Question 26 Tess; 2-nyaroxyı groups; DNAQUESTION 26For a reaction that can take place with or without catalysis by an enzyme, what would be the effect (increase, decrease or no change) in presence of the enzyme on the:(a) Initial velocity of the reaction?(b) Equilibrium constant of the reaction?(c) Standard free energy change of the reaction?(d) Activation energy of the reaction?

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Answered: For a reaction that can take place with…

Biochemistry

9th Edition

ISBN:9781305961135

Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Publisher:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougal

Chapter6: The Behavior Of Proteins: Enzymes

Section: Chapter Questions

Problem 13RE: RECALL For the hypothetical reaction 3A+2B2C+3D the rate was experimentally determined to be...

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MATHEMATICAL The hydrolysis of a phenylalanine-containing peptide is catalyzed by -chymotrypsin with the following results. Calculate KM and Vmax for the reaction. PeptideConcentration(M)Velocity(Mmin1)2.51045.010410.010415.01042.21065.81065.91067.1106
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Initial rate data for an enzyme that obeys Michaelis–Menten kinetics areshown in the following table. When the enzyme concentration is 3 nmolml-1, a Lineweaver–Burk plot of this data gives a line with a y-intercept of0.00426 (μmol-1 ml s). (a) Calculate kcat for the reaction.(b) Calculate KM for the enzyme.(c) When the reactions in part (b) are repeated in the presence of 12 μM ofan uncompetitive inhibitor, the y-intercept of the Lineweaver–Burk plotis 0.352 (μmol-1 ml s). Calculate K′I for this inhibitor.
MATHEMATICAL For the Vmax obtained in Question 26, calculate the turnover number (catalytic rate constant) assuming that 131024mol of enzyme were used.
BIOCHEMICAL CONNECTIONS You need to carry out an enzymatic reaction at pH 7.5. A friend suggests a weak acid with a pKa of 3.9 as the basis of a buffer. Will this substance and its conjugate base make a suitable buffer? Why or why not?
BIOCHEMICAL CONNECTIONS What are the structural differences between vitamin C and sugars? Do these structural differences play a role in the susceptibility of this vitamin to air oxidation?
MATHEMATICAL An organic chemist is generally happy with 95% yields. If you synthesized a polypeptide and realized a 95% yield with each amino acid residue added, what would be your overall yield after adding 10 residues (to the first amino acid)? After adding 50 residues? After 100 residues? Would these low yields be biochemically satisfactory? How are low yields avoided, biochemically?
RECALL Using an energy diagram, show why the lock-and-key model could lead to an inefficient enzyme mechanism. Hint: Remember that the distance to the transition state must be minimized for an enzyme to be an effective catalyst.
MATHEMATICAL For an enzyme that displays MichaelisMenten kinetics, what is the reaction velocity, V (as a percentage of Vmax), observed at the following values? (a) [S]=KM (b) [S]=0.5KM (c) [S]=0.1KM (d) [S]=2KM (e) [S]=10KM
RECALL For the hypothetical reaction 3A+2B2C+3D the rate was experimentally determined to be Rate=k[A]1[B]1 What is the order of the reaction with respect to A? With respect to B? What is the overall order of the reaction? Suggest how many molecules each of A and B are likely to be involved in the detailed mechanism of the reaction.
BIOCHEMICAL CONNECTIONS For the process Nonpolarsolute+H2OSolution what are the signs of Suniv,SsysandSsurr? What is the reason for each answer? Ssurr refers to the entropy change of the surroundings, all of the Universe but the system.)

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