Background Enzymes are biological catalysts that increase the rates of chemical reactions by lowering the activation energies for those reactions. Chymotrypsin is a major pancreatic enzyme, and is a member of the serine protease family. This family of enzymes catalyse the hydrolytic cleavage of peptide bonds. The major difference among members of the serine proteases is specificity. Chymotrypsin is specific for peptides of the amino acids phenylalanine, tyrosine and tryptophan. It attacks only peptide bonds on the carboxyl side of tyrosine, tryptophan and phenylalanine (hydrophobic or aromatic amino acids) (SEE LECTURE NOTES). Pre-practical "MUST DO" to be included in your lab-book: 1. Reaction mechanism 2. Draw the GPNA molecule and identify the phenylalanine portion. 3. Draw L-phenylalanine with the correct stereochemistry 4. Why do you need to add the substrate into the buffer in the cuvette and not the other way around? 5. Why do you need to add the enzyme just before starting UV acquisition? HO. GPNA NO 2 Chymotrypsin H2O HO. GP ΌΗ + NO2 NH2 NA

Introduction to General, Organic and Biochemistry
11th Edition
ISBN:9781285869759
Author:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Publisher:Frederick A. Bettelheim, William H. Brown, Mary K. Campbell, Shawn O. Farrell, Omar Torres
Chapter31: Immunochemistry
Section: Chapter Questions
Problem 31.75P
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can someone do the reaction mechanism for this reaction and draw the molecules for Q2 and q3

Background
Enzymes are biological catalysts that increase the rates of chemical reactions by lowering the
activation energies for those reactions. Chymotrypsin is a major pancreatic enzyme, and is a
member of the serine protease family. This family of enzymes catalyse the hydrolytic cleavage of
peptide bonds. The major difference among members of the serine proteases is specificity.
Chymotrypsin is specific for peptides of the amino acids phenylalanine, tyrosine and tryptophan.
It attacks only peptide bonds on the carboxyl side of tyrosine, tryptophan and phenylalanine
(hydrophobic or aromatic amino acids) (SEE LECTURE NOTES).
Pre-practical "MUST DO" to be included in your lab-book:
1. Reaction mechanism
2. Draw the GPNA molecule and identify the phenylalanine portion.
3. Draw L-phenylalanine with the correct stereochemistry
4. Why do you need to add the substrate into the buffer in the cuvette and not the other
way around?
5. Why do you need to add the enzyme just before starting UV acquisition?
Transcribed Image Text:Background Enzymes are biological catalysts that increase the rates of chemical reactions by lowering the activation energies for those reactions. Chymotrypsin is a major pancreatic enzyme, and is a member of the serine protease family. This family of enzymes catalyse the hydrolytic cleavage of peptide bonds. The major difference among members of the serine proteases is specificity. Chymotrypsin is specific for peptides of the amino acids phenylalanine, tyrosine and tryptophan. It attacks only peptide bonds on the carboxyl side of tyrosine, tryptophan and phenylalanine (hydrophobic or aromatic amino acids) (SEE LECTURE NOTES). Pre-practical "MUST DO" to be included in your lab-book: 1. Reaction mechanism 2. Draw the GPNA molecule and identify the phenylalanine portion. 3. Draw L-phenylalanine with the correct stereochemistry 4. Why do you need to add the substrate into the buffer in the cuvette and not the other way around? 5. Why do you need to add the enzyme just before starting UV acquisition?
HO.
GPNA
NO 2
Chymotrypsin
H2O
HO.
GP
ΌΗ
+
NO2
NH2
NA
Transcribed Image Text:HO. GPNA NO 2 Chymotrypsin H2O HO. GP ΌΗ + NO2 NH2 NA
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