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Part 3, Question A: The enzyme examfinalase uses a general acid-base mechanism to catalyze the reversible hydration/dehydration to interconvert L-serine and dehydroalanine. This follows a classic aß-elimination reaction in the direction of dehydration, with a AG° = 0. i. The active site is shown below. Sketch a proposed general acid-base reaction mechanism, where Gluso is the general base catalyst and Lys,16 is the general acid catalyst. Sketch all of the products on the right side of the equilibrium arrow. dehydroakanine Glu ii. Examfinalase was mutated, such that Arg:s1, which is positioned in close proximity to Glu is mutated to an Asp residue. Predict what impact this will have on the pK, of Glusai and offer a clear rationale.

Part 3, Question A: The enzyme examfinalase uses a general acid-base mechanism to catalyze the reversible hydration/dehydration to interconvert L-serine and dehydroalanine. This follows a classic aß-elimination reaction in the direction of dehydration, with a AG° = 0. i. The active site is shown below. Sketch a proposed general acid-base reaction mechanism, where Gluso is the general base catalyst and Lys,16 is the general acid catalyst. Sketch all of the products on the right side of the equilibrium arrow. dehydroakanine Glu ii. Examfinalase was mutated, such that Arg:s1, which is positioned in close proximity to Glu is mutated to an Asp residue. Predict what impact this will have on the pK, of Glusai and offer a clear rationale.

Human Anatomy & Physiology (11th Edition)
Human Anatomy & Physiology (11th Edition)
11th Edition
ISBN:9780134580999
Author:Elaine N. Marieb, Katja N. Hoehn
Publisher:Elaine N. Marieb, Katja N. Hoehn
Chapter1: The Human Body: An Orientation
Section: Chapter Questions
Problem 1RQ: The correct sequence of levels forming the structural hierarchy is A. (a) organ, organ system,...
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iii. In the direction of dehydration, Examfinalase is subject to homoallosteric effects with its substrate, L- serine and heteroallosteric effects with the allosteric effector, alanine, which stabilizes the T state of the enzyme. Sketch a plot of velocity vs. [L-serine] for both the wild-type and R251D mutation. In both cases, show the plots in the presence and absence of alanine. To facilitate clear comparisons, show all four plots on the same curve.
Transcribed Image Text:iii. In the direction of dehydration, Examfinalase is subject to homoallosteric effects with its substrate, L- serine and heteroallosteric effects with the allosteric effector, alanine, which stabilizes the T state of the enzyme. Sketch a plot of velocity vs. [L-serine] for both the wild-type and R251D mutation. In both cases, show the plots in the presence and absence of alanine. To facilitate clear comparisons, show all four plots on the same curve.
Part 3, Question A: The enzyme examfinalase uses a general acid-base mechanism to catalyze the reversible hydration/dehydration to interconvert L-serine and dehydroalanine. This follows a classic af-elimination reaction in the direction of dehydration, with a AG = 0. i. The active site is shown below. Sketch a proposed general acid-base reaction mechanism, where Gluzoi is the general base catalyst and Lys,u is the general acid catalyst. Sketch all of the products on the right side of the equilibrium arrow. Arg CH dehydroalanine NH CH G ii. Examfinalase was mutated, such that Arg.sı, which is positioned in close proximity to Gluo, is mutated to an Asp residue. Predict what impact this will have on the pK, of Gluai and offer a clear rationale.
Transcribed Image Text:Part 3, Question A: The enzyme examfinalase uses a general acid-base mechanism to catalyze the reversible hydration/dehydration to interconvert L-serine and dehydroalanine. This follows a classic af-elimination reaction in the direction of dehydration, with a AG = 0. i. The active site is shown below. Sketch a proposed general acid-base reaction mechanism, where Gluzoi is the general base catalyst and Lys,u is the general acid catalyst. Sketch all of the products on the right side of the equilibrium arrow. Arg CH dehydroalanine NH CH G ii. Examfinalase was mutated, such that Arg.sı, which is positioned in close proximity to Gluo, is mutated to an Asp residue. Predict what impact this will have on the pK, of Gluai and offer a clear rationale.
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