Lecture_19-M-M_Transformations

Lecture_19-M-M_Transformations - 5 105 3 105 0 -1 v (s ) 4...

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ENZYME KINETICS Transformations of the Michaelis-Menten Equation 0 1 10 5 2 10 5 3 10 5 4 10 5 5 10 5 0 5 10 15 20 25 v 0 (s -1 ) [S] 0 (mM) K M V max /2 What is the approximate V max for this enzyme? 4.5 x 10 5 What is the approximate K M for this enzyme? 5 μM The M-M Equation can be transformed to provide more accurate information 1. Standard MM Equation v 0 = V max S [ ] K M + S [ ] 2. Take the inverse of both sides 1 v 0 = K M + S [ ] V max S [ ] 3. Separate into two parts and simplify 1 v 0 = K M V max S [ ] + S [ ] V max S [ ] 1 v 0 = K M V max S [ ] + 1 V max 1 v 0 = K M V max 1 S [ ] + 1 V max Linear transformation of the M-M equation! 1 v 0 = K M V max 1 S [ ] + 1 V max y = m x + b ± a plot of 1/v 0 vs 1/[S] yields a straight line ± the slope is K M /V max ± the y-intercept is 1/V max ± the -x-intercept (set y = 0) = -1/K M
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1 v 0 = K M V max 1 S [ ] + 1 V max v 0 = V max S [ ] K M + S [ ] [S] (mM) v 0 (μM•s -1 ) 1 2.5 2 4.0 7 6.3 10 7.6 20 9.0 2 3 4 5 6 7 8 9 10 0 5 10 15 20 25 v0 ( µ M•s-1) v 0 ( µ M•s -1 ) [S] ( µ M) 1/[S] 1/v 0 1 0.4 0.5 0.25 0.2 0.16 0.1 0.13 0.05 0.11 0.1 0.15 0.2 0.25 0.3 0.35 0.4 0.45 0 0.2 0.4 0.6 0.8 1 1.2 1/v0 y = 0.10419 + 0.29589x R= 0.99803 1/v 0 1/[S] 1 v 0 = K M V max 1 S [ ] + 1 V max y-intercept = 0.104 -x-intercept = -1/K M y = 0.296x + 0.104 0.1 0.15 0.2 0.25 0.3 0.35 0.4 0.45 0 0.2 0.4 0.6 0.8 1 1.2 1/v0 y = 0.10419 + 0.29589x R= 0.99803 1/[S] = 1/V max V max = 9.615 μM•s -1 = -1/0.35 K M = 2.8μM (set y=0 in the equation) Reversible Inhibition
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This note was uploaded on 11/28/2011 for the course CHEM 340 taught by Professor T.baird during the Fall '11 term at S.F. State.

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Lecture_19-M-M_Transformations - 5 105 3 105 0 -1 v (s ) 4...

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