**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

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..
What statement about states of the allosteric enzyme is TRUE? The value of KM for the T state is lower than for the R state. O The value of Vmax for the T state is lower than for the R state. O The value of KM for the T state and the R state is the same. The value of Vmax for the T state is higher than for the R state. O The value of KM for the T state is higher than for the R state.
The effect of on the activity of an enzyme can usually be overcome by increasing the concentration of substrate(s). Choose the best answer the phosphorylation of the R groups of serine (S), threonine (T) and tyrosine (Y) an allosteric effector a noncompetitive inhibitor a competitive inhibitor
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."
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
For each of the statements below about the dUTPase enzyme, mark whether it is true or false. If it is false, change the language to make the statement true. _______If the dUTPase enzyme is the rate determining step in a larger metabolic pathway, the reaction likely lies near to equilibrium and is irreversible. _______For the dUTPase reaction, it is not likely that DG’ = DG°’ _______ dUTPase has a higher affinity for its substrate than for its product, but both of these are higher than the affinity for the transition state _______Kinetic analysis of dUTPase using Michaelis-Menten methods assumes that the formation of the E*S complex has a large negative value for DG
Number 4 please
which of the following describes an enzyme ALLOSTERIC site?
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
Why can’t enzyme kinetics prove that a particular enzyme mechanism is correct?

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