Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
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Chapter 28, Problem 8P
Interpretation Introduction
Interpretation:
The advantage of a non-competitive inhibitor as a potential drug in comparison with a competitive inhibitor should be determined.
Concept introduction:
Non-competitive inhibition can be defined as a type of enzyme inhibition. In this inhibition, usually, the inhibitor diminishes the enzyme activity. The inhibitor gets attached to the enzyme in a similar manner as the substrate does. It occurs even if it has been previously bound or not to the substrate.
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I. Active site analysis.
Below is a diagram of a putative active site for Monoamine oxidase. As we learned, the purpose of
tertiary structure is to form a scaffold so you can orient just a few amino acids in the right orientation
to promote binding and/or catalysis. The position where this occurs is the active site. The amino acid
architecture of an active site is designed to bind substrates. Amino acid side chains are capable of
hydrogen bonding, ionic and hydrophobic interactions. Fill in each amino acid that you think is
suitable for interacting with the part of the substrate it is closest to. Assume the pH will be at 7.0
a.a.#1
a.a.#2
a.a.#6
HO
Lond
NH₂
НО
a.a.#5
OH
a.a.#3
a.a.#4
Please help. An explanation will be very helpful. Thank you
Show solutions. Thanks.
Chapter 28 Solutions
Biochemistry (Looseleaf)
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Similar questions
- In full details. Define 'activation energy' of an enzyme catalysed single substrate reaction and mention the effects of an enzyme on this energy.arrow_forwardNH2 'N. NH NH NH2 Benzamidine and Leupeptin are competitive trypsin inhibitors. They are shown in their deprotonated forms at high pH. Modify the above drawings to show the protonation and charge at pH 7.0 Draw competitive inhibitors for chymotrypsin based on these structures IZ ZI ZIarrow_forwardX Incorrect. Suppose that an uncatalyzed reaction is spontaneous because AG has a value of -10 kcal/mol. An enzyme that catalyzes the reaction is identified. What effect will the enzyme have on the rate of the reaction? Choose all that are correct. The enzyme increases the AG value. The enzyme increases the rate of reaction. The enzyme decreases the rate of reaction. The enzyme decreases the AG value. The enzyme raises the activation energy. The enzyme lowers the activation energy.arrow_forward
- Explain well. Thank you expert. Asap pleasearrow_forwardHi, help please. Discuss each method of regulating phosphofructokinase below as indicated by the circle. Discuss 1.) The type of regulation occurring, 2.) What compound or condition performs the regulation, 3.) How/why it influences the enzyme activity.arrow_forwardGiven the active site and reaction mechanism below, what is the mechanism of irreversible inhibition of the inhibitor provided? NH* Active Site *H₂N. HN NH₂ +H₂N HN H₂N NH₂* Non-specific inhibition Uncompetitive Inhbitor Transition State Analog i Affinity-based inhibition Mechanism-Based Inhibition Reaction Mechanism *H₂N. NH HN- HN [*] H₂N NH₂ 2+Mn Mn²+ i +H₂N. H₂N i H₂N NH₂ HO Inhibitor *H₂N. B OH r View site informatiarrow_forward
- Select all that apply. Which of the following are not properties of enzymes? not required to sustain the life of an organism sensitive to pH and temperature of their environment able to interact with all compounds or substrates large proteins with a special surface patternarrow_forwardantidote for tetrodotoxin poisoning. First, what is the name of the made up drug? Second, describe the details of how the drug will work. description should contain details of how the drug will act at the cellular and/or molecular level.arrow_forwardRecall that vmax is achieved only at high substrate concentrations. Do you predict that vmax will change when an uncompetitive inhibitor is introduced? Why or why not?arrow_forward
- Noncompetitive inhibition can often be explained by which of the following models? the induced fit model the lock and key model both (a) and (b) neither (a) nor (b)arrow_forwardGiven the active site and reaction mechanism below, what is the mechanism of irreversible inhibition of the inhibitor provided? NH+ Active Site Mn²+ *H₂N. HN N NH H₂ Mn²+ +H₂N. HN H₂N "NH₂ Non-specific inhibition Uncompetitive Inhbitor I Transition State Analog Affinity-based inhibition Mechanism-Based Inhibition Reaction Mechanism HN NH *H₂N HN HẠN TÌNH, 2+Mn Mn²+ ‡ +H₂N. H₂N H₂N NH₂ Inhibitor i *H₂N. B но в он OH View site informatarrow_forwardHelp please. This question is specifically asking for the identification of the biomolecules that are attached to the sphingosine core, then we need to answer what bond causes those biomolecules to be connected to the sphingosine, what reaction created that bond (maybe addition or oxidation etc.), what were the starting materials and lastly what reagents or conditions are needed for the reaction to occur. Thank you!arrow_forward
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