Biochemistry (Looseleaf)
9th Edition
ISBN: 9781319114800
Author: BERG
Publisher: MAC HIGHER
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Question
Chapter 9, Problem 18P
Interpretation Introduction
Interpretation:
The advantage of the specificity of the enzymes from a biological and chemical perspective should be determined. Also, the difficulty to evolve an enzyme with high catalytic activity but low specificity should be determined.
Concept introduction:
Enzymes are biological catalysts that accelerate the
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Students have asked these similar questions
On the figure below are shown three Lineweaver-Burk plots for enzyme
reactions that have been carried out in the presence, or absence, of an inhibi-
tor. Indicate what type of inhibition is predicted based on each Lineweaver-
Burk plot. For each plot indicate which line corresponds to the reaction
without inhibitor and which line corresponds to the reaction with inhibitor
present.
1
1
1
[S]
[S]
[S]
In any given enzyme, the active site is only a small portionof the entire molecule. Synthesis of such a relatively largemolecular machine requires an enormous amount of cellular energy. Explain why this inefficiency is tolerated.
A multi-enzyme complex Is made up of three polypeptide chains, A, B and C. A is
associated with decarboxylase activity; B is a transacetylase, while C is a
dehydrogenase. When the protein was placed in a nonpolar solvent, then run in
PAGE, two protein bands were observed. Enzyme assays showed that one
protein band exhibited decarboxylase activity while the other has both
transacetylase and dehydrogenase activities. When the protein was also placed
in an aqueous solvent at pH 5.0, then run in electrophoresis, two protein bands
were also detected. Further enzyme assays also showed that one protein band
exhibits transacetytase activity while the other has both decarboxylase and
dehydrogenase activities.
a. What types of non-covalent interactions are possible between A, B and C?
b. Addition of urea, a reducing agent gave 4 bands in the PAGE profile with a
subsequent loss of decarboxylase activity. What could be the reason for the
observed result? Explain briefly in terms of the structure…
Chapter 9 Solutions
Biochemistry (Looseleaf)
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Similar questions
- The following reaction coordinate diagram charts the energy of a substrate molecule (S) as it passes through a transition state (X‡) on its way to becoming a stable product (P) alone or in the presence of one of two different enzymes (E1 and E2). How does the addition of either enzyme affect the change in Gibbs free energy (ΔG) for the reaction? Which of the two enzymes binds with greater affinity to the substrate? Which enzyme better stabilizes the transition state? Which enzyme functions as a better catalyst?arrow_forwardGraphically explain the term saturation of the enzyme? Why is the rate of an enzymecatalyzed reaction proportional to the amount of E.S complex?arrow_forwardThe 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.arrow_forward
- Describe the two models that explain the behavior of allosteric enzymes. Include thelimitation or advantage of each. Give also an example of each.arrow_forwardWould 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.arrow_forwardTwo experiments were performed with the enzymeribonuclease. In experiment 1 the effect of increasingsubstrate concentration on reaction velocity was measured.In experiment 2 the reaction mixtures were identical tothose in experiment 1 except that 0.1 mg of an unknowncompound was added to each tube. Plot the data accordingto the Lineweaver-Burk method. Determine the effect of theunknown compound on the enzyme’s activity. (Substrateconcentration is measured in millimoles per liter. Velocity ismeasured in the change in optical density per hour.)arrow_forward
- Consider the hypothetical biochemical pathway shown below. Assume that each letter (A, B, C, etc) represents a molecule and each number (1, 2, 3, etc) represents an enzyme. Draw arrows indicating all the probable feedback inhibition interactions that would be expected to regulate the activity of enzymes in this pathway.arrow_forwardMost enzymes are quite specific, catalyzing a particular reaction on a set of substrates that are structurally quite similar to one another. Why are highly specific enzymes advantageous from a biological perspective? They allow catalyzed reactions to produce potentially useful by-products. They allow for the sharing of enzymes by multiple metabolic pathways. They allow an inhibitor to simultaneously inhibit multiple steps in a metabolic pathway. They allow control of which reactions occur at appreciable rates. Why are most enzymes highly specific from a chemical perspective? Enzymes generally requires a tight fit between enzyme and substrate. Interactions between the enzyme and the substrate stabilize the substrate. The active sites of enzymes are always identical in shape to the substrates they bind. The formation of weak interactions between the enzyme and the substrate requires energy.arrow_forwardDiscuss in a short paragraph (3–5 sentences for each mutation) whether or not the enzyme is likely to completely lose catalytic activity if the following mutations are carried out. You may assume that steric effects do not distort the active site so much that catalysis cannot take place; focus your analysis on discussing the chemistry the amino acid side chains are able to perform and the properties that enable them to do so. Mutation 1: H to E Mutation 2: H to N Mutation 3: S to D Mutation 4: S to Carrow_forward
- Enzymes are stereochemically specific; that is, they oftenconvert only one stereoisomeric form of substrate intoproduct. Why is such specificity inherent in theirstructure?arrow_forwardRuBP carboxylase is not an idel enzyme by any means. Describe some of the active site's and substrate specificity's issues. When the amino acid sequences of this enzyme from several species are compared, they are nearly similar. What importance does this homogeneity have?arrow_forwardThe milieu wherein enzymes occur in vivo is dramatically different from in vitro experiments, which is often used to investigate enzyme. Give an overview of this as well as the nature of enzyme reactions in vivo. Name, in addition, the factors affecting the concentration of enzymes in vivo.arrow_forward
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