Serine Proteases, such as chymotrypsin, contain Ser/Asp/His as a catalytic triad (i.e. threecollaborating amino acids) of amino acids involved in enzyme catalysis. Why is this?Examine each amino acid of this catalytic triad (schematically detailed below:Ser195/Asp102/His57) and, based on your understanding of amino acid characteristics,predict what the role of each amino acid could be.His57Ser195Asp102

The active site of enzymes are among the conserved regions of proteins. If evolution finds an active…

Answered: Serine Proteases, such as chymotrypsin,…

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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Similar questions

What would be the effect on the activity of phosphofructokinase of the mutation of Asp103 to the unusual amino acid shown below? Explain in terms of actual structures of the side chains of Asp and this unusual amino acid.
An enzyme that catalyzes disulfide– sulfhydryl exchange reactions, called protein disulfide isomerase (PDI), has been isolated. PDI rapidly converts inactive scrambled ribonuclease into enzymatically active ribonuclease. In contrast, insulin is rapidly inactivated by PDI. What does this important observation imply about the relation between the amino acid sequence of insulin and its threedimensional structure?
What is the smallest number of molecules of ATP and GTP consumed in the synthesis of a 200- residue protein, starting from amino acids? Assume that the hydrolysis of PP i is equivalent to the hydrolysis of ATP for this calculation.
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?
Based on your understanding of the structure and function of the enzyme chymotrypsin, explain why proteolytic activation by Trypsin in the intestine is required for chymotrypsin to bind its substrates with high affinity. Your answer should include a description of the amino acid residue or residues involved AND a kinetic experiment that suggested this.
Why do structural analogs of the transition-state intermediate of an enzyme inhibit the enzyme competitively and with low Ki values (binds tightly)?
Describe the features of the first binding site (for allosteric enzyme unprotkb-p39086), including structural features that recognize and complement the first ligand.
In the serine protease triad, the proximity of an aspartatecarboxylate group to the imidazole group of histidine raisesthe latter’s pKa. Explain.
Insulin possesses two polypeptide chains denoted A and B that are linked by disulfide bonds. Upon denaturation by reduction of the SH groups of insulin, followed by reoxidation, only 7% of the hormone activity is recovered. This is the level of activity expected for random pairing of cysteine residues to form disulfide bonds. How can these data be reconciled with the hypothesis that the amino acid sequence directs protein folding?
In a mixed heteropolymer experiment, messages were createdwith either 4/5C:1/5A or 4/5A:1/5C. These messages yielded proteinswith the amino acid compositions shown in the followingtable. Using these data, predict the most specific coding compositionfor each amino acid.4/5C:1/5A 4/5A:1/5CPro 63.0% Pro 3.5%His 13.0% His 3.0%Thr 16.0% Thr 16.6%Glu 3.0% Glu 13.0%Asp 3.0% Asp 13.0%Lys 0.5% Lys 50.0% 98.5% 99.1%
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?
Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.

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