Which of the following statements are correct? Explain your answers. A. The active site of an enzyme usually occupies only a small fraction of the enzyme surface. B. Catalysis by some enzymes involves the formation of a covalent bond between an amino acid side chain and a substrate molecule. C. $A \beta$ sheet can contain up to five strands, but no more. D. The specificity of an antibody molecule is contained exclusively in loops on the surface of the folded light-chain domain. E. The possible linear arrangements of amino acids are so vast that new proteins almost never evolve by alteration of old ones. F. Allosteric enzymes have two or more binding sites. G. Noncovalent bonds are too weak to influence the threedimensional structure of macromolecules. H. Affinity chromatography separates molecules according to their intrinsic charge. I. Upon centrifugation of a cell homogenate, smaller organelles experience less friction and thereby sediment faster than larger ones.
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The active site of an enzyme usually occupies only a small fraction of the enzyme surface. This statement is correct. The active site is a small region on the enzyme where the substrate binds and the catalytic reaction occurs. The rest of the enzyme surface is Show more…
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Which of the following statements is not true about substrates? - Substrates are molecules that bind to the active site of an enzyme and are chemically changed as a result of that binding. - The active site of each enzyme is specific for specific substrates. - The substrate often fits into a pocket or a groove on the enzyme. - Often the name of the substrate shows up in the name of the enzyme; for instance, catechol is the substrate for catechol oxidase. - A cofactor can be considered a substrate because it also binds to an enzyme. Which of the following statements are true about binding sites on enzymes? (Mark all correct responses) - An active site is the location on an enzyme to which a specific substrate binds. - On many enzymes, there are binding sites away from the active site to which molecules can bind and alter the activity of the enzyme. - The rate at which molecules bind to enzymes is influenced by the concentration of that particular molecule. - The shape of the active site (and therefore the rate of binding of the substrate to the active site) can be changed by changing the shape of the enzyme. - Molecules with similar shape will compete for binding sites on the enzyme.
Md.Daniyal A.
Which of the following statements concerning enzyme-catalyzed reactions is NOT correct? (a) Enzymes increase the reaction rate by lowering the activation energy (b) Enzymes increase the reaction rate by stabilizing the transient state of reactants (c) Enzymes increases the reaction rate by increasing the equilibrium constant (d) Enzyme activity may be affected by changes in pH (e) None of the above 4. A competitive inhibitor of an enzyme has all of the following properties EXCEPT; (a) Has a structure similar to the substrate (b) May have a higher affinity to the enzyme than the substrate (c) Binds to the active site of the enzyme (d) Increases the Km value (e) None of the above
Sri K.
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