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Regulartory Enzymes

Homotropic enzymes some enzymes having multiple units (two or more) interact in cooperation with each other ot yield enhanced responses to their substrates. The substrate molecyle functions as a modulator accelerating the enzyme activity. In this case all the interacting enzyme units are identical, each with a catalytic site. Haemoglobin is one such compound that exhibits homotropic kinetics. Binding of one substrate molecule (oxygen in the substrate ) with one subunit brings about a conformational change and subsequently increase the affinity of exygenwith the remaining subunits. This is a case of positive cooperativeity and the relationship is sigmoidal.

enzyme catalyzing the first step and fatty acid synthetease complex

behaviour of allosteric enzyme

A model was proposed by Monod –changeux – Wyman (MCW –Model) to explain the experimental observations on the behavior of allosteric enzymes. In case the binding of additional molecules, the cooperatively is negative.

allosteric enzyme teteamer

Heterotropic Enzymes a heterotropic enzyme has at least two sites, one for the substrate and the other for the modulator which is different from the substrate. Let us consider an example to explain heterotropic regulation.

Phosphofructokinase is an enzyme that transfers a phosphate group from ATP to phosphorylate fructose-6-phosphate to form fructose 1, 6-diphosphate. This is the substrate for oxidation to yield usable energy in terms of ATP. The enzyme catalyzes an irreversible reaction and in order to effector.  When the concentration of AMP rises, it indicates the need of more product of the reaction, functions as an activator to regulate phosphofructokinase.

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