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Concept explainers
(a)
Interpretation: The validation of the given pairing of concept related to regulation of enzyme activity has to be stated.
Concept introduction: The regulation of enzyme activity is very important within a cell. There are three mechanisms associated with the regulation of enzyme activity: 1. feedback control, 2. proteolytic enzymes and zymogens, and 3. Covalent modification.
(b)
Interpretation: The validation of the given pairing of concept related to regulation of enzyme activity has to be stated.
Concept introduction: The regulation of enzyme activity is very important within a cell. There are three mechanisms associated with the regulation of enzyme activity: 1. feedback control, 2. proteolytic enzymes and zymogens, and 3. Covalent modification.
(c)
Interpretation: The validation of the given pairing of concept related to regulation of enzyme activity has to be stated.
Concept introduction: The regulation of enzyme activity is very important within a cell. There are three mechanisms associated with the regulation of enzyme activity: 1. feedback control, 2. proteolytic enzymes and zymogens, and 3. Covalent modification.
(d)
Interpretation: The validation of the given pairing of concept related to regulation of enzyme activity has to be stated.
Concept introduction: The regulation of enzyme activity is very important within a cell. There are three mechanisms associated with the regulation of enzyme activity: 1. feedback control, 2. proteolytic enzymes and zymogens, and 3. Covalent modification.
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Chapter 21 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- The steps of the chymotrypsin mechanisms are listed below (1-7). Put the steps of chymotrypsin mechanism in the correct order. Figure representing chymotrypsin mechanism is given for reference. a.The portion (N-terminal end) of original substrate with the new C terminus diffuses away b. Substrate binding c. His 57 catalyzes removal of H from Ser 195 hydroxyl; Ser 195’s nucleophilic O attacks carbonyl C of substrate; tetrahedral intermediate is formed d. Water binding; water is deprotonated by His 57; resulting OH nucleophilically attacks carbonyl of remaining substrate; tetrahedral intermediate is formed e. His 57 donates H to N of…arrow_forwardWhich 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.arrow_forwardDefine the following terms: a. genetic control b. proenzyme c. zymogen d. positive cooperativity e. negative cooperativityarrow_forward
- Choose the correct answer in the following questions below: A noncompetitive inhibition is best overcome (or reversed) by: Increasing [enzyme] Increasing [Substrate] Increasing [product] All of the above The infectious prion protein which are believed to cause a neurodegenerative disease by acting as a template to misfold other cellular prion proteins are usually β-helices. True False An apoenzyme is a component of all conjugated enzymes, while a coenzyme is a component of some conjugated enzymes True Falsearrow_forwardDefine the following terms:a. oxidoreductaseb. lyasec. ligased. transferasee. hydrolasef. isomerasearrow_forwardSelect all the true statements about sequential versus concerted models of allostery. a. In sequential allostery, binding of the substrate on one end of an enzyme causes a conformational change on the other end which propagates to another enzyme and enables easier binding of a second substrate to the second enzyme b. No conformational changes occur in either model c. In concerted allostery, the two forms of the enzyme exist in equilibrium because of a conformational change independent of substrate binding d. In concerted allostery, binding of the substrate to one of the forms is favorable (but not to the other) and binding of the second substrate is enhanced on the favorable formarrow_forward
- Figure 6-33 (Subunit interactions in an allosteric enzyme, and interactions with inhibitors and activators) depicts allosteric modulation of an enzyme through non-covalent interactions. What features of an activator might lead to different levels of enzyme regulation? Select one or more: a. ability to cause a conformational change that results in an altered activity. b. affinity for the regulatory site c. boiling point d. bond flexibility (i.e. abundance of freely rotating single bonds instead of more rigid bonds like double bonds) e. molecular weightarrow_forward3) Read the situations below and indicate which of the four methods of enzyme regulation is occurring for each. a) The energy-carrying molecule ATP is made by the enzyme ATP synthase. Muscle cells use a lot of energy and also have higher amounts of the ATP synthase enzyme than many other cell types. General mechanism of enzyme regulation: S b) Prostaglandins are messenger molecules involved in the inflammatory response, as well as the perception of pain. They are synthesized from polyunsaturated fatty acid substrates by an enzym called cyclo-oxygenase. "Ibuprofen" is the active ingredient in a variety of anti-inflammatory medications such as Motrin® and Advil®. It reduces pain and swelling by binding to a hydrophobic channel in the active site of cyclo-oxygenase, blocking the polyunsaturated fatty acids from binding to the enzyme, and therefore stopping production of prostaglandins. General mechanism of enzyme regulation:arrow_forwardWhich of the following statements regarding protein phosphorylation is FALSE? Select one: A. Phosphorylation is catalyzed by enzymes called protein kinases. B. Phosphorylation inhibits the activity of enzymes C. Aspartate residues can be phosphorylated. D. Phosphorylation is a reversible covalent modification of enzymes. Which is usually the slowest way to regulate a reaction in a metabolic pathway? Select one: A. Allosteric modulation B. Covalent modification C. Changing the enzyme concentration D. All of the above are usually equally as fastarrow_forward
- A hypothetical three-step metabolic pathway consists of intermediates W, X, Y, and Z and enzymes A, B, and C. Deduce the order of the enzymatic steps in the pathway from the following information: 1. Compound Q, a metabolic inhibitor of enzyme B, causes Z to build up. 2. A mutant in enzyme C requires Y for growth. 3. An inhibitor of enzyme A causes W, Y, and Z to accumulate. 4. Compound P, a metabolic inhibitor of enzyme C, causes W and Z to build up.arrow_forwardDraw a mechanism using the general features of a serine protease to explain how inhibitor x might work using the following information: inhibitor x is a representative of a new family of serine protease inhibitors. treatment of chymotrypsin with inhibitor X rapidly decreased activity. to determine the mode of inhibition the researchers used dialysis to exchange the buffer with buffer lacking free inhibitor x. after dialysis, the enzyme did NOT recover any activity.arrow_forwardMany biosynthetic pathways are regulated by feedback control, where the product of a pathway turns off an enzyme that catalyzes an early step in the pathway. Usually, this control comes from an allosteric interaction. Of the types of reversible enzyme inhibition (Competitive inhibition, Noncompetitive inhibition, and Uncompetitive inhibition), what type is most likely to occur in a feedback control mechanism like this and why?arrow_forward
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