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You characterize a new enzyme's kinetics.

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You characterize a new enzyme's kinetics. Using a saturating (very high so all E is ES) substrate concentration, you measure the initial rate of the reaction at various enzyme concentrations. Does this data fit the Michaelis Menton model/equation? If not, what may be happening?

E (nM), rate (mM,s)

5, 50
10, 225
15, 500
25, 1500
50, 3600
100, 7200

A. NO, the rate should only vary with substrate concentration, not enzyme concentration. The person collecting the data doesn't have a clue.

B. No, the activity does not change with increasing enzyme concentration correctly. The enzyme may be only active in a dimer that forms a high concentration.

C. Yes, it obeys the MM equation well.

D. No, the activity does not change with increasing enzyme concentration correctly. The enzyme may be inactive in a dimer that forms at high concentration

E. No, the rate should decrease as you increase the enzyme concentration. This reaction is not enzyme catalyzed.

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In regards to enzyme concentration, as the enzyme concentration increases the rate of the reaction increases linearly, because there are ...

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Michaelis-Menton Equation and finding Vmax and Km from a graph

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A) What is the initial velocity v0 called when the substrate concentration [S] >>>KM ([S] )?
Label on graph.
B) Simplify the above MM equation using the assumption that [S] >>>KM. From this simplified equation, what is the rate constant that describes the MM kinetics in the region [S] >>>KM?
Indicate on graph.
1. Would this rate be useful in determining the catalytic efficiency of a biological enzyme under physiological conditions?
C) Simplify the above MM equation using assumption the [S] <<KM. From this simplified equation, what is the rate constant that describes the MM kinetics for [S] <<KM?
1. Would this rate be useful in determining the catalytic efficiency of a biological enzyme under physiological conditions?
D) Using the MM equation, what is true about the initial velocity v0 when KM = [S]?
Indicate on the graph.
This is the concentration at which one half of the enzyme's active sites are occupied by substrates.

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