Draw the mechanism of action of an HIV protease. Label the substrate, the intermediates, and the products. Indicate each type of catalysis that occurs throughout the mechanism..
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Draw the mechanism of action of an HIV protease. Label the substrate, the intermediates, and the products. Indicate each type of catalysis that occurs throughout the mechanism..
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- Sydney Brennen isolated Salmonella typhimurium mutants that were implicated in the biosynthesis of tryptophan and would not grow on minimal medium supplemented with intermediates in tryptophan biosynthesis, some mutants were able to grow while others remained unable to grow. Review the data attached to order the biosynthetic pathway by both enzymatic step and by intermediate biomolecule. Label the step impacted by each of the mutant cell lines.the following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.9) Considering the enzymatic reaction catalyzed by HIV protease: Options A) hydrolysis is the net reaction observed. B) a peptide bond is cleaved on the carboxyl side of a proline residue. C) a serine residue serves as the nucleophile during the catalytic event. D) inhibitors have been designed to covalently link to the active site just like natural substrates do. E) None of the above is true. F) All of the above are true.
- Using the catalytic mechanism of serine proteases, draw and label a reaction coordinate diagram/graph of the chymotrypsin-catalyzed hydrolysis of a peptide bond.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 Tetrahydromethanopterinpresent the chemical mechanism of the HIV protease. Discuss the mode of action of some inhibitors of this enzyme.
- In serine protease catalytic triad mechanism, the first and second products that leaves the active site are Carboxylic acid and amide respectively Amide and carboxylic acid respectively Ester and amide respectively Carboxylic acid and ester respectivelyWhich of the following protein domains would you expect to find in an "easily druggable" target but NOT in an "undruggable" target. An easily druggable target is defined as a target with an easily accessible active site than can be activated or inhibited. Please Explain. Answer Choices: A) Extracellular domain B) Intracellular domain C) Membrane Spanning domain D) ATP-binding domain E) Protein Binding domainWe 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. H2O
- Aeroderma pigmentosum patients have a 10,000-fold increase in the risk of developing Skin cancer. These patients have to avoid exposure to UV light. Please explain why. To answer the question please: I) name the process that is affected and provide a scheme; 2) indicate template, substrates, sources of energy that are involved in the process; 3) propose the consequences of the process.Draw the catalytic triad of a serine protease at the first tetrahedryl intermediate stage. Your drawing should include the amino acids that make up the triad, any part of the substrate that should be present, and any other molecules that are present in the active site.Describe the experimental evidence that supports lysozyme’s catalysis by acid– base catalysis, covalent catalysis, and transition state stabilization.