Although we have introduced catalytic strategies separately, an enzyme typicallyemploys more than one during a reaction. The catalytic strategies employed byserine protease include:Select one or more:O a. reduction of AStb. transition state stabilizationOc.metal-assisted catalysisO d. acid/base catalysisO e. covalent catalysis

Serine proteases are enzymes that have a serine residue in their active site which plays a vital…

Answered: Although we have introduced catalytic…

Biochemistry

9th Edition

ISBN:9781319114671

Author:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Publisher:Lubert Stryer, Jeremy M. Berg, John L. Tymoczko, Gregory J. Gatto Jr.

Chapter1: Biochemistry: An Evolving Science

Section: Chapter Questions

Problem 1P

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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
Which one of the following statements is true of enzyme catalysts? a. Their catalytic activity is independent of pH. b. They are generally equally active on D and L isomers of a given substrate. c. They can increase the equilibrium constant for a given reaction by a thousand fold or more. d. They can increase the reaction rate for a given reaction by a thousand fold or more. e. To be effective, they must be present at the same concentration as their substrate.
Which of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that apply
Which of the following is TRUE concerning the induced fit model of enzyme catalysis? * (One correct answer only) A. The active site can be influenced by molecules binding elsewhere on an enzyme B. The initial binding of enzyme and substrate is the most tightly bound conformation C. The induced fit must occur prior to the initial binding of enzyme and substrate in order for the reaction to proceed D. The binding of enzyme and substrate is weakest in the transition state
Would you expect an “enzyme” designed to bind to its target substrate astightly as it binds the reaction transition state to show a rate enhancementover the uncatalyzed reaction? In other words, would such a protein actuallybe a catalyst? Explain why or why not.
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.
in cells, an enzyme catalyzes the reaction ab → a + b. it was isolated, however, as an enzyme that carries out the opposite reaction a + b → ab. explain the paradox.
Which of the following would best explain how an enzyme catalyzes two different reactions? A) The enzyme contains a-helices and B-pleated sheets. B) The enzyme is subject to cooperativity C) Either the enzyme has two distinct active sites or the substrates involved in the two reactions have very similar structures D) The enzyme is subject to competitive inhibition and allosteric regulation E) The enzyme is composed of at least two subunits
An enzyme catalyzes a reaction in which substrateA is cleaved into two products, P and Q. In the catalytic mechanism, the enzyme converts A to a covalently-bound reaction intermediate X and product P, P then desorbs from the enzyme, and in a second chemical step, the enzyme converts the intermediate X in the EX complex to the final product Q (in EQ), which then desorbs from the enzyme E.You discover two inhibitors of this enzyme, I and J. I is a competitive inhibitor of the substrate A, and has nearly double the molecular weight of J. On the other hand, J is a mixed inhibitor of enzyme E, and its inhibitory effect on Km/ Vmax (the slope effect from the double reciprocal plot) is greater than that of 1 / Vmax (the intercept effect in a double reciprocal plot). That is Kis< Kii . At low pH, the conversion of EX to EQ is greatly slowed, kcat is decreased, and the intercept effect of inhibitor J is elevated, that is, the value of Kiiis diminished. When a high, fixed concentration of…
An enzyme catalyzes a reaction in which substrate A is cleaved into two products, P and Q. In the catalytic mechanism, the enzyme converts A to an covalently-bound reaction intermediate X and product P, P then desorbs from the enzyme, and in a second chemical step, the enzyme converts the intermediate X in the EX complex to the final product Q (in EQ), which then desorbs from the enzyme E. You discover two inhibitors of this enzyme, I and J. I is a competitive inhibitor of the substrate A, and has nearly double the molecular weight of J. On the other hand, J is a mixed inhibitor of enzyme E, and its inhibitory effect on Km / Vmax (the slope effect from the double reciprocal plot) is greater than that of 1 / Vmax (the intercept effect in a double reciprocal plot). That is Kis < Kii . At low pH, the conversion of EX to EQ is greatly slowed, kcat is decreased, and the intercept effect of inhibitor J is elevated, that is, the value of Kii is diminished. When a high, fixed concentration…
the type of enzyme inhibition in which covalent bulky adduct prevents catalysis is ? a) uncompetitive b) reversible c) noncompetitive d) competitive e) Irreversible
A mixed inhibitor of an enzyme (sometimes called a mixed non-competitive inhibitor) can decrease the rate of a reaction by any of the following EXCEPT by: a) binding to a site other than the active site of the enzyme. b) binding to the active site of the enzyme, preventing substrate binding. c) decreasing kcat. d) Increasing KM.

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