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18 Nov 2019
Ignore the circled answers, some of them are wrong but I don't know which. What are the correct answers for questions 6-11?
6. Kinetic analysis of an enzyme using a particular substrate gave v 180 umolmin and KM 0060 mM. What would be the velocity of this reaction at the same temperature, pH, and [Ele when [S] 0.030 mM? d. 40 umol/min a. 180 umol/min e. 120 umol/min 60 umol/min 90 umol min Consider the Lineweaver-Burk plot of enzyme kinetic data that was generated by MS Excel to answer the next two questions. The linear equation for the double reciprocal plot is y 0.246x 0.0279 Lineweaver-Burk Plot of an Enzyme catalyzed conversion of S to P a. 0.246 Hmolmin b, 0.0279 umol/min c, 8.82 pumol/min 35.8 ymol/min. 0.1 4.07 umol min 1/v min/umol 0.08 8. KM equals: y 0.246x 0.0279 35.8 mM 8.82 mM c. 0.481 mM d. -0.0279 mM e, 0.100 mM 0.6 0.2 -0.2 ,246 1/[S] mM 9. Consider the kinetic plot of an enzyme catalyzed reaction to the right. Which of the following is correct concerning this enzyme? -s- Compound "Y" stabilizes the less active"T state" of this This enzyme exhibits "cooperative binding" of the substrate. This enzyme does not have quaternary structure. d. This kinetic plot implies that compound "Y" is a competitive inhibitor of a "typical" Michaelis Menten enzyme. e. Compound "X" binds to a regulatory site on the enzyme and "switches" it to the more active "R" form. 10, Phosphorylation and dephosphorylation is a means by which some enzymes can be regulated. Which amino acid residue in an enzyme is not a possible site of phosphorylation? e. all of these are sites of phosphorylation 11. What class ofenzyme catalyzes the Reaction of the Week 17? ATP CH2-OPO, 2 a. Oxidoreductase Lyase Hydrolase d. Transferase
Ignore the circled answers, some of them are wrong but I don't know which. What are the correct answers for questions 6-11?
6. Kinetic analysis of an enzyme using a particular substrate gave v 180 umolmin and KM 0060 mM. What would be the velocity of this reaction at the same temperature, pH, and [Ele when [S] 0.030 mM? d. 40 umol/min a. 180 umol/min e. 120 umol/min 60 umol/min 90 umol min Consider the Lineweaver-Burk plot of enzyme kinetic data that was generated by MS Excel to answer the next two questions. The linear equation for the double reciprocal plot is y 0.246x 0.0279 Lineweaver-Burk Plot of an Enzyme catalyzed conversion of S to P a. 0.246 Hmolmin b, 0.0279 umol/min c, 8.82 pumol/min 35.8 ymol/min. 0.1 4.07 umol min 1/v min/umol 0.08 8. KM equals: y 0.246x 0.0279 35.8 mM 8.82 mM c. 0.481 mM d. -0.0279 mM e, 0.100 mM 0.6 0.2 -0.2 ,246 1/[S] mM 9. Consider the kinetic plot of an enzyme catalyzed reaction to the right. Which of the following is correct concerning this enzyme? -s- Compound "Y" stabilizes the less active"T state" of this This enzyme exhibits "cooperative binding" of the substrate. This enzyme does not have quaternary structure. d. This kinetic plot implies that compound "Y" is a competitive inhibitor of a "typical" Michaelis Menten enzyme. e. Compound "X" binds to a regulatory site on the enzyme and "switches" it to the more active "R" form. 10, Phosphorylation and dephosphorylation is a means by which some enzymes can be regulated. Which amino acid residue in an enzyme is not a possible site of phosphorylation? e. all of these are sites of phosphorylation 11. What class ofenzyme catalyzes the Reaction of the Week 17? ATP CH2-OPO, 2 a. Oxidoreductase Lyase Hydrolase d. Transferase
Bunny GreenfelderLv2
19 Sep 2019