faizan_ahmad
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Km is constant but Vmax will increase. Of course if the enzyme has michaelis-menten kinetics at all!
cheers,
DG
Thanks!
I am sure your argument is that Km is not a function of [E]. We have measured Km of the enzyme in the presence and absence of urea which shifts the N state <--> D state equilibrium from left to the right. We have observed that Km is increased in the presence of urea. Then this argument fails to explain this observation.
FA
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An enzyme in the native buffer solution exists in the equilibrium, native (N) state <--> denatured (D) state. So it has its KM and Vmax in this buffer. If one adds a cosolute to the enzyme solution, and if the cosolute shifts the equilibrium from D state to N state (i.e., the enzyme gets stabilized), then will the cosolute also effect the KM and Vmax?
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in Biochemistry and Molecular Biology
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I thank both of you! We equilibrate the enzyme in urea solution. The enzyme is, say 25%, denatured as measured by several conformational properties. Our buffer and substrate solutions contain the same amount of urea. So all activity measurements are done at constant urea solution. I am sure you will now come up with different answers for Km and Vmax now.