Fill the blank with the option below The substrate concentration at which an enzyme-catalyzed reaction proceeds at on-half its maximum velocity The rate enhancement of the enzyme catalyzed reaction over uncatalyzed reaction The rate of the reaction when the concentration of the products is zero and the reverse rate is negligible The rate at which the enzyme-substrate complex is formed The number of time an enzyme molecule transforms a substrate molecule per unit of time The proportionality constant that relates the velocity of a chemical reaction to the concentrations of the reactants The maximum velocity of an enzymatic reaction when the binding site is saturate with substrate A measure of the catalytic activity of an enzyme at low concentrations of substrate The rate constant for the equilibrium between the reactants and the enzyme-substrate complex

the Km of an enzyme for its substrate is 50mM. At what concentration of substrate would the enzymaticslly catalyzed reaction be at 60% maximum - 30 - 60 -75 - 50 -80

Which of the following statements regarding enzymes and transition states is true? stabilization of the transition state must be less than stabilization of ES for catalysis to occur binding of substrate to an enzyme often causes strain, thus promoting transition state formation the transition state conformation of an enzyme catalyzed reaction is identical to the conformation seen in the uncatalyzed transition state formation of the transition state always assures that the reaction will proceed to product none of the above are true

Which class of enzymes have sigmoid or S-shaped plots of the rate of a reaction, v, versus the substrate concentration, [S], instead of the hyperbolic curves of the Michaelis-Menten equation? transferases holoenzymes O hydrolases O allosteric enzymes O ribozymes

Which of the following statements is false regarding an enzyme's ability to catalyse a reaction? an enzyme provides a reaction surface and a hydrophilic environment for the reaction to take place an enzyme binds reactants such that they are positioned correctly and can attain their transition-state configurations an enzyme allows the reaction to go through a more stable transition state than would normally be the case an enzyme can weaken bonds in reactants through the binding process

For each of the statements below about the dUTPase enzyme, mark whether it is true or false. If it is false, change the language to make the statement true. _______If the dUTPase enzyme is the rate determining step in a larger metabolic pathway, the reaction likely lies near to equilibrium and is irreversible. _______For the dUTPase reaction, it is not likely that DG’ = DG°’ _______ dUTPase has a higher affinity for its substrate than for its product, but both of these are higher than the affinity for the transition state _______Kinetic analysis of dUTPase using Michaelis-Menten methods assumes that the formation of the E*S complex has a large negative value for DG

Draw the velocity curves of both regular and allosteric enzymes. Rationalize the shape of the graphs by explaining what happens during the reaction.

Number 4 please

Please help with both the parts

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