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 as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non-ionizable R groups. a) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn-Phe-Lys substrate ending your answer with product and free enzyme.

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
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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 as
chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C
terminus of polar, non-ionizable R groups.
a) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that
occurs to cleave the tripeptide Asn-Phe-Lys substrate ending your answer with product
and free enzyme.
b) From the list below, which of the components would most likely be found in the area of
the enzyme that substitutes the hydrophobic pocket of chymotrypsin? Very briefly
explain your choice(s).,
Ser
lle
Zn
Val
c) You've constructed a molecule that is able to bind to the 1 tetrahedral intermediate of
your new.enzyme, preventing catalysis. From experimental results, you can see that this
molecule is only able to bind to the tetrahedral intermediate. Assuming that this enzyme
follows Michaelis-Menten kinetics, draw a well labelled graph that shows the effects of
this molecule on your new enzyme. How would you correctly classify this molecule?
Transcribed Image Text: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 as chymotrypsin. Your new enzyme differs from chymotrypsin because it cuts peptides at the C terminus of polar, non-ionizable R groups. a) Beginning with the first tetrahedral intermediate, draw the mechanism of catalysis that occurs to cleave the tripeptide Asn-Phe-Lys substrate ending your answer with product and free enzyme. b) From the list below, which of the components would most likely be found in the area of the enzyme that substitutes the hydrophobic pocket of chymotrypsin? Very briefly explain your choice(s)., Ser lle Zn Val c) You've constructed a molecule that is able to bind to the 1 tetrahedral intermediate of your new.enzyme, preventing catalysis. From experimental results, you can see that this molecule is only able to bind to the tetrahedral intermediate. Assuming that this enzyme follows Michaelis-Menten kinetics, draw a well labelled graph that shows the effects of this molecule on your new enzyme. How would you correctly classify this molecule?
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