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QUESTION 2 Below is diagram of a part of the reaction mechanism of the enzyme Aldolase. The first structure shows the ES complex with the substrate (fructose-1,6-bisphosphate) bound to the enzyme's substrate binding site. The second structure shows one of the intermediates of the reaction mechanism interacting with the enzyme active site. The enzyme is shown as a the wavy line around the perimeter. Parts of amino acid side chains key to the reaction mechanism are shown interacting with the substrate and intermediate. Use these structures to answer the following questions: HO CH₂ -CH HC -OH HC H₂C :0 E-S Complex -OH OPO, +H₂N- N S57 2K119 H224 H₂O -20₂PO НО CH₂ -CH HC O HC- -OH H₂C E-TS Complex OPO₂-2 *HN- K119 S57 H224 What type of catalytic strategy is the lysine involved in? What type of catalytic strategy is the histidine involved in? What type of catalytic strategy is the serine involved in? Which amino acid accounts for the fact that this enzyme is specific for fructose-1,6-phosphate and not fructose? Which mutation could potentially replace H224 and still retain activity? Acid/Base Catalysis Covalent Catalysis Metal Catalysis Proximity/Orientation Effect Transition State Stabilization lysine histidine serine H224F H224E H224N

QUESTION 2 Below is diagram of a part of the reaction mechanism of the enzyme Aldolase. The first structure shows the ES complex with the substrate (fructose-1,6-bisphosphate) bound to the enzyme's substrate binding site. The second structure shows one of the intermediates of the reaction mechanism interacting with the enzyme active site. The enzyme is shown as a the wavy line around the perimeter. Parts of amino acid side chains key to the reaction mechanism are shown interacting with the substrate and intermediate. Use these structures to answer the following questions: HO CH₂ -CH HC -OH HC H₂C :0 E-S Complex -OH OPO, +H₂N- N S57 2K119 H224 H₂O -20₂PO НО CH₂ -CH HC O HC- -OH H₂C E-TS Complex OPO₂-2 *HN- K119 S57 H224 What type of catalytic strategy is the lysine involved in? What type of catalytic strategy is the histidine involved in? What type of catalytic strategy is the serine involved in? Which amino acid accounts for the fact that this enzyme is specific for fructose-1,6-phosphate and not fructose? Which mutation could potentially replace H224 and still retain activity? Acid/Base Catalysis Covalent Catalysis Metal Catalysis Proximity/Orientation Effect Transition State Stabilization lysine histidine serine H224F H224E H224N

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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QUESTION 2 Below is diagram of a part of the reaction mechanism of the enzyme Aldolase. The first structure shows the ES complex with the substrate (fructose-1,6-bisphosphate) bound to the enzyme's substrate binding site. The second structure shows one of the intermediates of the reaction mechanism interacting with the enzyme active site. The enzyme is shown as a the wavy line around the perimeter. Parts of amino acid side chains key to the reaction mechanism are shown interacting with the substrate and intermediate. Use these structures to answer the following questions: -20 PO CH₂ HỌ—CH HC HC H₂C -OH E-S Complex OH OPO3 H₂N- S57 K119 H224 H₂O -20₂PO CH₂ H HO- -CH HC O HC -OH H₂C E-TS Complex OPO₂ *HN- K119 S57 H224 What type of catalytic strategy is the lysine involved in? What type of catalytic strategy is the histidine involved in? What type of catalytic strategy is the serine involved in? Which amino acid accounts for the fact that this enzyme is specific for fructose-1,6-phosphate and not fructose? Which mutation could potentially replace H224 and still retain activity? Acid/Base Catalysis Covalent Catalysis Metal Catalysis Proximity/Orientation Effect Transition State Stabilization lysine histidine serine H224F H224E H224N
Transcribed Image Text:QUESTION 2 Below is diagram of a part of the reaction mechanism of the enzyme Aldolase. The first structure shows the ES complex with the substrate (fructose-1,6-bisphosphate) bound to the enzyme's substrate binding site. The second structure shows one of the intermediates of the reaction mechanism interacting with the enzyme active site. The enzyme is shown as a the wavy line around the perimeter. Parts of amino acid side chains key to the reaction mechanism are shown interacting with the substrate and intermediate. Use these structures to answer the following questions: -20 PO CH₂ HỌ—CH HC HC H₂C -OH E-S Complex OH OPO3 H₂N- S57 K119 H224 H₂O -20₂PO CH₂ H HO- -CH HC O HC -OH H₂C E-TS Complex OPO₂ *HN- K119 S57 H224 What type of catalytic strategy is the lysine involved in? What type of catalytic strategy is the histidine involved in? What type of catalytic strategy is the serine involved in? Which amino acid accounts for the fact that this enzyme is specific for fructose-1,6-phosphate and not fructose? Which mutation could potentially replace H224 and still retain activity? Acid/Base Catalysis Covalent Catalysis Metal Catalysis Proximity/Orientation Effect Transition State Stabilization lysine histidine serine H224F H224E H224N
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