm/min B. 1.0 mM/min C. 0.5 μM/min D. 50 µM/min E. 90 µM/min 25 30 35 37