Catalysis and allosteric regulation

Montero-Moran GM, Lara-Gonzalez S, Alvarez-Anorve LI et al (2001) On the multiple functional roles of the active site histidine in catalysis and allosteric regulation of Escherichia coli glucosamine 6-phosphate deaminase. Biochemistry 40 10187-10196... 

Not only does allosteric regnlation have a profound influence on our understanding of biochemical regulation but the concept has considerable biological importance. These two sites within the enzyme, catalytic and allosteric, can evolve independently to provide the most efficient systems for both catalysis and regnlation. 

There are several demonstration cases that successfully reproduce heterotopic allosteric systems. 64-701 Design of homotropic allosteric systems, on the other hand, is more difficult, but more important for the efficient regulation of equilibria and catalysis. 71,72 Here we introduce several examples of four different allosteric systems, designed mainly with regard to sugar recognition. 

The regulation of enzyme action and function can be accomplished by allosteric effects. The binding of an effector at an allosteric site can induce conformational changes at an active site and alter the reactivity of an enzyme towards its substrate. This feature of enzymic catalysis should be capable of imitation in simpler synthetic systems. 

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