Answered: The enzyme methylmalonyl-CoA mutase is…

The enzyme methylmalonyl-CoA mutase is a mutase, which is a specific type of the major enzyme class of isomerases that catalyze [ Select) reactions.

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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What type of enzyme is needed to catalyze the following reaction?
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.
1. The reaction catalyzed by aldolase splits fructose-1,6-bisphosphate (F16BP) into glyceraldehyde-3-phosphate (G3P) and dihydroxyacetone phosphate (DHAP). The AG°" for the reaction is 23.8 kJ/mole. If the concentrations of G3P and DHAP are 2.5 mM and 1 mM, respectively, what concentration of F16BP is needed for the reaction to be at equilibrium in a human cell?
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
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)
Past paper
Q2 CH,OH CH,OPO,2- H H OH H OH 0-PO,2- но но OH H. OH OH Glucose-1-phosphate Glucose-6-phosphate Calculate the standard free-energy change (AG°) fo the reaction catalyzed by the enzyme phosphoglucomutase. When at standard temperature (25 °C) and pressure, the equilibrium of each molecule is 1 mM glucose 1-phosphate and 19 mM glucose 6-phosphate. HINT: at 25 °C, RT = 2.479 kJ/mol