During chymotrypsin-mediated catalysis, which of the following statements is true? Select any/all answers that apply. A. A basic (positively-charged) side chain of the substrate polypeptide sits within the oxyanion hole of the enzyme. B. A basic (positively-charged) side chain of the substrate polypeptide sits within the specificity pocket of the enzyme. C. Ser195 hydrogen-bonds with the backbone carbonyl group of the substrate polypeptide within the oxyanion hole of the enzyme. D. All three residues that comprise the catalytic triad of the enzyme interact directly with the substrate polypeptide chain. E. Both covalent catalysis and acid-base catalysis occur.

During chymotrypsin-mediated catalysis, which of the following statements is true? Select any/all answers that apply. A. A basic (positively-charged) side chain of the substrate polypeptide sits within the oxyanion hole of the enzyme. B. A basic (positively-charged) side chain of the substrate polypeptide sits within the specificity pocket of the enzyme. C. Ser195 hydrogen-bonds with the backbone carbonyl group of the substrate polypeptide within the oxyanion hole of the enzyme. D. All three residues that comprise the catalytic triad of the enzyme interact directly with the substrate polypeptide chain. E. Both covalent catalysis and acid-base catalysis occur.

Biochemistry

6th Edition

ISBN:9781305577206

Author:Reginald H. Garrett, Charles M. Grisham

Publisher:Reginald H. Garrett, Charles M. Grisham

Chapter23: Fatty Acid Catabolism

Section: Chapter Questions

Problem 21P: Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved...

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Which of the following is true under the following conditions: an enzyme displaying Michaelis-Menten kinetics where the enzyme concentration is 10 nM, the substrate concentration is 45 mM, and the Km is 50 µM? a) The enzyme has low catalytic efficiency for the substrate. b)The rate of catalysis is near half-maximal velocity. c)The enzymatic reaction is near maximal velocity. d)Halving the substrate concentration has little effect on the catalytic rate. e) There is not enough information provided.
When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 450C lost 50% of its activity in 12 minutes, but when incubated at 450C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates
When enzyme solutions are heated, there is a progressive loss of catalytic activity over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 °C lost 50% of its activity in 12 min, but when incubated at 45 °C in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 min. Suggest why thermal denaturation of hexokinase was retarded in the presence of one of its substrates.
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 β 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 three- dimensional structure of macromolecules.
The active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?
The following questions deal with a fundamental understanding of enzyme catalysis.a. Why is the rate of an enzyme-catalyzed reaction proportional to the amount of (ES) complex?b. What do you think is meant by saturation of the enzyme?c. What do you think is meant by the term “saturation kinetics”?d. How does the Michaelis-Menten equation explain why the rate of an enzyme-catalyzed reaction reachesa maximum value at high [S]?
Graphically explain the term saturation of the enzyme? Why is the rate of an enzymecatalyzed reaction proportional to the amount of E.S complex?
Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate  delta delta G〒 on your sketch: Chemical step is rate limiting
Explain why the very tight binding of a substrate to an enzyme is not desirable for enzyme catalysis, whereas tight binding of the transition state is desirable.
Which of the following best explains why enzyme catalysis is affected by a change in pH? A. Change in pH alters ionization states of serine in the active site involved in nucleophilic catalysis B. The ionization states of his, asp and glu involved in acid/base catalysis are altered with change in pH C. Change in pH alters ionization states of contact amino acids in the active site D. All enzymes have optimum pH
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?
Shown below is a proposed mechanism for the cleavage of sialic acid by the viral enzyme neuraminidase. The kcat for the wild-type enzyme at pH =6.15, 37 °C is 26.8 s-1.(a) Describe the roles of the following amino acids in the catalytic mechanism: Glu117, Tyr409, and Asp149. List all of the following that apply:general acid/base catalysis (GABC), covalent catalysis, electrostaticstabilization of transition state.(b) Based on the information shown in the scheme, would you expect mutation of Glu 117 to Ala to have a greater effect on KM or kcat?(c) For the R374N mutant at pH = 6.15, 37 °C, kcat is 0.020 s-1, and KMis relatively unaffected. Based on this result, it seems that R374 is morecritical for catalysis than for substrate binding. Explain how R374 stabilizesthe reaction transition state more than the substrate (i.e., what feature of this reaction would explain tighter binding to the transition state vs. substrate?).

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	A.	A basic (positively-charged) side chain of the substrate polypeptide sits within the oxyanion hole of the enzyme.
	B.	A basic (positively-charged) side chain of the substrate polypeptide sits within the specificity pocket of the enzyme.
	C.	Ser¹⁹⁵ hydrogen-bonds with the backbone carbonyl group of the substrate polypeptide within the oxyanion hole of the enzyme.
	D.	All three residues that comprise the catalytic triad of the enzyme interact directly with the substrate polypeptide chain.
	E.	Both covalent catalysis and acid-base catalysis occur.