Chorismate mutase Subject

Chorismate mutase (CM) catalyzes the Claisen rearrangement of chorismate to prephenate in the shikimic acid pathway used in the biosynthesis of aromatic amino acids. It represents a reference enzyme to explore the fundamentals of catalysis and has been the subject of extensive experimental and computational research. These have shown both that catalysis proceeds without covalent binding of the substrate to the enzyme, and that the uncatalyzed reaction in water proceeds by the same mechanism. This makes CM a particularly convenient target for QM/MM studies. 

The discussions given in this chapter have shown that although chorismate mutase has been a subject of extensive experimental and theoretical investigations, there are still considerable uncertainties concerning how the Claisen rearrangement from chorismate to prephenate is actually catalyzed by the enzyme. The computational investigations have led different possibilities, but experimental studies with modem techniques are necessary to identify the most likely mechanism of the CM catalysis. 

Two distinct isozymes of chorismate mutase have been demonstrated in N. silvestris. Form CM-1 is subject to allosteric control by phenylalanine, tyrosine and... 

Of the enzymes subsequent to EPSP synthase, only chorismate mutase has been the subject of inhibitor studies (see Chapter 5 by P. Bartlett in this volume). 

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