Prob Set _5 MCB 102 F 13 ANS KEY

1 014 m per 10 min 0014 nmoles l 1 min 1 023 pmoles

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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.

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