Why would it be difficult to evolve an enzyme with high catalytic activity but low specificity?Such an enzyme would need to be able to generate a single product from several different substrates.Such an enzyme would need to be able to catalyze several types of reactions, depending on which substrate it binds.O Such an enzyme would need to be able to bind substrates without changing the conformation of the enzyme orthe substrate.Such an enzyme would need to be able to bind substrates with substantial parts of the substrate not in close contactwith the enzyme. Most enzymes are quite specific, catalyzing a particular reaction on a set of substrates that are structurally quite similar toone 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.

Specificity is a property of an enzyme which estimates the number of different chemical species…

Answered: Most enzymes are quite specific,…

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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Similar questions

Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are true
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?
As biological catalysts, enzymes play a fundamental role in many cellular processes. Which of the following statements about enzymes is correct? 1. Enzymes are essential for anabolic pathways; they are not required for catabolic pathways. 2. While an increase in temperature can increase the rate of an uncatalyzed reaction, it can’t increase the rate of an enzyme-catalyzed reaction. 3. Enzymes force substrates into unique conformations that do not occur in the absence of an enzyme. 4. Enzymes decrease the free energy of a reaction’s transition state. A. 1, 2 and 3 B. 1 and 3 C. 2 and 4 D. 4 only E. All of 1, 2, 3 and 4 are correct
Two substrates (A and B) are used to produce a certain biological product in an enzyme- catalyzed reaction. It is found that both substrates must bind to the enzyme, first Substrate A, then Substrate B before the product is produced. What kind of kinetic mechanism is described? Linear Reaction Ordered Sequential Reaction Random Sequential Reaction Ping Pong Reaction
Indicate whether each of the following statements about an enzyme active site is true or false. It is the location where substrate molecules are produced. It always has a fixed, rigid geometry. It always has a geometrical shape exactly complementary to that of substrate. It always accommodates several structurally related substrates. It is the location where substrate molecules are converted to product molecules. It always has a shape that has a degree of flexibility to it. It always accommodates only one specific substrate.
Many pharmaceuticals exert their action by inhibiting the activity of enzymes. Choose the false statement regarding enzyme inhibition. A- Enzyme can be inhibited by a ligand that binds to an active site B- Enzyme can be inhibited by a ligand that binds to a site other than that of substrate C- Enzyme can be inhibited by a ligand that forms a covalent bond with enzyme. D- It is true of all enzyme inhibitors, that the degree of inhibition is reduced when the concentration of inhibitor is lowered by metabolism or E- Enzyme may be inhibited by a ligand that does not bind in the substrate site
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?
Which of the following aspects of catalysis by enzymes can NOT be explained by the Fischer Lock and Key Hypothesis? Enzymes will lower the activation energy barrier for reaction. Enzymes will specifically recognize their substrates. Appropriate substrates will bind to the enzyme to form a Michaelis complex. Enzymes have an "active site" where appropriate substrates will be bound. Two of the above cannot be explained by the Fischer "Lock and Key" Hypothesis.
When lead acts as a poison, it can do so either by replacing another ion (such as zinc) in the active site of an enzyme or by reacting with cysteine side chains to form covalent bonds. Which of these is irreversible and why? Match the items in the left column to the appropriate blanks in the sentences on the right. Reset Help a covalent bond When occurs between the active site (containing cystein) and the inhibitor (lead), replacement of an ion the substrate is excluded or the catalytic reaction is blocked. an ionic bond When occurs and the inhibitor (lead) replaces another ion. reaction with side chains The is an example of a permanent, irreversible change. ion exchange The is an example of a change that can be reversed.
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?
hich of the following are advantages of quaternary structure? Choose all correct nswers 1) The genes may be for single subunits, rather than requirement for transcription and translation of giant sequences 2) Subunit construction may provide the structural basis for protein regulation 3) Multi-subunit proteins are more water soluble than single subunit proteins of the same size 4) Defects in protein synthesis may be fixed at the subunit level, rather than giant polypeptide level 5) May have multiple active sites - one on each subunit
Examine the figure below, which compares the energetics of a catalyzed and uncatalyzed reaction during the progress of the reaction from substrate (S) to product (P). The highest peak in such a diagram corresponds to the transition state, which is an unstable, high-energy arrangement of substrate atoms that is intermediate between substrate and product. The free energy required to surmount this barrier to the reaction is termed the activation energy. Enzymes function by lowering the activation energy, thereby allowing a more rapid approach to equilibrium. UNCATALYZED activation energy progress of reaction CATALYZED activation energy S ES | progress of reaction free energy free energy

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