(a)
Interpretation:
A double-reciprocal plot which corresponds to the velocity-versus-substrate curveneeds to be plotted.
Concept introduction:
The Michaelis-Menten equation relates the concentration of substrate with the velocity of the reaction. A constant which expresses the substrate’s concentration if the velocity of reaction equals to the half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by
(b)
Interpretation:
A plausible explanation that corresponds to the kinetic results shown by Michaelis-Menten enzyme needs to be stated.
Concept introduction:
The Michaelis-Menten equation relates the concentration of substrate with the velocity of the reaction. A constant which expresses the substrate’s concentration if the velocity of reaction equals to the half of the maximum velocity of the reaction is known as Michaelis-Menten constant. It is denoted by
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Chapter 8 Solutions
BIOCHEMISTRY 2 TERM ACCESS
- From the reaction data below, determine whether the reaction is first order or second order and calculate the rate constant. Time (s) 0 Reactant (mM) 6.2 1 3.1 2 2.1 3 1.6 4 1.3 5 1.1 Only a plot of 1/[reactant] versus t gives a straight line, so the reaction is 0.150 mM-1 s-1 . S second order . The slope, k, isarrow_forwardFrom the reaction data below, determine whether the reaction is first order or second order and calculate the rate constant. Time (s) 0 Reactant (mM) 5.4 1 4.6 2 3.9 3 3.2 4 2.7 5 2.3 Only a plot of In[reactant] versus t gives a straight line, so the reaction is s-1. . The negative of the slope, k, isarrow_forwardA protein has a molecular mass of 400 kDa when measured by size-exclusion chromatography. When subjected to gel electrophoresis in the presence of sodium dodecyl sulfate (SDS), the protein gives three bands with molecular masses of 180, 160, and 60 kDa. When electrophoresis is carried out in the presence of SDS and dithiothreitol (DTT), three bands again form, this time with molecular masses of 160, 90, and 60 kDa. How many subunits does the protein have, and what is the molecular mass of each? four subunits: 180, 160, 90, and 60 kDa three subunits: 180, 160, and 60 kDa three subunits: 160, 90, and 60 kDa four subunits: 160, 90, 90, and 60 kDa Correct Answerarrow_forward
- Calculate KM and Vmax from the following data: KM= i Vmax [S] (μM) vo (mM.s-¹) 0.1 0.34 0.2 0.53 0.4 0.74 0.8 0.91 1.6 1.04 μM mM s-1arrow_forwardPropose a detailed chemical mechanism for the enzyme catalyzed reaction below and briefly note similarities, if any, to enzymes that we've studied. CO2 + CO2 2 CO2 HO CH3arrow_forwardState and describe the four stages of protein formation, please include the types of bonds at each stage.arrow_forward
- Please state and describe the four different types of non-covalent interactions.arrow_forwardPls help with these three questionsarrow_forward11. Which of the compounds below is the major product of the following reaction sequence? NOTE: PCC is pyridinium chlorochromate 1. BH 3 PCC 2. H2O2, NaOH NH HN ΗΝ, A B C CH3NH2, NaBH3CN D E NHarrow_forward
- 10. Which of the compounds below is the major organic product obtained from the following reaction sequence? Ph Ph Ph A B OH 1. EtMgBr H2CrO4 Zn(Hg), aq. HCI PhCHO ? 2. H₂O, H+ Ph. C D Ph "ར HO OH Earrow_forward7. What is the major organic product obtained from the following reaction sequence? Ph A OH 99 Ph OH D Br HOCH2CH2OH H2SO4 1. Mg, Et₂O 2. PhCH2CHO HCI, H₂O Br OH Ph Ph OH B C Br OH Ph Earrow_forwardPls helparrow_forward
- BiochemistryBiochemistryISBN:9781305577206Author:Reginald H. Garrett, Charles M. GrishamPublisher:Cengage LearningBiochemistryBiochemistryISBN:9781305961135Author:Mary K. Campbell, Shawn O. Farrell, Owen M. McDougalPublisher:Cengage LearningBiology: The Dynamic Science (MindTap Course List)BiologyISBN:9781305389892Author:Peter J. Russell, Paul E. Hertz, Beverly McMillanPublisher:Cengage Learning
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