10.32 Give an explanation for the Lineweaver-Burkplot for a certain enzyme-catalyzed reaction shownbelow. Explain why the plot is not linear1Vo1[S]no to boil ante

Michaelis Menten equation describes the mathematical relationship between initial rate of reaction…

Answered: 10.32 Give an explanation for the…

Biology: The Dynamic Science (MindTap Course List)

4th Edition

ISBN:9781305389892

Author:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Publisher:Peter J. Russell, Paul E. Hertz, Beverly McMillan

Chapter6: Energy, Enzymes, And Biological Reactions

Section: Chapter Questions

Problem 16TYK

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A Lineweaver-Burk plot generates a line with the following formula: y = 0.3x + 0.4. What is the Km of this enzyme?
Lysozyme is an antibacterial enzyme found in animals. Residues Asp 101 and Arg 114 are required for efficient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not significantly alter the enzyme's tertiary structure, but significantly reduces its catalytic activity. Explain.
7.8 The turnover number is defined as the maximum number of substrate molecules that can be converted into product molecules per unit time by an enzyme molecule. The concentration of enzyme active sites is not necessarily equal to the concentration of enzyme molecules, because some enzyme molecules have more than one active site. If the enzyme molecule has one active site, the turnover number is given by turnover number=?max[E]t=?2(?max is often written as ?max)turnover number=Rmax[E]t=k2(Rmax is often written as Vmax) If the enzyme molecule has more than one active site, then [E]t[E]t is multiplied by the number of active sites to determine its effective concentration. Determine the value of the turnover number of the enzyme carbonic anhydrase, given that ?maxRmax for carbonic anhydrase equals 249 μmol⋅L−1⋅s−1249 μmol⋅L−1⋅s−1 and [E]t=2.16 nmol⋅L−1[E]t=2.16 nmol⋅L−1 . Carbonic anhydrase has a single active site. turnover number =
Trypsin, a peptidase that hydrolyzes polypeptides, functions in the small intestine at an optimum pH of 7.7–8.0. How is the rate of a trypsin-catalyzed reaction affected by each of the following conditions?
Asp residue (both of which are essential for catalysis) with pK, values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction? Explain your reasoning. (
The active site of an enzyme that uses a general acid-base catalytic mechanism contains a Glu and an Asp residue (both of which are essential for catalysis) with pKa values of 5.9 and 4.5, respectively. If the enzyme is found in the lysosome (pH = 5.2), which residue will act as the general acid and which will act as the general base during the initial steps of the reaction?
7.2 Malate dehydrogenase catalyses the reaction: (S)-malate + NAD oxaloacetate + NADH + H* The rate of the forward reaction was investigated in the presence of saturating concentrations of malate and a fixed concentration of enzyme. The following results were obtained: Absorbance (at 340 nm) at timet (minutes) [NAD'] (mmol r") 1 = 0.5 1.0 1.5 2.0 2.5 3.0 1.5 0.033 0.056 0.079 0.102 0.122 0.138 0.036 0.063 0.089 0.040 0.069 0.099 0.128 0.150 0.168 0.043 0.075 0.108 0.140 0.163 0.175 0.047 0.084 0.121 0.158 0.177 0.184 0.052 0.095 0.137 0.180 2.0 0.116 0.138 0.154 2.5 3.33 5.0 10.0 0.192 0.200 Calculate Km and Vmax-
Lysozyme residues Asp 101 and Arg 114 are required for effi cient catalysis, although they are located at some distance from the active site Glu 35 and Asp 52. Substituting Ala for either Asp 101 or Arg 114 does not signifi cantly alter the enzyme’s tertiary structure, but it signifi cantly reduces its catalytic activity. Explain.
The active site of lysozyme contains two amino acid residues essential for catalysis: Glu35 and Asp52. The pKa values of the carboxyl side chains of these residues are 5.9 and 4.5, respectively. What is the ionization state(protonated or deprotonated) of each residue at pH 5.2, the pH optimum of lysozyme? How can the ionization states of these residues explain the pH-activity profile of lysozyme shown below?
During the process of synthesizing palmitate (C16), an acyl ACP __________. For the sake of this question, don’t treat acetyl ACP or malonyl ACP as an acyl ACP; assume the acyl ACP is a product at least 4 carbons long. Choose ALL that apply. (A) can be condensed with malonyl ACP to produce a Cn+2 b-ketoacyl ACP (B) is formed from the reduction of a trans D2-enoyl ACP(C) is a product of acetyl transacylase(D) is reduced by NADPH (E) is a substrate for b-ketoacyl synthase(F) can be condensed with acetyl ACP to produce a Cn+2 b-ketoacyl ACP
Using the appropriate graph and table above, explain what the N426S mutation appears to be doing to the enzyme’s function. Discuss the kinetic parameter changes and their meaning in this context, not the structure of the enzyme, which was not given to you.
If these amino acids are separated using electrophoresis and pH = 6, will the glutamic acid move to the anode (+) or to the cathode (-) or not. Explain.

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10.32 Give an explanation for the Lineweaver-Burk plot for a certain enzyme-catalyzed reaction shown below. Explain why the plot is not linear 51 ohw 11 intidisted for barn 07 13 T [S] undidat