**Question:**Why would it be difficult to evolve an enzyme with high catalytic activity but low specificity?**Options:**- ○ 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.- ○ Such an enzyme would need to be able to bind substrates without changing the conformation of the enzyme or the substrate.- ○ Such an enzyme would need to be able to bind substrates with substantial parts of the substrate not in close contact with the enzyme. Most 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 require 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

Under which of the following conditions could a biochemical reaction inside a cell have a positive enthalpy change and still occur spontaneously? (Recall that AG = AH – TAS) O When the reaction is in rapid equilibrium. O When there is a large increase in entropy. O When the AG is positive. O At an enzyme active site under Vmay conditions. O None of the above.
Draw each of the enzymatic step for each chemical conversion and write the enzyme together with the co-factor for the steps where a co-factor is involved. How many carbons are transferred in the conversion from step 1 into the intermediate from step 2? Step 1 OH ACP-s ? (multiple enzymatic steps) OH OH Step 2 ACP-S R1 5..
The above reaction coordinate diagram in the presence of enzyme is inconsistent with the "lock and key" model of enzyme-substrate l binding. Draw and properly label the reaction. coordinate diagram for the enzymatic reaction according to the "lock and key" model. Explain why this model is inconsistent with catalytic properties of enzymes.
How many of the following statements are true? Allosteric enzymes display sigmoidal kinetics for plots of V versus [S] Allosteric enzymes exist in T and R states Allosteric enzymes display kinetics that becomes less sigmoidal in the presence of activators
kcat is: a measure of the catalytic efficiency of the enzyme the rate constant for the reaction ES → E + P the rate constant for the reaction ES → E + S the [S] that half saturates the enzyme ½ Vmax
Hb serves as our model for regulation of enzyme reaction rates. But Hb is not an enzyme. Explain the reasoning of Jacque Monod and his colleagues for invoking Hb as a "model enzyme."
enzymes are naturally occurring catalysts responsible for various biochemical reactions. Give a modern and recent application of an enzyme used in a biochemical reaction a - the commercial or trade name of the catalyst and enzyme. b - the properties of the catalyst and enzyme (e.g., shape, size, colour, price). c - the advantages and the disadvantages of the chosen catalyst and enzyme d - catalytic reaction (e.g., the reactant, product, reaction equation, phase, selectivity, promoter, catalyst support, operating temperature & pressure).
When the product of reaction \\( A \\) becomes the reactant of reaction \\( B \\), the metabolic pathway is cyclic divergent bidirectional convergent linear
A dichotomous key works by determining positive and negative reactions to different biochemicals. Why does this method allow us to identify one species of organism from another? – for this question, do not describe the dichotomous key procedure, think about why it works, what are biochemical reactions based on? Think enzymatic pathways, what are enzymes, what are they a reflection of? Keep the answer between 2-3 sentences
Which of the following are true when enzymes and substrate interact? kı E + S ● ES- -P k-1 the rate of the formation of ES = k1 [ES] the rate of the formation of the product = k2[ES] k1 [ES] = k-1 [ES] the rate of breakdown of ES to reform the enzyme and substrate = K-1[E][S] the rate of formation of ES = k1[E][S]
Consider the following free energy diagram for an uncatalyzed and enzyme-catalyzed reaction. Select all the statements that are true. Without enzyme With enzyme A+B Time AB Oa. The reaction is now spontaneous due to the addition of enzyme b. The rate of the enzyme catalyzed reaction is faster than the uncatalyzed reaction O C. The reaction is exergonic O d. The change in free energy for the reaction is greater in the catalyzed reaction, compared to the uncatalyzed reaction e. The enzyme stabilizes the transition state for the reaction Released Energy pes
Although we have introduced catalytic strategies separately, an enzyme typically employs more than one during a reaction. The catalytic strategies employed by serine protease include: Select one or more: O a. reduction of ASt b. transition state stabilization Oc. metal-assisted catalysis O d. acid/base catalysis O e. covalent catalysis

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