
Biochemistry
9th Edition
ISBN: 9781319114671
Author: Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.
Publisher: W. H. Freeman
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Transcribed Image Text:The effect of pH on the activity of an enzyme was examined. At its active site, the enzyme has an
ionizable group that must be positively charged for substrate binding and catalysis to take place. The
ionizable group has a pKa of 6.0. The substrate is negatively charged throughout the pH range of the
experiment.
At what pH = 9, the enzyme will be operating at
answer is either Vmax, 1/2 Vmax or less than 1/2 Vmax (type in one of the 3 phrases as they are written
here.)
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- An enzyme catalyzes the reaction M-N. The enzyme is present at a concentration of 0.0000000022 M, and the Vmax is 0.0000028 Ms1. The Km for substrate is 5.5 µM. Calculate kcat-arrow_forwardConcentrations in biochemical systems are often very dilute. Consequently, scientific notation and logarithms are often used to express concentrations. In scientific notation, numbers are expressed as coefficient x 10" To convert a number to scientific notation, proceed as follows: 1. Move the decimal place so that there is one digit in front of the decimal. 2. Account for the moved decimal in the value of x. If the decimal moved to the right, x is negative; if it moved to the left, x is positive. A logarithm is basically an exponent. Unless otherwise indicated, a logarithm is the a of 10". The numbers after the decimal point are significant; the number before the decimal just identify the location of the decimal point for the number. Notice that it is easy to estimate a logarithm from scientific notation; it's the exponent! Logarithms are commonly used to express the concentration of H. The pH is defined as pH= log (In), where the base number is 2.303. The same general rules as logs…arrow_forwardIn a uni uni enzyme reaction, what is the substrate concentration relative to Km when anenzyme operates at 0.95 * V. What about 0.99 * V?arrow_forward
- Draw the Michaelis-Menten graph you would predict for the enzyme using 50 nM and 100 nM of enzyme in your assays.arrow_forwardAn enzyme contains an active site aspartic acid with a pKa = 5.0, whichacts as a general acid catalyst. On the accompanying template, draw thecurve of enzyme activity (reaction rate) versus pH for the enzyme (assumethat the protein is stably folded between pH 2–12 and that the active siteAsp is the only ionizable residue involved in catalysis). Briefly explain theshape of your curve.arrow_forwardIs 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…arrow_forward
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