In most enzymes, the required active site amino acids consists of only a fewresidues. Why is the rest of the protein necessary for full enzyme function?To bind to the membrane through hydrophobic residues.To interact with other proteins so that the enzyme can be imported intothe endoplasmic reticulum where enzymes are the most active.To provide the correct tertiary structure for the substrate binding siteand for proper orientation of the catalytic residues.To provide protein targeting sequences so that the enzyme can betransported to the mitochondrial matrix where gluconeogenesis takesplace.

Enzymes are proteins that function as biocatalysts and catalyse biochemical reactions.They have a…

Answered: In most enzymes, the required active…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter4: Cells

Section: Chapter Questions

Problem 1ITD

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The active site of an enzyme contains sequences that are conserved because they participate in the protein’s catalytic activity. The bulk of an enzyme, however, is not part of theactive site. Because a substantial amount of energy is required to assemble enzymes, why are they usually so large?
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?
Although all of these play a part, the most important factor which drives protein folding is: a) hydrogen bond formation b) salt bridge formation c) ion-dipole interactions d) the hydrophobic effect The active site of an enzyme binds which type of molecule? a) allosteric activator b) coenzyme c) substrate d) product A coenzyme is also considered to be a prosthetic group if it: a) assists in enzyme catalysis b) binds to the active site c) acts as an allosteric inhibitor d) is covalently bound to the enzyme Proteases catalyze the cleavage of proteins into smaller peptides and amino acids by reaction with water. Proteases fall into the broader class of: a) transferases b) lyases c) hydrolases d) oxidoreductases 13. The Michaelis - Menten constant Km represents: a) 1/2 Vmax b) the substrate concentration at 1/2 Vmax c) 1/2 the substrate concentration at Vmax d) the minimum amount of substrate needed to initiate the reaction Enzymes alter which of these…
Genetic engineering of enzymes to be utilized for bioremediation efforts results in which of the following changes? (you may select more than one) Decrease in the concentration required to reach one half maximal velocity. Increase in hydrogen bonding between substrate and enzyme. Primary sequence alterations resulting in 3D structural changes in the substrate binding site. Decrease in the maximum activity the enzyme can achieve in ideal conditions.
A prokaryotic species is facing a new environmental stressthat can be ameliorated by a catalytic activity that requiresthe side chain of a unique amino acid derivative called pyrovaline. How would such an organism develop a mechanism for the incorporation of this nonstandard amino acidinto an enzyme molecule? What would be the properties ofthe molecules required to solve this problem?
You discover a protein that displays improved catalytic efficiency. Would you predict that this protein has a mutation in residues important for increasing the binding affinity for its substrate or a mutation that increases the binding of its transition state? Explain.
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…
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.
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
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.
Enzymes are influenced by physical and chemical conditions affecting kinetic characteristics. Rubisco function is no different, and changes in temperature have profound influences on its activity based on changes in __Blank A___ and __Blank B___ Options for Blank A: - Vmax - Kineton Ratio - denaturization - H-bond linkage - Substrate availability Options for Blank B: - susceptibility to feed-forward interactions - cellular localization - mechanism of regulation - membrane binding characteristics - kinetics of catalytic function

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