Vmax

That's it. The velocity approaches Vmax asymptotically as the substrate concentration increases. However, changing other conditions can change the Michaelis–Menten plot -- for instance, a different pH or a different temperature can lead to ...

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... I recorded 28 points with [S] (mM) and V (mM/min). I subsequently plotted two graphs (a Michaelis-Menten and Lineweaver burk) and calculated the Vmax and Km. Vmax = 0.005033 mM/min KM = 23.41 So that I completely understand: the maximum velocity this enzyme can react at is 0.005022 mM/min at ...

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... by plotting the 1/[V] by 1/[S] graph, we may find the intercept on y axis....which is 1/Vm in this case....and then do the reciprocal to find out Vmax.....and then put this value in the above equation.....at a particular [S] and v....and find the value of Km....:)

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The two terms overlap to some extent. All "non-competitive" means is that the inhibitor lowers Vmax without changing Km. You can't read much mechanism into it. The notion of competitive, non-competitive, mixed-competitive are all kinetic behaviors. An allosteric site ...

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Sorry, that should be X -intercept = -1/Km, not y-intercept. And the slope is Km/Vmax not Vmax. Memory didn't serve me very well this time and I was too lazy to derive it from the rate expression-though that's a useful excercise if you've never done it before. This ...

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