Biochemistry: The Molecular Basis of Life
6th Edition
ISBN: 9780190209896
Author: Trudy McKee, James R. McKee
Publisher: Oxford University Press
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Question
Chapter 6, Problem 53SA
Summary Introduction
To review:
The reason behind the catalytic activity of ribonucleic acid (RNA) molecules.
Introduction:
Enzymes are protein molecules thatcatalyze the biochemical reactions by lowering down the activation energy. All the enzymes are made up of proteins, except for ribozyme, which is made up of RNA. Ribozymes are found in ribosomes.
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Most enzymes are quite specific, catalyzing a particular reaction on a set of substrates that are structurally quite similar to
one another.
Why are highly specific enzymes advantageous from a biological perspective?
They allow catalyzed reactions to produce potentially useful by-products.
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They allow an inhibitor to simultaneously inhibit multiple steps in a metabolic pathway.
They allow control of which reactions occur at appreciable rates.
Why are most enzymes highly specific from a chemical perspective?
Enzymes generally requires a tight fit between enzyme and substrate.
Interactions between the enzyme and the substrate stabilize the substrate.
The active sites of enzymes are always identical in shape to the substrates they bind.
The formation of weak interactions between the enzyme and the substrate requires energy.
Streptokinase is an enzyme produced by Streptococci bacteria and is used to digest fibrin clots. It is therefore very effective at eliminating blood clots that cause heart attacks and strokes. Why does a physician not worry that injecting streptokinase will also destroy healthy tissue in their patients? – this answer should discuss the specificity of enzymes for their substrates, defined by the shape of the active site.
Find an enzyme that is used by humans for some industrial or useful process (apart from its original purpose; e.g. food production, textiles, agriculture, clinical diagnosis, medical treatment, biofuel production, material polymerization, etc.).
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200 words only
Chapter 6 Solutions
Biochemistry: The Molecular Basis of Life
Ch. 6 - Prob. 1QCh. 6 - Prob. 2QCh. 6 - Prob. 3QCh. 6 - Prob. 4QCh. 6 - Prob. 5QCh. 6 - Prob. 6QCh. 6 - Prob. 7QCh. 6 - Prob. 8QCh. 6 - Prob. 9QCh. 6 - Prob. 1RQ
Ch. 6 - Prob. 2RQCh. 6 - Prob. 3RQCh. 6 - Prob. 4RQCh. 6 - Prob. 5RQCh. 6 - Prob. 6RQCh. 6 - Prob. 7RQCh. 6 - Prob. 8RQCh. 6 - Prob. 9RQCh. 6 - Prob. 10RQCh. 6 - Prob. 11RQCh. 6 - Prob. 12RQCh. 6 - Prob. 13RQCh. 6 - Prob. 14RQCh. 6 - Prob. 15RQCh. 6 - Prob. 16RQCh. 6 - Prob. 17RQCh. 6 - Prob. 18RQCh. 6 - Prob. 19RQCh. 6 - Prob. 20RQCh. 6 - Prob. 21RQCh. 6 - Prob. 22RQCh. 6 - Prob. 23RQCh. 6 - Prob. 24RQCh. 6 - Prob. 25RQCh. 6 - Prob. 26RQCh. 6 - Prob. 27RQCh. 6 - Prob. 28RQCh. 6 - Prob. 29RQCh. 6 - Prob. 30RQCh. 6 - Prob. 31RQCh. 6 - Prob. 32RQCh. 6 - Prob. 33RQCh. 6 - Prob. 34RQCh. 6 - Prob. 35RQCh. 6 - Prob. 36RQCh. 6 - Prob. 37RQCh. 6 - Prob. 38RQCh. 6 - Prob. 39RQCh. 6 - Prob. 40RQCh. 6 - Prob. 41RQCh. 6 - Prob. 42RQCh. 6 - Prob. 43FBCh. 6 - Prob. 44FBCh. 6 - Prob. 45FBCh. 6 - Prob. 46FBCh. 6 - Prob. 47FBCh. 6 - Prob. 48FBCh. 6 - Prob. 49FBCh. 6 - Prob. 50FBCh. 6 - Prob. 51FBCh. 6 - Prob. 52FBCh. 6 - Prob. 53SACh. 6 - Prob. 54SACh. 6 - Prob. 55SACh. 6 - Prob. 56SACh. 6 - Prob. 57SACh. 6 - Prob. 58TQCh. 6 - Prob. 59TQCh. 6 - Prob. 60TQCh. 6 - Prob. 61TQCh. 6 - Prob. 62TQCh. 6 - Prob. 63TQCh. 6 - Prob. 64TQCh. 6 - Prob. 65TQCh. 6 - Prob. 66TQCh. 6 - Prob. 67TQCh. 6 - Prob. 68TQCh. 6 - Prob. 69TQCh. 6 - Prob. 70TQCh. 6 - Prob. 71TQCh. 6 - Prob. 72TQCh. 6 - Prob. 73TQCh. 6 - Prob. 74TQCh. 6 - Prob. 75TQCh. 6 - Prob. 76TQCh. 6 - Prob. 77TQCh. 6 - Prob. 78TQCh. 6 - Prob. 79TQCh. 6 - Prob. 80TQCh. 6 - Prob. 81TQ
