If possible, please help with part A and part B 5. Consider the isomerization of glucose-6-phosphate (G6P) into fructose-6-phosphate (F6P):G6PF6PThis reaction can be described assuming simple Michaelis-Menten kinetics:[G6P] + [E] = [G6PE] → [F6P] + [E]-a.What is the name of the enzyme used in this reaction? What type of enzyme is it?b.How does this reaction prepare the substrate for the payoff phase of glycolysis? Why is it needed?

Glycolysis is a metabolic pathway which results in formation of pyruvic acid along with the release…

Answered: 5. Consider the isomerization of…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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7. Chalcone isomerase catalyzes the reaction illustrated below. A series of modification experiments were performed on this enzyme to identify which amino acid residues might be in the active site and which might promote the cyclization reaction. OH Ho. Но Explain the following results: A) Acetic anhydride treatment inhibited enzyme activity. B) Pyrocarbonate inhibited activity and was found to modify 7 residues. However, this enzyme only contains 6 His and modification of these did not affect activity. C) lodoacetate inhibited activity but this effect coult be decreased in the presence of substrate or product. D) Methane methanethiol sulfonate modified the enzyme but did not inhibit catalytic turnover. In addition, this modification was reversed in the presence of B-mercaptoethanol. keNyons Rengent
Given the following reaction, identify the class and subclass of the enzyme involved. H. CH2OH H-C-OH C=0 но-с-н но-с-н H-C-OH H-C-OH H-C-OH H-C-OH CH2OPO,2 CH2OPO,2- Class: [ Select] [ Select ] Ligase Hydrolase Lyase Subcla Transferase Isomerase Oxidoreductase
b) Why might the compound shown below act as a transition state analog of phosphoglucose isomerase? A drawing of the normal transition state for this enzyme is needed. HO- OH T .N -OH -OH CH₂OPO₂²-
2. If glyceraldehyde-3-phosphate dehydrogenase in red blood cells is completely inhibited, which intermediates in glycolysis accumulate most? Please use the following equation and the provided information to explain your reasoning. AG=AG° + RTln [C] [D]d [A] [B]' Fructose 1,6-bisphosphate → Glyceraldehyde 3-phosphate + Dihydroxyacetone phosphate The standard free energy for the above reaction is: AG" = +23.9 KJ/mol T° = 298 R = 8.314 J mol-¹ K-1
One of the examples that we have used to illustrate the concept of equilibrium is the isomerization of glucose-6-phosphate (G6P) to fructose-6-phosphate (F6P), which is the second step in g ycolysis. Draw a graph to show how the reaction Gibbs energy varies with the fraction fof F6P in solution.Label the regions of the graph that correspond to the formation of F6P and G6P being spontaneous, respectively.
5. Shown below are the first steps in the mechanism of a cysteine protease, which catalyses amide bond hydrolysis in a similar manner as serine proteases. (a) Complete this mechanisms, and (b) sketch the approximate reaction coordinate diagram for this catalyzed reaction relative to the uncatalyzed proteolysis. HN N HN cysteine protease
2. If glyceraldehyde-3-phosphate dehydrogenase in red blood cells is completely inhibited, which intermediates in glycolysis accumulate most? Please use the following equation and the provided information to explain your reasoning. AG=AG° + RTln [C][D]d [A] [B]¹ Fructose 1,6-bisphosphate → Glyceraldehyde 3-phosphate + Dihydroxyacetone phosphate The standard free energy for the above reaction is: AG" = +23.9 KJ/mol T° = 298 R = 8.314 J mol-¹ K-¹
11. This below notation represents a Bi-Bi reaction. Aspartate Oxaloacetate a-Ketoglutarate Glutamate Enzyme Enzyme E (E-NH3) (oxaloacetate) (E-NH3) (E-NH3) (a-ketoglutarate) E (aspartate) (glutamate) In this rection, in which step the ternary complex is formed? Briefly explain your answer.
10. Chymotrypsin is a serine protease enzyme. The Km for the reaction of chymotrypsin with N-acetylvaline ethyl ester is 8.8*102, and the Km for the reaction of chymotrypsin with N- acetyltyrosine ethyl ester is 6.6*10“ M. catalytic triad Ser 195 His 57 Gly 193 N-H OH R-N- Ca N-H O-C- Asp 102 N-acetyl valine N-acetyl tyrosine Chymotrypsin Active Site a. What is the nucleophile here and how is it activated? b. Which substrate has an apparent higher affinity for the enzyme. c. Propose a reason for the difference in affinity based on the shape of each of the substrates (see active site figure, cleaves on the C-side of aromatic residues).
5. Consider the reaction for assembly of a tetrapeptide from for amino acids: Serine + Proline + Alanine + Methionine ----> SPAM tetrapeptide Is this reaction anabolic or catabolic? Is this a positive or negative delta G reaction? List at least three other terms you could use to describe this reaction. 6. Consider the reaction: Glutamic acid + Ammonia + ATP ----> Glutamate + ADP + Pi Is this reaction anabolic or catabolic? Is this a positive or negative delta G reaction? This is actually an example of a coupled reaction! Briefly, explain why reaction coupling is required, and how it works in this example.
complete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.
(i) Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting the roles of the catalytice triad for the two phases of the catalytic reactions. Explain the significance of the oxyanion hole for the catalysis. (ii) All serine proteases contain the catalytic triad and these amino acids are positioned in the exact same conformation. Since this is true, why do trypsin and chymotrypsin have such different substrate specificity? What features of the enzyme allow for this situation?

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