Which of the following is not an assumption made when evaluating Michaelis Menton kinetics? the reaction is happening at body temperature the substrate is in great excess of the catalyst measurement of initial velocity of the reaction reaction conditions are occurring under steady state
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- With a ∆G°´ of -16.7 kJ/mol, the reaction catalyzed by hexokinase is considered to be _____. at equilibrium substrate and product concentration dependent freely reversible metabolically irreversible none of the aboveA particular reaction has a ΔG‡ of 37.0 kJ mol-1. In the presence of an enzyme, the same reaction has a ΔG‡ of 5.70 kJ mol-1. Calculate the value of ΔΔG‡ in kJ mol-1.Which of the followingdescribe superior properties of enzymes (biological catalysts) over traditional chemical catalysts? a. They are mostly and generally operative under mild temperature, pressure, and pH conditions b. They are regulated only by substrate concentration c. They do not effect the reaction equilibrium, but lower the reaction's activation energy d. They are recycled at the end of the reaction Choose all that apply
- Which of the following statements is TRUE of enzyme catalysts? for heads up question 2 and 3 are false 1) To be effective, they must be present at the same concentration as their substrate. 2) They can increase the equilibrium constant for a given reaction by a thousand-fold or more. 3) They lower the free energy for conversion of substrate to product. 4) Their catalytic activity is dependent on pH. 5) They are generally equally active on D and L isomers of a given substrate.An enzymes catalyzed reaction is studied in the presence and absence of an inhibitor. The following data was obtained in the image provided. Plot 1/[S] as abscissa and 1/V as ordinate for both catalyzed reactions and reaction with inhibitor. Use the same graph for both plots Michaelis–Menten kinetics Lineweaver–Burk plot Calculate the following: Km of enzyme in the reaction without inhibitor Km' of the enzyme in the reation with inhibitor Vmax of the uninhibited reaction Vmax of the inhibited reaction What kind of inhibitor was added to the enzyme catalyzed reaction? Explain your answer in terms of changes in Km and Vmax.Suggest an appropriate reason for the observation : “On increasing temperature of the reacting system by 10 degrees, the rate of reaction almost doubles or even some times becomes five folds.”
- A catalyst like lactase that assists in the metabolism od milk is best described as Group of answer choices homogeneous heterogeneous enzymatic non-truseable 7, What graph will demonstrate that experimental concentration data fit a second-order reaction? Group of answer choices ln[reactant] vs. time ln(k) vs. 1/T 1/[reactant] vs. time [reactant] vs. time ln(k) vs. EaA hypothetical enzyme that follows Michaelis-Menten kinetics functions has a substrate concentration 50mM at 50% of Vmax. Find the substrate concentration when the velocity of reaction is equal to 75% of Vmax.Explain the krebs cycle. You must know the reactants, products and location for each step.
- Reaction 25.2 Glucose (aq) + PO43- (aq) ⇄ Glucose-PO43- (aq) Reaction 25.2 is nonspontaneous and very slow. Use this information to sketch a reaction diagram for Reaction 25.2. Clearly label the x axis, y axis, products, reactants, and activation energy.Which of the following statements is true for the shown reaction? The reaction can occur in both cytosol and mitochondria Under starved conditions, the reaction becomes reversible to allow the synthesis of ketonebodies The reaction requires FMN as a cofactor Increase in NADH stimulates the reaction None of the aboveWhich of the following best indicates a reason why Hisneeds to be a good proton donor (not acceptor) in the catalytic triad mechanism? So that it can create the alkoxide ion. So that it can create a hydroxyde ion. None of the other options is suitable because His's only role is to be a proton acceptor. So that the first product forms and leaves with the correct number of H's. So that it can stabilize the transition state.