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
In modern and recent application of a catalyst and an enzyme used in a chemical and biochemical reaction a) give the commercial or trade name of the catalyst and enzyme of both rxn b) the properties of the catalyst and enzyme (e.g., shape, size, colour, price).
Match the classes of enzymes with their functions: Catalyze cleavage of molecules driven by addition of water Catalyze transfer of functional groups within a molecule Catalyze linking two molecules into a larger one Catalyze electron transfer reaction between two molecules Catalyze transfer of functional groups between different molecules Hydrolyze peptide bonds [Choose ] [Choose] [Choose ] [Choose ] [Choose] [ Choose ] Proteases Transferases Oxidoreductases Ligases Hydrolases Isomerases + + + + ‡
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.
Xylanase is a class of hydrolyase enzymes that can break down hemicellulose into fermentable sugars. Xylanase is widely used in the pulp and paper industry for chlorine-free enzymatic bleaching of wood pulp. Besides that, xylanase is also applied in several industries like feed, pharmaceuticals, food and beverages. At the industrial scale, xylanases are mainly produced by microorganisms such as bacteria and fungi. 1. Solid-state fermentation and submerged fermentation are the two major techniques applied in the production of xylanase enzymes. Outline how the xylanase enzymes are produced using these two techniques. Identify the advantages and disadvantages of these two techniques. 2. Select a suitable microorganism and substrate that could be applied to produce xylanase enzymes economically at industrial scale via the submerged fermentation techniques with justifications.
enzymes are naturally occurring catalysts responsible for various biochemical reactions. Give a modern and recent application of an enzyme used in a biochemical reaction a - the commercial or trade name of the catalyst and enzyme. b - the properties of the catalyst and enzyme (e.g., shape, size, colour, price). c - the advantages and the disadvantages of the chosen catalyst and enzyme d - catalytic reaction (e.g., the reactant, product, reaction equation, phase, selectivity, promoter, catalyst support, operating temperature & pressure).

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