You have discovered a new enzyme that has a nearly identical active site to chymotrypsin.This new enzyme uses the same catalytic triad and the same reaction mechanism aschymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the Cterminus of polar, non-ionizable R groups.a) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis thatoccurs to cleave the tripeptide Asn-Phe-Lys substrate ending your answer with productand free enzyme.b) From the list below, which of the components would most likely be found in the area ofthe enzyme that substitutes the hydrophobic pocket of chymotrypsin? Very brieflyexplain your choice(s).,SerlleZnValc) You've constructed a molecule that is able to bind to the 1 tetrahedral intermediate ofyour new.enzyme, preventing catalysis. From experimental results, you can see that thismolecule is only able to bind to the tetrahedral intermediate. Assuming that this enzymefollows Michaelis-Menten kinetics, draw a well labelled graph that shows the effects ofthis molecule on your new enzyme. How would you correctly classify this molecule?

As given peptide is Asn-Phe-lys, and discovered enzyme cleaves at C terminal of non ionizable polar…

Answered: You have discovered a new enzyme that…

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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Please, please I do not understand this question for Biochemistry. Can you help me? Steps leading to the correct answer would be helpful!
The enzyme chymotrypsin, catalyses the hydrolysis of nitrophenyl acetate and other acyl esters. Name the amino acid residue, the side chain of the residuee and the type of bonding/linkage involved in the formation of the acyl-enzyme complex during catalysis.
Intermediates of a pathway are shown in the following scheme. Using curved arrows, show the mechanism of each step labeled with a blue letter. Draw out abbreviated structures of the coenzymes, so that you can effectively show all arrow pushing. You may abbreviate the coenzymes by putting R groups on the molecule, but do draw out the parts of the structure that are involved in the arrow pushing. Some of the transformations will require you to show multiple structures to show all of the arrow pushing (particularly some of the coenzyme-mediated steps). You do not need to show specific amino acid residues that perform the catalysis. You can abbreviate acidic amino acid residues “Enz–B–H” and basic residues “B–Enz”.
What are cofactors and coenzymes in an enzymatic reaction? Is tetrahydro- folate considered a coenzyme or a cofactor? Explain.
for the coenzyme structures below label the following: a.) label the coenzymes b.) identify the reactive components of both coenzymes c.) identify the component that differs between NAD+ and NADP+ d.) how come these coenzymes are known as dinucleotides?
A simple enzymatic reaction proceeds as follows. E+S↔E.S→ E+P Derive the Michaelis–Menten equation for this reaction.
Please answer this question and the highlighted question is wrong please explain why and give me the correct answer
Consider the following mechanism: What kind of reaction is occurring during this step of glycolysis? What metabolite is in Box 1? What metabolite is in Box 2? What metabolite is in Box 3? What enzyme catalyzes this reaction? Circle and label one place on the mechanism where covalent catalysis is occurring. Suggest an amino acid that could fill the role of residue “A” in the mechanism above and draw its structure at pH 7.4. Suggest an amino acid that could fill the role of residue “B” in the mechanism above and draw its structure at pH 7.4. Under standard conditions, this reaction is unfavorable (DG¢° = 23.8 kJ/mol). What conditions in the cell allow for the actual free energy change to be lower (DG » 0), making the reaction readily reversible? Explain your answer. *please help and explain as well as you can*
Soy sauce is prepared in a CLOSED tank by fermenting a salted mixture of soybeans and wheat with yeast, over a period of 8 to 12 months. The resulting sauce (after solids are removed) is rich in ethanol. (a) How is ethanol produced in the resulting soy sauce? What is the importance of this process? Include the enzymes involved. (b) Could ethanol be produced when the reaction mixture is incubated in an OPEN tank?
1. In a catabolic pathway, metabolite X gets converted into metabolite Y, metabolite X 0 J mol-¹ and AG' is <0 J mol-¹ for this reaction. a) At standard states, is this reaction favorable? b) Is the reaction favorable or unfavorable at cellular condition? c) Is this an endergonic or exergonic reaction in the cell? d) Would you describe this as a thermodynamically downhill or uphill reaction in the cell?
How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reaches a maximum value at high substrate?
The covalent catalytic mechanism of an enzyme depends on a single active site Cys whose pK is 8. A mutation in a nearby residue alters the micro environment so that this pK increases to 10. Would the mutation cause the reaction rate to increase or decrease? Explain.

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