Briefly discuss the role of thiamine pyrophosphate in enzymatic reactions, using material from this chapter to illustrate your points.
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Q: Select all the intermediates that would be isolated if the enzyme malate dehydrogenase was inhibited
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Q: To understand the entire glycolytic pathway better, kindly complete the table Structural activator…
A:
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Q: E. coli can convert glutamate to ornithine. Describe the two reactions that do so.
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Q: Given the active site below, which best describes the mechanism(s) of catalysis?
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Q: Discuss oxidative decarboxylation, using areaction from this chapter to illustrate your points.
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Q: Describe how coenzyme A is important in the thiolase-catalyzed reaction.
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Briefly discuss the role of thiamine pyrophosphate in enzymatic reactions, using material from this chapter to illustrate your points.
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Solved in 3 steps
- Suggest the possible class of enzyme (or name of enzyme) for each of theenzyme-catalyzed reactions below. Briefly explain your answer.To understand the entire glycolytic pathways better, kindly complete the table below Steps Structural Formula Enzyme, activator and coenzyme required Structural formula of the product Is the reaction reversible or irreversible?Describe the characteristics of allosteric enzymes and explain how the kinetic curves of such enzymes differ from Michaelis– Menten enzymes.
- Provide the general outline of biosynthesis of oxylipins and cite enzyme in each step. ANSWER THIS PLEASE ASAP!!!Suggest a name for an enzymes that catalyzes each of the following reactions.1. Hydrolysis of Lactose 2. Oxidation of Nitrate3. Decarboxylation of Citrate4. Reduction of ExalateWhat is the step by step process Embden-Meyerhoff-Parnas pathway? Can you please explain in detail the important enzymes/pathways involved thank you
- 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.the following is a coenzyme or cofactor involved in enzymatic reaction. identify the biochemical role that S-adenosylmethionine plays within a biochemical tranformation.Suggest the possible class of enzyme (or name of enzyme) for each of the enzyme-catalyzed reactions below. Briefly explain your answer.
- What are catalases? Why are they called antioxidant enzymes? Give the industrial applications of this enzyme.Using lysozyme as an example, what can an enzyme’s structure reveal about its catalytic mechanism?Enzymes are stereochemically specific; that is, they oftenconvert only one stereoisomeric form of substrate intoproduct. Why is such specificity inherent in theirstructure?