Fill the blank with the option belowThe substrate concentration at which an enzyme-catalyzed reaction proceeds at on-half its maximum velocityThe rate enhancement of the enzyme catalyzed reaction over uncatalyzed reactionThe rate of the reaction when the concentration of the products is zero and the reverse rate is negligibleThe rate at which the enzyme-substrate complex is formedThe number of time an enzyme molecule transforms a substrate molecule per unit of timeThe proportionality constant that relates the velocity of a chemical reaction to the concentrations of the reactantsThe maximum velocity of an enzymatic reaction when the binding site is saturate with substrateA measure of the catalytic activity of an enzyme at low concentrations of substrateThe rate constant for the equilibrium between the reactants and the enzyme-substrate complex1. Vo2.4.3. V₁Acronym Parameter6.7.I5. Km8.1I9. AAG10. AGrate constantrate ofdisappearanceIspecificityconstantmaximalvelocityturnovernumberIDefinition[Select][Select][Select][Select][Select][Select][Select][Select][Select][Select]>>>>

The substrate concentration at which an enzyme catalysed reaction proceeds at half maximum velocity…

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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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Sketch the complete reaction free energy diagram for an enzyme-catalyzed conversion of a single substrate (S) into product (P), where the reaction is spontaneous in the forward direction Overlay the free energy diagram for the uncatalyzed reaction and indicate  delta delta G〒 on your sketch: Chemical step is rate limiting
Select the graph that correctly illustrates the effect of a positive modifier (effector) on the velocity curve of an allosteric enzyme. Place the correct graph in the set of axes. The solid blue curve represents the unmodified enzyme. The dashed green curve represents the enzyme in the presence of the effector. R is the highly active form of the enzyme and T is the less active form of the enzyme. Assume that this is a positively cooperative enzyme, meaning that the affinity for substrate increases with increasing substrate concentration.
The concept of “induced fit” refers to the fact that: a. enzyme specificity is induced by enzyme-substrate binding. b. enzyme-substrate binding induces an increase in the reaction entropy, thereby catalyzing the reaction. c. enzyme-substrate binding induces movement along the reaction coordinate to the transition state. d. substrate binding may induce a conformational change in the enzyme, which then brings catalytic groups into proper orientation. e. when a substrate binds to an enzyme, the enzyme induces a loss of water (desolvation) from the substrate.
When enzyme solutions are heated, there is a progessive loss of catalytic activty over time due to denaturation of the enzyme. A solution of the enzyme hexokinase incubated at 45 degrees Celsius lost 50% of its activity in 12 minutes, but when incubated at 45 degrees Celsius in the presence of a very large concentration of one of its substrates, it lost only 3% of its activity in 12 minutes. Suggest why thermal denaturation of hexokinase was retarded in the presence of one substrates.
Which of the following statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.
Which statements are false? Initial velocities of enzyme reactions are best obtained in the absence of product because it simplifies analysis. Initial velocities refer to the velocity of the reaction right after it is initiated. The velocity of the reaction as a function of measuring time are curved just like an isothermal binding curve because of substrate binding to the enzyme. Initial velocities correspond to the pre-steady state condition for free enzyme. Initial velocities can sometimes be measured by spectroscopy such as UV/Vis spectroscopy when monitoring the production of NADH from NAD+. The velocity of the reaction will eventually go to zero. The reaction will reach equilibrium because of the presence of the enzyme. It is always better to use substrate rather than product to measure enzyme kinetics.
Select the correct option a.A holoenzyme is a catalytically inactive enzyme in the absence of its cofactor b.An enzyme cofactor is the amino acid side group in the enzyme active site c.Each of the option listed here is true d.An apoenzymes is catalytically active RNA molecule e.A co-substrate is a detachable enzyme cofactor required with another substrate for an enzyme reaction
Which of the following statements are correct? explain your answers.a. The active site of an enzyme usually occupies only a small fraction of the enzyme surface.B. catalysis by some enzymes involves the formation of a covalent bond between an amino acid side chain and a substrate molecule.c. a β sheet can contain up to five strands, but no more.d. The specificity of an antibody molecule is contained exclusively in loops on the surface of the folded light-chain domain.e. The possible linear arrangements of amino acids are so vast that new proteins almost never evolve by alteration of old ones. f. allosteric enzymes have two or more binding sites. G. noncovalent bonds are too weak to influence the three- dimensional structure of macromolecules.
An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.
Which of the following is true for the induced-fit model of enzyme-substrate binding? A. The conformation of the enzyme’s active site changes when the enzyme binds to its substrate B. Stronger interactions between the enzyme and its substrate are formed as compared to the lock-and-key model of enzyme-substrate binding C. Both A and B D. Neither A nor B Which statement does not apply to transition states? A. only exist transiently (have lifetimes on the order of 10^-14 to 10^-13 seconds) B. differ in energy from the substrate by the activation energy C. Chemical bonds are in the process of being formed and broken. D. Many have been detected and purified experimentally.
The above graphs (Lineweaver-Burk) were plotted using data from an experiment that investigated changes in initial velocity, V0, (in mmol/min) as a function of substrate concentration, [S], (in mmol/L) for an enzyme-catalysed reaction. The initial velocity was measured at a fixed concentration of enzyme at different concentrations of substrate in the absence of any inhibitor and was then repeated in the presence of a competitive inhibitor at two different concentrations. Use the graph to determine the maximal velocity of the reaction the Km value of the uninhibited reaction the Km value of the reaction with (i) the lower level of inhibitor and (ii) the higher level of the inhibitor. TEMPLATE FOR ANSWERS Vmax of uninhibited reaction Intercept on y-axis = = __________________ Vmax = __________________ Km value of the uninhibited reaction Intercept on x-axis = =…
If you graph the velocity of an enzymecatalyzed reaction vs. [S] for each of two substrates that are partof a random mechanism, would you expect to see the same shapecurve? Why or why not?

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