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

How has the analysis of enzyme kinetics been fundamental to the modern design of pharmaceuticals?

What are enzymes? What distinguishes enzymes from regular chemical catalysts? On the specificity of enzyme action, please comment. Which factor accounts for their specificity the most? Describe the enzyme catalysis mechanism.

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…

Where is the active site for this enzyme located?

One way of expressing the rate at which an enzyme can catalyze a reaction is to state its turnover number. The turnover number is the maximum number of substrate molecules that can be acted on by one molecule of enzyme per unit of time. The table gives the turnover number of four representative enzymes. Enzyme Substrate Turnover number (per second) Ribonuclease RNA 100 Fumarase fumarate 800 Lactate dehydrogenase lactate 1000 Urease urea 10,000                               How many molecules of urea can one molecule of urease act on in 12.0 min ?

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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

The figure below represents a reaction in the presence and absence of an enzyme catalyst. What can you conclude about this reaction? energy activation energy activation energy 1 uncatalysed reaction catalysed reaction A) It is endergonic in the absence of the enzyme. B) It will proceed more quickly in the presence of the enzyme. C) Once the reaction has reached equilibrium, there will be more product in the enzyme-catalyzed reaction. D) It has a negative AG. OE) Both B and D are true

Given: Your professor gives you a vial of enzyme and a vial of substrate. The product of this reaction is fluorescent and you can measure the concentration of the product as a function of time. (answer a, b, and c)a) Your professor tells you to quantify how much product is being produced per minute at thebeginning of the experiment. What exactly are you measuring?b) On the same plot, show the kinetic curve for an increased quantity of enzyme. Assume a 2x concentration. Indicate Km and Vmax.c) You don’t have a computer hand. Sad. How can you plot the data such that you can get important Michaelis-Menten values?