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HO. GPNA NO 2 Chymotrypsin H2O HO. GP ΌΗ + NO2 NH2 NA 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 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?

Introduction to General, Organic and Biochemistry
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 draw out the reaction mechanism for this reaction showing all the curly arrows and 
2. Draw the GPNA molecule and identify the phenylalanine portion. 
3. Draw L-phenylalanine with the correct stereochemistry

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
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?
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