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Similar questions
- Enzymes are proteins that increase the rate of chemical reactions by lowering the energy activation required to facilitate the process. Explain the generalized and sequential enzyme mechanism of action (hint: from substrates to products).arrow_forwardIn any given enzyme, the active site is only a small portionof the entire molecule. Synthesis of such a relatively largemolecular machine requires an enormous amount of cellular energy. Explain why this inefficiency is tolerated.arrow_forwardInhibitors are common in biological systems. Why might some organisms release enzyme inhibitors into their surrounding environment?arrow_forward
- Lead exerts its poisonous effect on enzymes by two mechanisms. Which mechanism is irreversible and why?arrow_forwardThe covalent catalytic mechanism of an enzyme depends on a single active site Cys whose pK is 8. A mutation in a nearby residue alters the micro environment so that this pK increases to 10. Would the mutation cause the reaction rate to increase or decrease? Explain.arrow_forwardMany organisms are able to live in extremely cold or hot temperatures, for example, the thermophilic bacteria that live in the hot springs of Yellowstone National Park. Draw a figure representing the predicted activity curve for enzymes in bacteria found in these habitats.arrow_forward
- Often, an enzyme requires a cofactor or prosthetic group in its active site in order to be an efficient catalyst. Many such cofactors are synthesized by plants and obtained in the diet as vitamins. Find a description in your text of a particular B vitamin. Give its name and describe its biological function in terms of the name(s) and function(s) of the enzyme(s) that require it.arrow_forwardLiving things must regulate the rate of catalytic processes.Explain how the cell regulates enzymatic reactions.arrow_forwardWhen biological enzymes are heated, they lose their catalytic activity. The change that occurs is an ENDOTHERMIC and SPONTANEOUS process. Based on the given information, what is the sign of Δ˚G? Based on the given information, what is the sign of Δ˚H? Is the structure of the original enzyme MORE or LESS ordered than the new form? Explain your answer.arrow_forward
- Some enzymes can be regulated by covalent modification, in which a group is covalently bonded to an amino acid side chain. Phosphorylation of side chains is a common regulatory covalent modification. In this essay, you will explore phosphorylation of side chains. Compare and contrast the types of interactions a free alcohol side chain such as serine could make with that of a phosphorylated alcohol such as phosphoserine (pSer). Could this modification affect the 3D structure of the protein? How? Imagine you are trying to separate a protein containing an unphosphorylated S residue from the same protein containing a pSer residue. Discuss how you could use ion-exchange chromatography to separate these two proteinsarrow_forwardFor a lot of enzymes that work on fatty acids, the rate determining step is the release of the product from the active site. This means that the activation energy for product release is much higher than the free energy of catalysis. What enthalpic or entropic contributions would make the activation energy for product release so high and explain?arrow_forwardIf you can clearly visualize the chymotrypsin mechanism of action, you should be able to picture the structure of the transition state right after the enzyme attacks the first substrate. Think hard about what we have covered, and visualize that transition state accurately:arrow_forward
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