You have discovered a new enzyme that has a nearly identical active site tochymotrypsin. This new enzyme uses the same catalytic triad and the samereaction mechanism as chymotrypsin. Your new enzyme differs fromchymotrypsin because it cuts peptides at the C terminus of polar, non-ionizable R groups.A) Beginning with the first tetrahedral intermediate, draw the mechanism ofcatalysis that occurs to cleave the tripeptide Asn- Phe- Lys substrate endingyour answer with the product and free enzyme.B) From the list below, which of the components would most likely be foundin the area of the enzyme that substitutes the hydrophobic pocket ofchymotrypsin? Very briefly explain your choice(s):Ser ileZn+ ValC) You've constructed a molecule that is able to bind to the 1st tetrahedralintermediate of your new enzyme, preventing catalysis. From experimentalresults, you can see that this molecule is only able to bind to the tetrahedralintermediate. Assuming that this enzyme follows Michaelis- Mentne Kinetics,draw a well labelled graph that shows the effects of this molecule on yournew enzyme. How would you correctly classify this molecule?

Name: You have discovered a new enzyme that has a nearly identical active s
Uploaded: 2024-03-20T06:42:55.000Z
Channel: Bartleby
Description: You have discovered a new enzyme that has a nearly identical active site tochymotrypsin. This new enzyme uses the same catalytic triad and the samereaction mechanism as chymotrypsin. Your new enzyme differs fromchymotrypsin because it cuts peptides