Biological Science (6th Edition)
6th Edition
ISBN: 9780321976499
Author: Scott Freeman, Kim Quillin, Lizabeth Allison, Michael Black, Emily Taylor, Greg Podgorski, Jeff Carmichael
Publisher: PEARSON
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Textbook Question
Chapter 3, Problem 4TYK
What is an active site?
a. the location in an enzyme where substrates bind and react
b. the place where a molecule or ion binds to an inactive protein to induce a shape change
c. the portion of a motor protein involved in moving cargo in a cell
d. the site on an antibody where it binds to bacterial cells or viruses
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Students have asked these similar questions
Which statement is/are TRUE about inhibitors?
A. Mode of action of penicillin on bacteria is an example of irreversible inhibition.
B. Increasing the substrate concentration does not affect competitive inhibitors
C. Uncompetitive inhibitors bind only to the enzyme-substrate complex
D. In the Lineweaver-Burke plot, the lines for enzymes in the presence and absence of noncompetitive inhibitor have different x-intercepts.
Which of the following best explains why enzyme catalysis is affected by a change in pH?
A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis
B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH
C. Change in pH alters ionization states of contact amino acids in the active site
D. All enzymes have optimum pH
Which ONE of the following would be most effective as a feedback mechanism for anenzymatic reaction? A. Reduced concentration of the product B. A change in pH C. Increased concentration of substrate D. Temporary binding of a non-substrate molecule in the active binding site
Chapter 3 Solutions
Biological Science (6th Edition)
Ch. 3 - 1. What two functional groups are bound to the...Ch. 3 - 2. What type of bond is directly involved in the...Ch. 3 - What type of information is used to direct...Ch. 3 - 4. What is an active site?
a. the location in an...Ch. 3 - Prob. 5TYUCh. 3 - Prob. 6TYUCh. 3 - 7. Why are proteins not considered to be a good...Ch. 3 - Prob. 8TYUCh. 3 - Prob. 9TYPSSCh. 3 - 10. Make a concept map (see BioSkills 12) that...
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Need a deep-dive on the concept behind this application? Look no further. Learn more about this topic, biology and related others by exploring similar questions and additional content below.Similar questions
- How can a noncompetitive inhibitor affect enzymeactivity without binding to the active site?a. It binds to another location on the enzyme, altering the active site shape.b. It physically blocks the entrance to the active site.c. It alters the shape of the substrate, making it difficult for it to bind to theactive site.d. It degrades the substrate.arrow_forwardAn inhibitor that reversibly binds to a site other than the enzyme's active site is called a(n) a. noncompetitive inhibitor b. competitive inhibitor c. antagonisitc inhibitor d. antibioticarrow_forwardDraw the Lock and Key theory for protein active sites. Then draw what an inhibitor might look-like based on this modelarrow_forward
- What is the active site of an enzyme? A. Specific molecule that acts as the reactant in an enzyme-mediated reaction B. An ion or nonprotein organic molecule that associates with an enzyme and is necessary for its function C. The part of an enzyme where substrates bind and a reaction occurs D. A specific ion or molecule that binds to an enzyme to enhance or inhibit its activityarrow_forwardWhich of the following is true as it relates to the phosphorylation of enzymes? a) Phosphorylation of an enzyme changes its activity. b) Phosphates can be added to R groups of any amino acid. c) Phosphate groups are added by a class of enzymes known as kinases. d) a and c e) a, b and carrow_forwardthe strength of a ligand-protein binding is known as the binding sites a. conformation b. competition c. saturation d. affinityarrow_forward
- In the diagram below, the orange circle represents an effector and the dark purple shapes (both the diamond and the rod) represent a substrate. Based on this information, which statement(s) about the diagram is/are true? Select all that apply. A Allosteric site B Allosteric site C Allosteric site Allosteric effector Active site Allosteric effector Active site, Allosteric effector Novel binding sitearrow_forwardWhich of the following statements is/are correct?a) Enzyme quantities depend on the rate of their synthesis and degradationb) Enzyme quantity is decreased if an amino-acid involved in the catalytic activity is modifiedc) Protein kinase A activity is regulated through protein interaction.d) Kinases control the activity of other enzymes by covalent modification; irreversiblephosphorylation explain each of the following optionarrow_forwardProteases are one of the main drug targets. Choose the False statement regarding proteases. A. Proteases are enzymes that cleave peptide bonds. B. Water is a reactant in the reaction catalyzed by proteases. C. Proteases, like all enzymes show substrate specificity, meaning they cleave only substate that fit the bonding product. D. Proteases rely on the proton transfer from NADH to the substrate. E. Protease mechanism involves only acid-base catalysis.arrow_forward
- Imagine you have a new drug and you believe it activates a particular pathway. You want to prove this by showing that it phosphorylates 4 different proteins that all act at different steps in that pathway. Which experimental technique will you choose and why?arrow_forwardDefine the following terms: a. CAMs b. selectins c. cadherins d. antifreeze glycoprotein e. RNasearrow_forwardWhich one of the following is NOT a ligand?A. Glucagon B. Bacterial proteinC. Air Explain/defend answer above by referring to each option suppliedarrow_forward
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