Examine the figure below, which compares the energetics of a catalyzed and uncatalyzed reaction duringthe progress of the reaction from substrate (S) to product (P). The highest peak in such a diagramcorresponds to the transition state, which is an unstable, high-energy arrangement of substrate atomsthat is intermediate between substrate and product. The free energy required to surmount this barrierto the reaction is termed the activation energy. Enzymes function by lowering the activation energy,thereby allowing a more rapid approach to equilibrium.UNCATALYZEDactivationenergyprogress of reactionCATALYZEDactivationenergyS ES|progress of reactionfree energyfree energy

Most of the chemical reactions in cells cannot undergo quickly enough by themselves. They need…

Answered: Examine the figure below, which…

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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Would 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.
Enzyme X and enzyme Y catalyze the same reaction and exhibit the νo versus [S] curves shown below. Which enzyme is more effi cient at low [S]? Which is more effi cient at high [S]?
enzyme e helps to catalyse the conversion of substrate s to product p which of the following parameters would change in response to increasing the concentration of E in this reaction - both the vmax and catalytic efficiency of enzyme e - the catalytic efficiency of enzyme e - both catalytic efficiency for E and affinity of enzyme e for substrate S - turnover number of enzymes - affinity of enzyme E for substrate S
Which of the following does NOT describe enzyme-catalyzed rate acceleration derived from the binding of substrate to enzyme a. repulsion between like charges b. substrate proximity and orientation c. reduction of entropy (increased order) d. desolvation of the substrate by the enzyme active site e. introduction of strain in bonds that need to break
The synthesis of enzymes in response to changing metabolicneeds is referred to as _____________________.
Would you expect an “enzyme” designed to bind its target substrate as tightly as it binds the reaction transition state to show a rate enhancement over the uncatalyzed reaction? In other words, would such protein be a catalyst? Use a reaction energy diagram to explain why or why not.
An enzyme catalyzes a reaction in which substrateA is cleaved into two products, P and Q. In the catalytic mechanism, the enzyme converts A to a covalently-bound reaction intermediate X and product P, P then desorbs from the enzyme, and in a second chemical step, the enzyme converts the intermediate X in the EX complex to the final product Q (in EQ), which then desorbs from the enzyme E.You discover two inhibitors of this enzyme, I and J. I is a competitive inhibitor of the substrate A, and has nearly double the molecular weight of J. On the other hand, J is a mixed inhibitor of enzyme E, and its inhibitory effect on Km/ Vmax (the slope effect from the double reciprocal plot) is greater than that of 1 / Vmax (the intercept effect in a double reciprocal plot). That is Kis< Kii . At low pH, the conversion of EX to EQ is greatly slowed, kcat is decreased, and the intercept effect of inhibitor J is elevated, that is, the value of Kiiis diminished. When a high, fixed concentration of…
Draw the structures of the amino acids whose side chainsmost commonly participate in catalytic mechanisms whenthey occur in the active sites of enzymes.
Enzyme A catalyzes the reaction S → P and has a KM of 50 μM and a Vmax of 100 nM s–1. EnzymeB catalyzes the reaction S → Q and has a KM of 5 mM and a Vmax of 120 nM s–1. When 100 μM ofS is added to a mixture containing equal amounts of enzymes A and B, which reaction product (Por Q) will be more abundant after 1 minute of reaction?
An enzyme catalyzes a reaction in which substrate A is cleaved into two products, P and Q. In the catalytic mechanism, the enzyme converts A to an covalently-bound reaction intermediate X and product P, P then desorbs from the enzyme, and in a second chemical step, the enzyme converts the intermediate X in the EX complex to the final product Q (in EQ), which then desorbs from the enzyme E. You discover two inhibitors of this enzyme, I and J. I is a competitive inhibitor of the substrate A, and has nearly double the molecular weight of J. On the other hand, J is a mixed inhibitor of enzyme E, and its inhibitory effect on Km / Vmax (the slope effect from the double reciprocal plot) is greater than that of 1 / Vmax (the intercept effect in a double reciprocal plot). That is Kis < Kii . At low pH, the conversion of EX to EQ is greatly slowed, kcat is decreased, and the intercept effect of inhibitor J is elevated, that is, the value of Kii is diminished. When a high, fixed concentration…
Which of the following statements about enzyme character-istics is true?(a) Enzymes generally exhibit a high degree of specificityfor one particular substrate.(b) Enzyme-substrate complexes occur when a substratemolecule collides with the allosteric site of an enzyme.(c) Chemical bonds within a substrate are strength-ened when this substrate forms an enzyme-substratecomplex.(d) Enzymes have a region called the active site, which pro-vides an area where it can form a loose association withits substrate.(e) a and d.
Indicate whether each of the following statements about an enzyme active site is true or false. a. It is the location where substrate molecules are produced. b. It always has a fixed, rigid geometry. c. It always has a geometrical shape exactly complementary to that of substrate. d. It always accomodates several structurally related substrates. e. It is the location where substrate molecules are converted to product molecules. f. It always has a shape that has a degree of flexibility to it. g. it always accomodates only one specific substrate.

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