A plot of the velocity v, or rate, of an concentration [S] that is sigmoid or Sened instead of hyperbolic is characteristic of: enzymatic reaction vs. the substrate a) b) c) allosteric enzymes modulator proteins isozymes proenzymes zymogens
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![A plot of the velocity v, or rate, of an enzymatic reaction vs. the substrate
concentration [S] that is sigmoid or S abaned instead of hyperbolic is characteristic of:
a)
b)
allosteric enzymes
modulator proteins
isozymes
proenzymes
zymogens](/v2/_next/image?url=https%3A%2F%2Fcontent.bartleby.com%2Fqna-images%2Fquestion%2Fb0016275-e9a1-4972-a183-517fe36ccc93%2F365fb933-1ea2-402a-8402-4f82c10771b6%2F8vewrip_processed.jpeg&w=3840&q=75)
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- Using the ActiveModel for enoyl-CoA dehydratase, give an example of a case in which conserved residues in slightly different positions can change the catalytic rate of reaction.Why Do Anabolic and Catabolic Pathways Differ? Why is the pathway for the biosynthesis of a biomolecule at least partially different from the pathway for its catabolism? Why is the pathway for the biosynthesis of a biomolecule inherently more complex than the pathway for its degradation?Using lysozyme as an example, what can an enzyme’s structure reveal about its catalytic mechanism?
- 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?In Bacillus subtilis, threonine is metabolized by the following sequence of reactions: (a) oxidation; (b) decarboxylation;(c) transamination; and (d) oxidation to produce pyruvate. Outline this sequence of steps, show the structures of thesubstances, use abbreviations for the cofactors, and show any enzyme-bound coenzymes. What type of enzyme bound intermediate is likely for reaction (d)?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
- What does the term “oxidative phosphorylation” mean? What is substrate-level phosphorylation? Are these processes the same? Explain.Concerning enzymatic reactions, how different are the graphic curve of the variation of the speed of a reaction as function of substrate concentration and the curve of variation of the speed of a reaction as function of temperature?For a lot of enzymes that work on fatty acids, the rate determining step is the release of the product from the active site. This means that the activation energy for product release is much higher than the free energy of catalysis. What enthalpic or entropic contributions would make the activation energy for product release so high and explain?
- Several names are compatible with standard nomenclature for the enzyme that catalyzes the reaction shown in the figure. However, the assigned name is based specifically based on its substrate and its coenzyme. What is that name?A simple enzymatic reaction proceeds as follows. E+S↔E.S→ E+P Derive the Michaelis–Menten equation for this reaction.What is the significance of the ΔG°’ value of each step of Glycolysis? Why do some values classify reactions as irreversible and others as easily reversible?