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What are some defining characteristics of enzymes that obey Michaelis-Menten kinetics?

What are some defining characteristics of enzymes that obey Michaelis-Menten kinetics?

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Answer #1

Allosteric enzymes obey Michaelis Menten kinetics.

The Michaelis-Menten model cannot account for the kinetic properties of many enzymes.
Allosteric enzymes  do not obey Michaelis-Menten kinetics .
These enzymes consist of multiple subunits and multiple active sites.
With allosteric catalysts, the catalytic activity influencing one substrate can change the properties of other dynamic destinations situated inside a similar compound.


The after effect of this connection harmony is an agreeable impact, which means the authoritative of the substrate to a chemical's dynamic site influences the official of substrate to other active sites..
This property of cooperativity records for the sigmodial bend of V0 versus the grouping of substrate.

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