If you wanted to improve the catalytic efficiency of an enzyme, would youmutate amino acid residues to increase/decrease binding affinity for thesubstrate, or to increase/decrease the binding of the transition state?Explain.Mutate amino acids to increase binding to the transition state because itincreases the activation energy; mutations that bind substrate moretightly decrease the activation energy.Mutate amino acids to decrease binding to the transition state becauseit increases the activation energy; mutations that bind substrate moretightly decrease the activation energy.Mutate amino acids to increase binding to the transition state because itdecreases the activation energy; mutations that bind substrate moretightly increase the activation energy.Mutate amino acids to increase binding to the substrate bind because itdecreases the activation energy; mutations that bind the transition statemore tightly increase the activation energy.

In the transition state, a molecule is neither a substrate nor a product. This state exists at the…

Answered: If you wanted to improve the 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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When the final product of a series of enzymatically-catalyzed reactions binds to the first enzyme in the pathway to limit its production, it generally uses ___ because the structure of this final product is generally not similar to that of any of the enzyme's normal substrates. Zymogen activation Covalent modification Competitive inhibition Allosteric activation Allosteric inhibition
The active (catalytic) site of an enzyme contains the side chains of amino acid residues that areconserved because they participate in the protein’s catalytic activity. The bulk of the enzyme,however, is not part of the active site. A substantial amount of energy is required to synthesizeenzymes. Why are these molecules so large?
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 weight
The covalent catalytic mechanism of an enzyme depends on a single active site Cys whose pK is 8. A mutation in a nearby residue alters the micro environment so that this pK increases to 10. Would the mutation cause the reaction rate to increase or decrease? Explain.
Indicate whether each of the following statements about an enzyme active site is true or false. a. It is the location where substrate molecules are produced. b. It always has a fixed, rigid geometry. c. It always has a geometrical shape exactly complementary to that of substrate. d. It always accomodates several structurally related substrates. e. It is the location where substrate molecules are converted to product molecules. f. It always has a shape that has a degree of flexibility to it. g. it always accomodates only one specific substrate.
Many 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?
Substrates and reactive groups in an enzyme’s active site must be precisely aligned in order for a productive reaction to occur. Why, then, is some conformational flexibility also a requirement for catalysis?
In an enzyme's active site, a catalytic histidine residue abstracts a proton from the hydroxyl group of a catalytic serine residue. The catalytic serine then performs a nucleophilic attack on the carbonyl carbon of a peptide bond (on the substrate). The final products of this reaction are a cleaved substrate at the peptide bond, with a new amino group and carboxyl group, and regenerated catalytic residues. In this reaction, the serine residue is displaying what? A. Proximity and Orientation B. Covalent catalysis C. Metal ion catalysis D .A and B E. B and C F. None stated here
Enzyme cofactors are usually inorganic ions that enhanceenzymatic activity by improving the “fit” between an enzymeand its substrate. True or false?
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?
Select the false statements regarding the position of participating regions of an enzyme. Within the allosteric site of an enzyme, non-amino acid additions are in optimal positions to chemically react with reversible inhibitors. Within the allosteric site of an enzyme, amino acid side chains have the ability to bind and hold onto activators. Within the allosteric site of an enzyme, amino acid side chains are in optimal positions to chemically react with substrates. Within the active site of an enzyme, non-amino acid additions such as cations are in optimal positions to bind and hold onto substrates.
Select the false statements regarding the position of participating regions of an enzyme. Within the allosteric site of an enzyme, non-amino acid additions are in optimal positions to chemically react with reversible inhibitors. Within the allosteric site of an enzyme, amino acid side chains have the ability to bind and hold onto activators. Within the allosteric site of an enzyme, amino acid side chains are in optimal positions to chemically react with substrates. Within the active site of an enzyme, non-amino acid additions such as cations are in optimal positions to bind and hold onto substrates. Select the false statements from the following regarding the RNA hypothesis of chemical evolution. RNA are diverse molecules in the modern cells able to provide genetic instructions while catalyzing anabolic and catabolic reactions. RNA is not able to hydrogen bond to itself. DNA became a storage molecule after ancestral RNA…

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