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Concept explainers
(a)
Interpretation: The validation of the given pairing of the enzyme classification terminology has to be stated.
Concept introduction: There are six main classes of enzymes: oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases. The six main classes are then further divided into subclasses, like carboxylase, hydratase, lipase.
(b)
Interpretation: The validation of the given pairing of the enzyme classification terminology has to be stated.
Concept introduction: There are six main classes of enzymes: oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases. The six main classes are then further divided into subclasses, like carboxylase, hydratase, lipase.
(c)
Interpretation: The validation of the given pairing of the enzyme classification terminology has to be stated.
Concept introduction: There are six main classes of enzymes, oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases. The six main classes are then further divided into subclasses, like carboxylase, hydratase, lipase.
(d)
Interpretation: The validation of the given pairing of the enzyme classification terminology has to be stated.
Concept introduction: There are six main classes of enzymes, oxidoreductases, transferases, hydrolases, lyases, isomerases, ligases. The six main classes are then further divided into subclasses, like carboxylase, hydratase, lipase.
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Chapter 21 Solutions
EBK GENERAL, ORGANIC, AND BIOLOGICAL CH
- A multi-enzyme complex Is made up of three polypeptide chains, A, B and C. A is associated with decarboxylase activity; B is a transacetylase, while C is a dehydrogenase. When the protein was placed in a nonpolar solvent, then run in PAGE, two protein bands were observed. Enzyme assays showed that one protein band exhibited decarboxylase activity while the other has both transacetylase and dehydrogenase activities. When the protein was also placed in an aqueous solvent at pH 5.0, then run in electrophoresis, two protein bands were also detected. Further enzyme assays also showed that one protein band exhibits transacetytase activity while the other has both decarboxylase and dehydrogenase activities. a. What types of non-covalent interactions are possible between A, B and C? b. Addition of urea, a reducing agent gave 4 bands in the PAGE profile with a subsequent loss of decarboxylase activity. What could be the reason for the observed result? Explain briefly in terms of the structure…arrow_forwardSucrase has an optimum temperature of 37°C and an optimum pH of 6.2. Determine the effect of the following on its rate of reaction: 1) no change 2) increase decrease 3) A. increasing the concentration of sucrase B. changing the pH to 4.0 C. running the reaction at 70°C What are the functions of Allosteric enzymes What are some factors that affects enzyme activity? I. II. III. IV. V. VI. Enzyme activity can be regulated by allosteric enzymes, feedback control, and covalent modifications. T/F Examples of Zymogens are the proteases trypsinogen and chymotrypsinogen. T/F? Trypsin catalyzes the removal of dipeptides from inactive chymotrypsinogen and trypsinogen to give the active proteases chymotrypsin and trypsin. T/F The removal of a polypeptide chain from proinsulin produces the active form of insulin. T/F? A kinase can activate an inactive enzyme by phosphorylation, ie adding a phosphate group. T/F? A phosphatase can activate an inactive enzyme by removal of phosphate. T/F? Identify…arrow_forwardHow to differentiate the following simply by seeing the reaction: a. oxidoreductase b. transferase c. hydrolase d. lyase e. isomerase f. ligasearrow_forward
- Define the following terms:a. oxidoreductaseb. lyasec. ligased. transferasee. hydrolasef. isomerasearrow_forwardDefine the following as they apply to an enzymatic reaction. Give an example of each. a. Enzyme-limited: b. Substrate-limited:arrow_forwardGive a complete and well descriptive definition of the following:1.1 Enzyme catalysis1.2 Co-enzyme1.3 Negative heterotropic co-cooperativitarrow_forward
- When studying the mechanism of the enzymatic reaction, functional groups were found that ensure the connection of the enzyme molecule with the substrate and take a direct part in the act of catalysis. What are these areas of the enzyme formed by these groups called? What functional structures form them and why?arrow_forwardList three effects of macromolecular crowding on the properties of enzymes and the reactions they catalyze.arrow_forwardName three weak forces by which the substrates bind in the active site of an enzyme.arrow_forward
- Match each reaction description to the type of enzyme that catalyzes the reaction. 1. Oxidation and reduction of compounds 2. Transfers a functional group from one compound to another compound 3. Utilizes water to break bonds within a compound 4. Addition/removal of a group of atoms and bonds within a compound 5. Forms a bond between two compounds A. Ligase B. Transferase C. Hydrolase D. Oxidoreductase E. Isomerase F. Lyasearrow_forwardIn the Enzyme Commission database system, an enzyme with the designation 4.3.2.1 would catalyze which reaction below? Select one: O a. The conversion of an alcohol to an aldehyde O b. The conversion of an alcohol to a phosphate O c. The conversion of an alcohol to an ether o d. The conversion of an alcohol to an alkene A buffer molecule is protonated at pH 9. Adding this buffer to a reaction greatly increases the rate of reaction at pH 9.0. What is true about the reaction? Select one: O a. The buffer is a specific base Ob. It is catalyzed by acid OC. It is catalyzed by base o d. The buffer is a specific acidarrow_forwardHow is it possible to determine the structure of an enzyme substrate complex by x ray crystallography when the reaction is over so quickly and the x ray analysis takes at least several minutes?arrow_forward
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