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

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter23: Fatty Acid Catabolism

Section: Chapter Questions

Problem 21P: Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved...

See similar textbooks

Similar questions

The oxyanion hole is comprised of hydrogen bonding atoms that project into a space on the active site that will have all H-bonding potential satisfied only during the catalytic cycle of the reaction. True or False? The catalytic triad residues are all next to each other in the primary sequence of trypsin. True or False?
The active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?
Mechanisms of catalysis : 2.1 Acid-base catalysis summary + example 2.2 Electrostatic catalysis summary + example 2.3 Covalent catalysis summary + example 2.4 Enzymen catalysis summary 2.5 Mechanism of chymotrypsin summary. These mechanisms involve several of the above-mentioned catalyses. In these summaries, do not just draw a diagram of the proposed mechanisms. It is more important to understand which reaction steps involve what kind of catalysis and how these help to reduce the activation energy needed for the reaction (e.g. a step in the reaction mechanism could be electrostatic catalysis to stabilise the transitions state) 2.6 Mechanism of lysozyme summary. These mechanisms involve several of the above-mentioned catalyses. In these summaries, do not just draw a diagram of the proposed mechanisms. It is more important to understand which reaction steps involve what kind of catalysis and how these help to reduce the activation energy needed for the reaction (e.g.…
Shown below is a proposed mechanism for the cleavage of sialic acid by the viral enzyme neuraminidase. The kcat for the wild-type enzyme at pH =6.15, 37 °C is 26.8 s-1.(a) Describe the roles of the following amino acids in the catalytic mechanism: Glu117, Tyr409, and Asp149. List all of the following that apply:general acid/base catalysis (GABC), covalent catalysis, electrostaticstabilization of transition state.(b) Based on the information shown in the scheme, would you expect mutation of Glu 117 to Ala to have a greater effect on KM or kcat?(c) For the R374N mutant at pH = 6.15, 37 °C, kcat is 0.020 s-1, and KMis relatively unaffected. Based on this result, it seems that R374 is morecritical for catalysis than for substrate binding. Explain how R374 stabilizesthe reaction transition state more than the substrate (i.e., what feature of this reaction would explain tighter binding to the transition state vs. substrate?).
What are the three key mechanisms and their associated features that are utilized by enzymes to catalyze reactions. Additionally, which two mechanims of the three you listed does the enzyme chymotrypsin use?
Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.
Where do each of these 5 main themes occur in the chymotrypsin mechanism? 1) substrate specificity 2) induced fit 3) covalent catalysis 4) acid/base catalysis 5) transition state stabilization
Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis?
UDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?
The oxyanion hole deprotonates an incoming water molecule to convert it to a potent nucleophile. True or False? The oxyanion hole is comprised of hydrogen bonding atoms that project into a space on the active site that will have all H-bonding potential satisfied only during the catalytic cycle of the reaction. True or False? The catalytic triad residues are all next to each other in the primary sequence of trypsin. True or False?
Given the following choices,a. what is the structure of the product of the reaction catalysed by ACAT?b. structure of the product produced from the reaction catalysed by phospolipase A2?c. general structure of TAGd. structure of glycerol
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.

SEE MORE QUESTIONS

Recommended textbooks for you

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

Biochemistry

ISBN:

9781305577206

Author:

Reginald H. Garrett, Charles M. Grisham

Publisher:

Cengage Learning

SEE MORE TEXTBOOKS