Saturday, February 4, 2023

84 Part 33 Regulation of Enzyme Functions EnzymesB. Pharm | Biochemistry | Bhushan Science

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A regulatory enzyme is an enzyme in a biochemical pathway which, through its responses to the presence of certain other biomolecules, regulates the pathway activity. This is usually done for pathways whose products may be needed in different amounts at different times, such as hormone production. Regulatory enzymes exist at high concentrations (low Vmax) so their activity can be increased or decreased with changes in substrate concentrations.

The enzymes which catalyse chemical reactions again and again are called regulatory enzymes.

1 Overview
2 Allosteric enzymes
2.1 Feedback inhibition
3 Covalently modulated enzymes
3.1 Phosphorylation
3.2 Proteolysis
4 References
Generally, it is considered that a hyperbolic structured protein in specific media conditions is ready to do its task, it is active, but some specific deactivation, are responsible for the regulation of some metabolism pathways. Regulatory enzymes are commonly the first enzyme in a multienzyme system: the product of the reaction catalyzed by the first enzyme is the substrate of the second enzyme, so the cell can control the amount of resulting product by regulating the activity of the first enzyme of the pathway.

There are many strategies of activation and deactivation of regulatory enzymes. Regulatory enzymes require an extra activation process and need to pass through some modifications in their 3D in order to become functional, for instance, catalyzing enzymes (regulatory enzymes). The regulation of the activation of these catalyzing enzymes is needed in order to regulate the whole reaction speed, so that it is possible to obtain the amount of product required at any time, that makes regulatory enzymes have a biological importance. Therefore, regulatory enzymes, by its controlled activation and are of two types: allosteric enzymes and covalently modulated enzymes; however, an enzyme can combine both types of regulation.

Allosteric enzymes

In a) the allosteric enzyme functions normally. In b), it is inhibited
This type of enzymes presents two binding sites: the substrate of the enzyme and the effectors. Effectors are small molecules which modulate the enzyme activity; they function through reversible, non-covalent binding of a regulatory metabolite in the allosteric site (which is not the active site). When bound, these metabolites do not participate in catalysis directly, but they are still essential: they lead to conformational changes in a concrete part of the enzyme. These changes affect the overall conformation of the active site, causing modifications on the activity of the reaction.[1]


Allosteric enzymes are generally larger in mass than other enzymes. Different from having a single subunit enzyme, in this case they are composed of multiple subunits, which contain active sites and regulatory molecule binding sites.

They present a special kinetics: the cooperation. In here, configuration changes in each chain of the protein strengthen changes in the other chains. These changes occur at the tertiary and quaternary levels of organisation.

84 Part 33 Regulation of Enzyme Functions Enzymes
B. Pharm | Biochemistry | Bhushan Science

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