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13 Dec 2019

In a unireactant enzyme E, with respect to substrate S:

a. the reaction is zero order at all [S]

b. the reaction is first order at all [S]

c. the reaction is second order at all [S]

d. the reaction varies between zero and first order with increasing [S]

e. the reaction varies between first and zero order with increasing [S]

Please example answer fin order for me to understand.

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Nestor RutherfordLv2

17 Dec 2019

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According the Michaelis-Menten mechanism, the dependence of enzymatic reaction rates on substrate concentration [S] isAnswer A.zero order at low [S] and first order at high [S] B.first order in [S] as long as substrate is at saturating concentration C.first order at low [S] and zero order at high [S] D.first order at low [S] and second order at high [S]

State whether the following are characteristics of zero-, first-, or second-order kinetics for the reaction R ----> P. If there is not enough information given to determine the order of the reaction, indicate so.

Use the following key to indicate your answer:

0 = zero order 1 = first order 2 = second order N/A = insufficient information

(a) ___ The reaction rate is not affected by [R].

(b) ___ A plot of ln[R] vs. time is linear.

(d) ___ A catalyst can accelerate the reaction.

(e) ___ A plot of 1/[R] vs. time is linear.

The zero order rate is seen in an enzyme catalyzed reaction when:
A. There is too much enzyme and too little substrate
B. Enzyme reactions are always first order
C. The Michaelis constant is very high
D. The V_max of the reaction is twice that which is observed
E. The enzyme substrate comples is at its maximum concentration

What happens when you add more enzyme to a catalyzed reaction that already is proceeding at V_max?
A. The reaction is inhibited because of competition for substrate
B. The plot of velocity vs. [S] will show a sigmoidal (an S-curve) shape
C. The reaction goes faster
D. The K_m of the reaction will change
E. There is no change in the rate of the reaction

Given two enzymes with the same V_max but with very different K_m values
A. The enzyme with the higher K_m will approach V_max at smaller [S]
B. V_max values cannot be the same with different K_m values
C. The steady state concentration of the enzyme-substrate complex is the same for each enzyme at every substrate concentration
D. The enzyme with a lower K_m value approaches V_max at lower [S]
E. Both values change when more enzyme is sdded

I think first one is E, second one is E, and last one is C. What are the correct answers for above?

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