2 Chymotrypsin is a serine protease. Assume chymotrypsin satisfies Michaelis-Menten kinetics. Below is a diagram showing the Michaelis complex.Please answer the following questions:Gly 193RANH'NHGly 193NHSer 195HNBHis 57|| AspN NH…-O-CH 102R'1) What are the names of the sites of the enzymes labelled with A and B? (15%)2) Mutation of Ser195 to a Cys residue produces a less active but functional enzyme. Based on the diagram of the Michaelis complex, draw a diagram of a Ser195Cys mutated enzyme bound transition-state complex. (40%)3) In the substrate peptide, which of the R and R' is an N-terminal residue, which is the C-terminal residue? (15%)4) If the Asp102 is mutated to an Asn, chymotrypsin catalytic efficiency is also greatly reduced, which of the following constant is significantly changed: k1, k-1, K2, KM, Kcat? Explain why it is changedbut others are not. (30%)

Chymotrypsin is a serine protease. It catalyses the hydrolytic cleavage of the peptide bond next to…

Answered: 1) What are the names of the sites of…

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

Problem 1P

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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?
D-Talose is a C2 epimer of D-galactose. Using the Fischer projection structure, draw the product of reaction ofD-talose with the given reagent or enzyme and write the systematic name of the product. 1. 2,4-DNP 2. Reaction with aminotransferase and then acetyltransferase at C4
The M and H subunits of lactate dehydrogenase have very similar sizes and shapes but differ in amino acidcomposition. If the only difference between the two were that theH subunit had a glutamic acid in a position where the M subunithad a serine, how would the five isozymes of LDH separate on electrophoresis using a gel at pH 8.6?
Why is triose phosphate isomerase considered to be catalytically perfect?
Give the corresponding class, subclass, sub-subclass, specific enzyme of the following E.C. codes. Give also the systematic name of the enzyme E.C. 2.7.4.3 E.C. 1.1.1.42 E.C. 5.3.1.8 E.C. 5.4.2.2 E.C. 3.4.13.18 Example:E.C. 2.7.1.1Class 2 = transferaseSubclass 7 = transfer of phosphateSub subclass 1 = an alcohol is the phosphate acceptorFourth number 1 = hexokinaseSystematic name = ATP:D-hexose 6-phosphotransferase
In germ-free mice, which harbor no intestinal bacteria, the O-linked oligosaccharides of intestinal glycoproteins tend to lack a terminal fucose residue (see Fig.). (a) What enzyme is not produced in normal quantities in these mice? (b) What monosaccharides tend to appear at the ends of O-linked oligosaccharides in these animals?
Draw the (B1-->A1) linked dissacharide formed between the C3 epimer of B-D-glucose and the C2 epimer of a-D-galactose. Explain in 1-2 sentences why (or why not) a precipiate would be observed when mixing this dissacharide in an alkaline solution of copper.
Lysozyme is an enzyme that hydrolyzes bacterial cell wall polysaccharides. When this reaction is carried out in the presence of H218O, it is observed that there is retention of configuration at the C1 carbon of the D site sugar as shown below: Would this result suggest that the enzyme mechanism involves the direct nucleophilic attack of water at C1 or that the enzyme mechanism involves attack by a nucleophilic amino acid side chain of the enzyme that generates a transient covalent intermediate?
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.
The highest energy point of the serine protease reaction is the formation of the tetrahedral oxyanion intermediate on the original carbonyl carbon of the scissile peptide bond. True or False? DIPF is an irreversible inhibitor of serine proteases. True or False? The acyl-enzyme intermediate is the transition state of the reaction. True or False? Serine proteases are classified as isomerases. True or False?
How would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?
In the first step of the aldolase reaction, an active site Lys229 residue, with its side chain amino group in the deprotonated state, acts as a nucleophile and attacks the carbonyl C2 carbon of fructose 1,6-bisphosphate to form a Schiff base (boxed in the scheme). Since the pKa of the Lys side chain amino group in free solution is ~10.5, the pKa of Lys229 side chain must have been perturbed to a (higher lower) value for the enzyme to be active at neutral pH. the answer should include sufficient details, including the definition of pKa.

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