Which statement BEST explains why enzymes bind to specific substrates? An enzyme can be inhibited so its active site is altered An enzyme folds differently in the presence of different substrates Different amino acid sequences cause variations in the shapes of an enzyme's active sites Enzyme-substrate binding is based on size so only large enzymes can bind to large substrates

Which statement BEST explains why enzymes bind to specific substrates? An enzyme can be inhibited so its active site is altered An enzyme folds differently in the presence of different substrates Different amino acid sequences cause variations in the shapes of an enzyme's active sites Enzyme-substrate binding is based on size so only large enzymes can bind to large substrates

Chemistry

10th Edition

ISBN:9781305957404

Author:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Publisher:Steven S. Zumdahl, Susan A. Zumdahl, Donald J. DeCoste

Chapter1: Chemical Foundations

Section: Chapter Questions

Problem 1RQ: Define and explain the differences between the following terms. a. law and theory b. theory and...

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1. What reaction is catalyzed by the enzyme carbonic anhydrase? Which metal ion serves as a cofactor for carbonic anhydrase? Explain how this metal ion is able to assist in catalyzing the reaction. 2. In relation to enzymes, what is the difference between a cosubstrate and a prosthetic group? Give one example of each.
Find an example of an enzyme that was NOT discussed in the book or video lectures. Answer the following questions about the enzyme that you chose. a) What is the chemical reaction that is catalyzed by the enzyme? b) Why is this enzyme/chemical reaction important to the organisms in which it occurs? Please post your source (include a link to the website you read your information)
The following graph shows the activity versus pH curve for pepsin, an enzyme that breaks down proteins into smaller peptides. Estimate its optimum pH. Maximum activity No activity pH 0 pH 3.8 pH 2 O pH4 Pepsin 01 2 3 pH 4 5
What is the process that involves the breaking of intermolecular forces that hold an enzyme into the ordered three dimensional shape? A) denaturation B) allosteric inhibition C) enzyme inhibition D) protein folding E) post-translational modification
Two-dimensional gel electrophoresis of proteins in a cell extract provides a qualitative way to compare proteins with respect to intracellular abundance. Describe a quantitative approach to determine the number of molecules of an enzyme per cell.
An enzyme has an optimal pH of 7.1 and an optimal temperature at 37° C. Which statement describes a reaction catalyzed by this particular enzyme at a constant temperature of 20° C? the reaction will slow down and then increase as the temperature increases O there is no effect O the reaction will be slower than if it ran at 37° C O the enzyme will provide an alternate active site so the reaction can proceed the enzyme will be denatured
Please study the table. Given the data collected for an enzyme-catalyzed reaction, what is the approximate KM for this enzyme? ISI mM Vo (umol/min) 8 x 10 80 2 x 10 140 8x 10-5 224 4 x 10 3 277 2x 10 2 280 1x 10- 279 2x10 mM 140 umol/min 280 jamol/min 2x 10 mM 98x10mM
29. In chymotrypsin both histidine and serine are important amino acids in the catalytic reaction. Below is an image showing one step of the reaction. Describe what is happening and the roles histidine and serine are playing. In your answer be sure to use correct terms in describing the type of enzyme mechanism being done each amino acid. His Asp 102 H₂C CH₂ Ser (195) CH₂ 4 Asp 102 H₂C CH₂ His 57 New N-terminus of cleaved polypeptide R chain Ser 195 CH₂
Bovine chymotrypsinogen has a molecular weight of 25.6 kDa. Amino acid analysis shows that this enzyme is 9% alanine (Mr 89.1). Calculate how many alanine residues are present in a molecule of bovine chymotrypsinogen. Round your answer to the nearest whole number.
The following graph is showing the effect of catalyzed reaction. Rate of reaction A enzyme concentration substrate concentration pH temperature B on the rate of an enzyme
Make the best matches to the following three terms. noncompetitive inhibitor inhibitor competitive inhibitor binds away from the active site of an enzyme to reduce the ca^ reduces the catalytic activity of an enzyme binds away from the active site of an enzyme to reduce the catalytic activity of an enzyme binds to the active site of an enzyme to reduce the catalytic activity of an enzyme
9. Describe the binding between an irreversible inhibitor, such as arsenic, and an enzyme. 10. Explain the difference between reversible competitive and noncompetitive inhibition.