The activity of an enzyme requires a glutamic acid to display its -COOH functional group in the protonated state. Suppose the pK, of the -COOH group is 4.07. (a) Will the enzyme be more active at pH 3.5 or 4.5? Explain. (b) What fraction of the enzymes will be active at pH = 4.07? Explain. (c) At what pH will the enzyme show 78% of maximal activity?

The activity of an enzyme requires a glutamic acid to display its -COOH functional group in the protonated state. Suppose the pK, of the -COOH group is 4.07. (a) Will the enzyme be more active at pH 3.5 or 4.5? Explain. (b) What fraction of the enzymes will be active at pH = 4.07? Explain. (c) At what pH will the enzyme show 78% of maximal activity?

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...

See similar textbooks

Similar questions

The isoelectric point, pI, of the protein hexokinase P-I is 5.25, while that of alkaline phosphatase is 4.5 What is the net charge of hexokinase P-I at pH 5.1 ?| What is the net charge of alkaline phosphatase at pH 2.1 ?[ The isoelectric point of glycine is 5.97 ; threonine, 5.6. During paper electrophoresis at pH 7.1, toward which electrode does glycine migrate? During paper electrophoresis at pH 4.5, toward which electrode does threonine migrate?
Please don't use hend raiting and step by step solutions
Proteins are thermodynamically unstable molecules since the Delta G of hydrolysis is quite negative. However, most proteins are not degraded unless they come into contact with proteases in cells. What is the reasoning for this paradox? The reaction is endergonic and will not proceed without energy. There is very little water inside cells to react with protein molecules. The free energy change doesn't reveal anything about the rate of the reaction. The concentration of proteins are low which allows them to be more stable.
Please don't provide handwritten solution .
Trypsin is a serine protease that has a KM of 15 mM. At an initial substrate concentration of 250 µM insulin, trypsin is found to degrade insulin at a rate of 0.6 µM/min. If the concentration of trypsin in solution was 4.326 µM, what is the kcat of trypsin in s-1?
What is the expected result if the enzyme monoamine oxidase is treated with the substrate analog named N,N-dimethylpropargylamine? H3C `N I CH3 N,N-dimethylpropargyl amine The product propargyl aldehyde (H-C=C-CH=O) will be formed and released. The product propargyl alcohol (H-CEC-CH₂-OH will be formed and released. The enzyme will be rapidly and covalently (irreversibly) inhibited. The enzyme will be reversibly and competitively inhibited in the presence of this substrate analog. a. b. monoamine oxidase C. d. MAO + O₂
The following graph of an enzyme catalyzed reaction what does B represen Rate of reaction A B maximum velocity minimum velocity competitive inhibition non-competitive inhibition
7. The free energy of a reaction is positive, i.e., greater than zero, indicating that this reaction cannot occur spontaneously or naturally. Do you think adding an enzyme to this reaction can cause the reaction to occur? Suggest a method you can employ thermodynamically to make this reaction occur. (Please provide detail explanation for your answers)
The isoelectric point (pl) of phenylalanine is pH 5.5. Draw the structure of the major form of glutamic acid at pH values of (a) 1 (b) 5.5 (c) 11.0.
Calculate the isolelectric point of the following tetrapeptide, IHGK. The pK, of the N-term is 9.59 and the pK, of the C-term is 2.29.