00:02
The given question from allosteric enzyme regulation show that the allosteric regulation it occurs when an activator or the inhibitor molecule that binds with a specific molecule regulator site, regulatory site on enzyme and induces the conformational or electrostatic changes that either enhance or reduce the enzyme activity.
01:58
Not all enzyme possess site for the allosteric binding, those that do are called allosteric enzyme.
02:08
So allosteric regulation term used to describe any case in which the proteins function at one site is affected by binding of regulatory molecule to a separate site, it may result in the either inhibition or stimulation of an enzyme's activity.
02:24
So that molecules that naturally regulate enzyme activity in a cell behaves something like reversible non -competitive inhibitors these regulatory molecules change an enzyme shape and the functioning of its regulatory molecules change an enzyme shape and the function of its active side by binding to a site elsewhere on the molecule via non -covalent interaction and the inhibition is that the key difference between the non -competitive non -competitive and the allosteric inhibitions, that is the non -competitive inhibition, is the maximum rate of the catalized reaction, that is vmax, it decreases, and the substrate concentration, that is, unchanged while the allosteric inhibition v -max remains unchanged and k -max increases.
04:02
Show the allosteric enzyme unique as compared to other enzyme of its ability to adapt the various conditions in the environment due to its special properties.
04:43
The special property of allosteric enzymes is that it contains allosteric site on the top of its active site, which binds the substrate.
04:59
And the enzyme activity is regulated.
05:04
So enzyme activity, that is regulated by the changing activity.
05:27
Of a pre -existing enzyme or change the amount of an enzyme...