(i)Describe the mechanism of chymotrypsin in cleaving a peptide bond, highlighting theroles of the catalytice triad for the two phases of the catalytic reactions. Explain thesignificance of the oxyanion hole for the catalysis.(ii)All serine proteases contain the catalytic triad and these amino acids are positioned inthe exact same conformation. Since this is true, why do trypsin and chymotrypsinhave such different substrate specificity? What features of the enzyme allow for thissituation?

Answer i- A catalytic triad is a group of three amino acids present in the active site of some…

Answered: Describe the mechanism of 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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Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain serine, histidine and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein substrates. (b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below. Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala, Arg, or Trp? Explain your answers. Val 216 Val 190 Asp 189 Chymotrypsin Trypsin Elastase
Chymotrypsin, trypsin, and elastase all share the same catalytic mechanism, but have different specificities. (a) These proteases are considered serine proteases because the active sites contain serine, histidine and aspartate. Describe the roles that each of these amino acid residues play in hydrolyzing protein substrates. (b) The active site pockets of chymotrypsin, trypsin, and elastase are shown in the image below. Based on the image, which side chain of the amino acids would they prefer to cleave respectively, Ala, Arg, or Trp? Explain your answers. Val 216KVal 190 Asp 189 Chymotrypsin Trypsin Elastase
Beginning with the 1st tetrahedral intermediate, show the complete steps in chymotrypsin mechanism that occurs to form the 2nd chymotrypsin intermediate in the chymotrypsin active site. The substrate for chymotrypsin to be used is Ala-Tyr-Gly. Further, name the amino acid(s) that would be released as a result of the reactions you'd illustrated above.
complete the following mechanism showing the cleavge of the peptide bond for the following cysteine protease reaction. you only need a catalytic dyad for cystein proteases because the pKa of cysteine is low enough (8) and close enough to the pH of 7.4 that is can easily be deprotonated by histidine.
What are the amino acids of the catalytic triad of chymotrypsin? State the mode of catalysis shown by each of the amino acids that you have named. (a) (b) Predict what will happen if aspartic acid of the triad is replaced by asparagine. (c) Briefly explain the role of the oxyanion hole for the catalysis of chymotrypsin.
There is a cysteine protease, which uses a similar chemical mechanism to chymotrypsin except for using cysteine instead of serine during catalysis. Please draw the stepwise chemical mechanism for the cysteine protease.
. (a) Explain the biochemical basis for the fact that one can synchro- nize cell populations þy treating them with deoxythymidine. (b) Explain the apparent paradox that dATP at low concentrations is an activator of ribonucleotide reductase, whereas at higher concen- trations it becomes inhibitory.
Asp residue (both of which are essential for catalysis) with pK, 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? Explain your reasoning. (
How would chymotrypsin's catalytic triad be affected by extremely low and extremely high pH values (assuming the rest of the protein remains intact)?
Lysozyme is an antibacterial enzyme found in animals. Residues Asp 101 and Arg 114 are required for efficient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not significantly alter the enzyme's tertiary structure, but significantly reduces its catalytic activity. Explain.
1. Please fully explain (use illustrate where appropriate) the Modes of Enzyme Catalysis exemplified by the serine protease: Chymotrypsin. In your answer discuss employing the illustration whenever possible: the overall reaction mechanism, stability of the reaction transition state, proximity and orientation effects, acid-base catalysis, and covalent catalysis. (c) (0) Ap Asp Toe His Asp 10 C-N bond cleavage HN Ho Ser Ger Binding of substi 196 Ser Gly alto video LBHB NH Sere HAR Proton donation by H (h) Fel of amino product yest OHN Hig Ser Ap (0) Formation of covalent (ES) Alp Me complex Serios
If the substrate for an enzyme catalyzed reaction contained a negative charge, which of the following amino acids would most likely be present in the active site to provide electrostatic destabilization of the ES complex? Leu Val O Asp O LYS QUESTION 15 What is the function of the histidine in the diagram of the mechanism at right with the substrate, a phenylalanine residue? (n) His Asp Nucleophilic affack by water stabilization of a metal ion covalent catalysis electrostatic attraction of the substrate O acid base catalysis 789 Mustly cloudy Click Save and Submit to save and submit. Click Save All Ansuwers to save all answers. here to search

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