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Unformatted text preview: r 10 min = 0.014 nmoles L-1 min-1 = 0.23 pmoles L-1 s-1
In the absence of inhibitor, the line intersects the x-axis at approx. 14; therefore, Km = 1 / 14 =
0.07 mM = 70 µM
In the presence of inhibitor, the line intersects the x-axis at approx. 1; therefore, Km = 1 / 1 = 1 mM
Thus, in the presence of 0.5 mM OAA, it takes more than a 14-fold higher concentration of isocitrate to
half-saturate the enzyme. Given that OAA affected the Km and not Vmax, it is a classic competitive
inhibitor, in keeping with its somewhat similar structure: Isocitrate Oxaloacetate...
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This note was uploaded on 03/15/2014 for the course MCB 102 taught by Professor Staff during the Fall '08 term at University of California, Berkeley.
- Fall '08