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.

The enzyme catalase is found in nearly all living organisms that are exposed to oxygen. This enzyme…

Answered: Write a paragraph or more to introduce…

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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Give a complete and well descriptive definition of the following:1.1 Enzyme catalysis1.2 Co-enzyme1.3 Negative heterotropic co-cooperativit
The milieu wherein enzymes occur in vivo is dramatically different from in vitro experiments, which is often used to investigate enzyme. Give an overview of this as well as the nature of enzyme reactions in vivo. Name, in addition, the factors affecting the concentration of enzymes in vivo.
As biological catalysts, enzymes play a fundamental role in many cellular processes. Which of the following statements about enzymes is correct? 1. Enzymes are essential for anabolic pathways; they are not required for catabolic pathways. 2. While an increase in temperature can increase the rate of an uncatalyzed reaction, it can’t increase the rate of an enzyme-catalyzed reaction. 3. Enzymes force substrates into unique conformations that do not occur in the absence of an enzyme. 4. Enzymes decrease the free energy of a reaction’s transition state. A. 1, 2 and 3 B. 1 and 3 C. 2 and 4 D. 4 only E. All of 1, 2, 3 and 4 are correct
A multi-enzyme complex Is made up of three polypeptide chains, A, B and C. A is associated with decarboxylase activity; B is a transacetylase, while C is a dehydrogenase. When the protein was placed in a nonpolar solvent, then run in PAGE, two protein bands were observed. Enzyme assays showed that one protein band exhibited decarboxylase activity while the other has both transacetylase and dehydrogenase activities. When the protein was also placed in an aqueous solvent at pH 5.0, then run in electrophoresis, two protein bands were also detected. Further enzyme assays also showed that one protein band exhibits transacetytase activity while the other has both decarboxylase and dehydrogenase activities. a. What types of non-covalent interactions are possible between A, B and C? b. Addition of urea, a reducing agent gave 4 bands in the PAGE profile with a subsequent loss of decarboxylase activity. What could be the reason for the observed result? Explain briefly in terms of the structure…
2 3 4 5 B Type here to search 6 7 8 9 10 O O 3 4 5 6 7 8 9 10 pH Level The 11 A researcher investigates the effect of eight different pH levels on the reactions catalyzed by the enzyme catalase. All other factors are held constant. Based on the following graph, what can you conclude about the relationship between the catalase and pH? Reaction Rate by pH Level O T 12 13 optimal (highest) pH level of catalase is 6.5. As the pH level increases, the reaction rate increases. As the pH level decreases, the reaction rate increases. There is no relationship between the pH level and the reaction rate. 14 W 15 16 DELL 17 18 19 20 21 22 → G 23 24 25 3:57 PM 9/15/2022 D D
List three effects of macromolecular crowding on the properties of enzymes and the reactions they catalyze.
How has the analysis of enzyme kinetics been fundamental to the modern design of pharmaceuticals?
Sucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…
Is the data that you are collecting in the above table quantitative or qualitative? Explain why. Which treatment had the least amount of browning? Which had the most? Why do you think you obtained these results? Remember that the enzyme polyphenol oxidase is a protein! For each treatment, apply your knowledge of how temperature, pH, and salt concentration affect enzyme activity and explain why you got the results that you did. Include bonds and the levels of protein structure that you explored in Activity A in your answer. How does temperature impact the rate of enzyme activity? If you were to leave the apple in the refrigerator longer, why would it eventually brown? Explain based on what you know about enzyme activity. How does pH and its impact on specific types of bonds explain the results you obtained in your lemon juice treatment? Include bonds and levels of protein structure in your answer. How does salt and its impact on specific types of bonds explain the results you obtained…
What is the importance of enzyme kinetics in the field of pharmaceutical studies? asap please
create a single illustration that will interrelate or link the two opposing pathways, the Glycogenesis and Glycogenolysis. I want you to include the enzyme in each step and include some important by-products as well. From the illustration, I want you to encircle the intermediate molecule to highlight the link between the two processes. Aside from the illustration, I want you to compare and contrast the two pathways in terms of function, number of reaction steps, and usage of UTP. You can tabulate this part to make it simpler.
You are required to isolate, purify and verify the purity of an enzyme from cytosol of a plant species for industrial use. Briefly describe how the desired enzyme can be obtained for the intended purpose stating the techniques involved. (MW of enzyme = 60 kbp)

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