You are trying to confirm that an enzyme you are studying has the following aminoacid in its active site, and that this amino is critical for catalysis:HN-H3NⓇWhich of the following inhibitors could you use to provide evidence of theimportance of this amino acid for enzyme function?Tetranitromethane2,3-ButanedioneDiethylpyrocarbonatelodoacetateNevirapine

Amino acid inhibitors are molecules that can interfere with the function of specific amino acids by…

Answered: You are trying to confirm that an…

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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In the meantime, here's a sneak peak: you will be investigating the enzyme called catalase. Write a paragraph or more to introduce the enzyme catalase. Include the following details in your introduction: • the substrate and products of catalase, • the type of reaction performed by catalase, • factors that could increase or decrease the activity of an enzyme like catalase, • how catalase is used by cells, • in what type of cells is catalase found, • an industrial use of catalase.
With appropriate chemical structures, explain the mechanism (mode-of-action) of fluoroacetate poisoning? Example: Step 1: Fluoroacetate is converted to Product “A”. This reaction is catalyzed by Enzyme __________________________ Structures of fluoroacetate and the product “A”. Name of Enzyme. Step 2: Product “A” from Step 1 is converted to Product “B.” Catalyzed by enzyme 2. Structure of Product B and name of Enzyme 2. etc.
A patient had severe acid reflux symptoms and decided to take the antacid, Amphojel (aluminum hydroxide). Answer both parts. If this is an oxidation-reduction (redox) and/or precipitation reaction, then show work to support your answer. If this is not an oxidation-reduction (redox) and/or precipitation reaction, then show work to support your answer. Assume that Calcium Iodide and Sodium Oxalate are the starting substances (reactants) in the reaction: What type of reaction(s) is/are being represented by the chemical reaction?
A catalase is an antioxidant enzyme that requires ferric ion for catalysis. Under conditions of iron deficiency, when the catalase lacks ferric ion, it would be referred to as: O prosthetic group O holoenzyme ароenzyme coenzyme
Which of the following aspects of catalysis by enzymes can NOT be explained by the Fischer Lock and Key Hypothesis? Enzymes will lower the activation energy barrier for reaction. Enzymes will specifically recognize their substrates. Appropriate substrates will bind to the enzyme to form a Michaelis complex. Enzymes have an "active site" where appropriate substrates will be bound. Two of the above cannot be explained by the Fischer "Lock and Key" Hypothesis.
1) Describe the change of Cis-aconitate to Isocitrate. 2) Are enzymes changed during a reaction they catalyze? 3) What does "induced fit" mean when talking about enzymes
Please answer this question and the highlighted question is wrong please explain why and give me the correct answer
For the three biochemical transformations below provide the names of the enzyme (or enzymes) responsible for the transformation, and identify by name or chemical structure the other necessary reactants and other products associated with each transformation. Make sure that your answer presents the missing information in a way that clearly connects it to the appropriate reaction.
Discuss in a short paragraph (3–5 sentences for each mutation) whether or not the enzyme is likely to completely lose catalytic activity if the following mutations are carried out. You may assume that steric effects do not distort the active site so much that catalysis cannot take place; focus your analysis on discussing the chemistry the amino acid side chains are able to perform and the properties that enable them to do so. Mutation 1: H to E Mutation 2: H to N Mutation 3: S to D Mutation 4: S to C
If you can clearly visualize the chymotrypsin mechanism of action, you should be able to picture the structure of the transition state right after the enzyme attacks the first substrate. Think hard about what we have covered, and visualize that transition state accurately:
Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are true
The structure of a metalloenzyme active site is down below(black picture). Describe, from a chemical and structural perspective, how the reactive site is designed to facilitate its catalytic reaction. The example below suggests the level of detail that is required. Make sure that you explain what the metal is doing, what the reaction is, and its biological significance.

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