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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- Explain the basis for the following statement: As a coenzyme, pyridoxal phosphate is covalently bound to enzymes with which it functions; yet during catalysis the coenzyme is not covalently bound.What is the mechanism of an enzyme reaction involving a coenzyme for Nucleophilic Addition Rxns? GiveEnolase 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.Put these steps in the mechanism of chymotrypsin catalysis in order from first to last. Note that some references may not break out each of these steps individually, but all steps should be ordered. There will be eight steps.
- 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.Isocitrate lyase cleaves the 6-carbon isocitrate to glyoxylate and succinate.Draw a plausible mechanism for this reaction.The 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 Tetrahydromethanopterin
- UDP-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?Describe the experimental evidence that supports lysozyme’s catalysis by acid– base catalysis, covalent catalysis, and transition state stabilization.Given the active site diagram below, indicate the mechanism(s) of catalysis. 5 HO OH HN OH ΝΗ *HN ΝΗ Zn²+ Acid-base, Metal ion 3 Metal ion, By Approximation Metal ion Acid-Base, By Approximation Acid-base