In a study of enzyme activity, the initial rate of reaction (y, in μMoles/min) is measured with various substrate concentrations (x, in mMoles/L) but the same enzyme concentration. The reaction rate measurements have an accuracy of 0.05 μMoles/min.

In 1913 Leonor Michaelis and Maud Menten presented a theory which predicted an inverse x & y relationship (the Michaelis-Menten equation):

1/v = (1 + K_m/[S] )/v_max

where v is the rate of reaction, v_max is the maximum possible rate of reaction, K_m is the Michaelis-Menton constant, and [S] is the concentration of the substrate. Comparison of the Michaelis-Menten equation with the generic inverse x & y relationship, suggests:

A = 1/v_max

B = K_m/v_max

so

K_m=B/A

1. Fit the below data to an inverse x & y relationship.
2. Consider the scientific claim of an inverse x & y law. Does this evidence (data) confirm or contradict this claim? Support your answer quantitatively.
3. Properly report (sigfigs, error, units) the A and B parameters of the best-fit relationship.
4. Use a spreadsheet to calculate the Michaelis-Menton constant, and properly report (sigfigs, error, units) the value.
5. Self-document the spreadsheet and turn in a hardcopy of the page.
6. Make a hardcopy plot of the data with best-fit curve. Make an additional hardcopy plot with scales chosen so as to linearize the curve. (FYI: this linearized curve is called a Lineweaver-Burk plot.)

X (mMoles/L)	Y (μMoles/min)
9.0 × 10-2	1.05
0.174	1.59
0.19	1.75
0.33	2.25
0.37	2.42
0.51	2.63
0.91	3.18
1.01	3.15
1.74	3.49
2.7	3.68

27111 7 69E7