Provide an example of covalent catalysis in the mechanism of chymotrypsin. What is the nucleophile involved in the formation of this covalent bond? What enabled this group to become a good nucleophile?
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- Briefly describe the role of nucleophilic catalysis in the mechanism of the chymotrypsin reaction.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.What is the mechanism of an enzyme reaction involving a coenzyme for Nucleophilic Addition Rxns? Give
- Enolase has a glutamic acid residue in its active site. Describe the experiment that was done that provided evidence for the proposed function of the glutamic acid residue in catalysis by enolase.Which one of the following best describes the role of water in the reaction that is catalyzed by chymotrypsin? choose the best answer based on your coverage. Water forms several H-bonds with the transition state to stabilize it. Water deprotonates the Ser, converting Ser into a strong nucleophile. Water is a product of the reaction. His deprotonates the water, converting the water into a strong nucleophile. Water serves as a catalyst, being consumed and then regenerated in the reaction.Briefly explain the role of the oxyanion hole for the catalysis of chymotrypsin.
- We talked about the types (mechanisms) of catalysis, including acid-base catalysis, covalent bond formation, metal ion stabilization, and nucleophile attacks of reactants/intermediates following substrate binding. Using the SN2 mechanism for Peptidoglycan cleavage by Lysozyme, indicate the type of catalysis that each of these groups are taking part in. Provide your answers in the thread. Note: this is not part of the assignments for Friday. i. Glu35 ii. Asp52 iii. H2OThe following are coenzymes or cofactors involved in enzymatic reactions. Identify the biochemical role that each plays within a biochemical transformation: Cofactor/Coenzyme Biochemical Role Thiamine pyrophosphate Coenzyme A Adenosine triphosphate Heme Lipoamide TetrahydromethanopterinUDP-glucuronosyltransferase enzymes bind the organic compound UDP-glucuronic acid (UDP-GA) in order to catalyse the transfer of a glucuronic acid group from UDP-GA to a drug molecule, releasing UDP from the active site as a product. UDP is then regenerated by the activity of another enzyme. What terms could be used to describe UDP-GA?
- Isocitrate lyase cleaves the 6-carbon isocitrate to glyoxylate and succinate.Draw a plausible mechanism for this reaction.Which of the following statements is true about the chymotrypsin reaction? 1. The catalytic triad at the active site is formed by three residues: His, Gly, and Ser 2. When the substrate is p-Nitrophenylacetate, the rate-limiting step is the release of p-Nitrophenolate. 3. During the reaction, LBHB forms when the proton is donated to His from Ser or water. 4. The chymotrypsin reaction involves “only” specific acid-base catalysis 5. The “oxyanion hole” is formed by the amide nitrogens of Ser and GluDescribe the experimental evidence that supports lysozyme’s catalysis by acid– base catalysis, covalent catalysis, and transition state stabilization.