Which enzyme would have the greatest catalytic efficiency? a) Km 20 nM; kcat 50 s-1 b) Km 0.04 uM; kcat 50 s-1 c) Km 10 nM; kcat 5 s-1 d) Km 40 nM; kcat 25 s-1
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Which enzyme would have the greatest catalytic efficiency?
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- Which of the following is TRUE under the following conditions: the enzyme concentration is 2.5 nM, substrate concentration is 75 nM, the KM = 150 nM, and the Vmax = 20 nmol/min a) The rate of the reaction is 20 nmol/min! b) The rate of the reaction is between 10 nmol/min and 20 nmol/min. c) The rate of the reaction is 10 nmol/min. d) The rate of the reaction is below 10 nmol/min. e) The rate cannot be determined from the above information.Based on the kinetic constants below, which enzyme will most efficiently catalyze conversion of the substrate into product? A) Vmax = 10 uM s-1, KM = 10 µM B) Vmax = 10 uM s-1, KM = 0.01 µM C) Vmax = 1000 uM s-1, KM = 500 µM D) Vmax = 1 uM s-1, KM = 1 µM E) Vmax = 200 uM s-1, KM = 10 µMAmong the following biochemical condition, which condition describes forward (spontaneous) reaction? a) Q >> Keq b) ΔΔG=0 c) Keq=1 d) Q << Keq
- Which of the following is true under the following conditions: an enzyme displaying Michaelis-Menten kinetics where the enzyme concentration is 10 nM, the substrate concentration is 45 mM, and the Km is 50 µM? a) The enzyme has low catalytic efficiency for the substrate. b)The rate of catalysis is near half-maximal velocity. c)The enzymatic reaction is near maximal velocity. d)Halving the substrate concentration has little effect on the catalytic rate. e) There is not enough information provided.there are A-D questions to this picture set up. A) What enzyme catalyzes this reaction? B) What is Delta G, please answer in Joules, K=19 C) If concentration of Glucose-1_Phosphate is 48.82 uM at equalibrium, what is the concentration of Glucose-6-phosphate in uM? D) If the reaction is NOT at equalibrium, what is delta G at 25C if the concentration of Glucose-1-phosphate is 15.04 uM and concentration of Glucose -6-phosphate is 1.62 mM? please answer in Joules and in significant figures. *note, 10^3uM in 1 mM Thank you!!Most enzymes have optimum operating conditions to function at maximum rate or velocity. Some of these conditions are the pH temperature the enzyme concentration and the substrate concentration. The optimum pH and temperature values for most enzymes are: a) pH of 1.0 and + 100 oC b) pH of 11.0 and - 7 oC c) pH of 7.0 and + 37 oC d) pH of 14.0 and + 370 oC e) None of the above
- You have been the only one who has been able to this. It has three other parts as well, A) Which Enzyme Catalyzes this reaction? choices are in image provided. B) What is ∆G°' for this reaction? Answer in Joules. K' = 19 C) If the concentration of Glucose-1-phosphate is 48.82 µM at equilibrium, what is the concentration of Glucose-6-phosphate in µM? D) If the reaction is not at equilibrium, what is ∆G' at 25°C if the concentration of Glucose-1-phosphate is 15.04µM and the concentration of Glucose-6-phosphate is 1.62 mM? Answer in Joules. Pay attention to units. Round to the correct number of significant figures. There are 103 µM in 1mM. Thank you and you are the winner for Genius of the day!!14) Which of the following statements is true under the conditions provided: the enzyme concentration is 0.5 nM, substrate concentration is 10 µM, and the KM = 20 µM? a) The enzymatic reaction occurs at maximal velocity. b) The enzymatic reaction occurs between half-maximal and maximal velocity. c) The enzymatic reaction occurs at around half-maximal velocity. d) The enzymatic reaction occurs at between zero and half-maximal velocity. e) Not enough information given to know about the enzymatic reaction rate.In a Lineweaver-Burk graph, the lines representing the uninhibited and inhibited enzyme catalyzed reaction meet each other on the x-axis. The type of inhibition which is occurring is: a) competitive b) noncompetitive c) uncompetitive d) allosteric CO2 exerts direct activity upon hemoglobin by: a) blocking oxygen from binding to the heme group b) displacing BPG from the central cavity c) oxidizing Fe+2 to Fe+3 which does not bind oxygen d) forming an N-terminal carbamate which favors the T-state The dominant motif found in hemoglobin and myoglobin is: a) helix-turn-helix b) twisted beta sheet c) beta barrel d) random coil Which of these is an ketohexose? a) fructose b) glucose c) ribose d) erythrose Which of these is a constitutional isomer of d-glucose? a) fructose b) galactose c) l-glucose d) ribose Which of these is an enantiomer of d-glucose? a) d-fructose b) d- galactose c) l-glucose d) d-ribose Which of these is a diastereomer of…
- Enzyme specificity us given by :- а) Km b) Vmax c) both d) noneIn an enzyme-catalyzed reversible reaction what happens when a) rate of change of enzyme-substrate complex concentration with time is positive b) rate of change of enzyme-substrate complex concentration with time is zero 9:0After purifying alkaline phosphatase, you perform enzyme kinetic experiments with and without an inhibitor to obtain the following plot: With inhibitor Without inhibitor 1/V (1/mM min?) 0.3 0.2 -150 -100 -50 50 100 150 200 250 300 1/s (1/mM) a) What is the name given to this type of enzymatic plot? b) Using the graph, calculate K_ and V_ inhibitor. Show all calculations. for the enzyme, with and without the max