Rearrangement of chorismate to prephenate. Use of chorismate mutase inhibitors to define the transition state structure

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Abstract
The enzymically catalyzed conversion of chorismate to prephenate may proceed through a chair-like or a boat-like transition state. To distinguish between these alternative, a series of structural analogs of the 2 possible transition state structures were prepared and they were tested as inhibitors of chorismate mutase-prephenate dehydrogenase [EC 1.3.1.12] from Escherichia coli K12. The enzymically catalyzed reaction passes through a chair-like intermediate. None of the compounds studied is an ideal transition state analog; the partial bond structure of the transition state probably precludes the corresponding orientation of the side chain in stable molecules. The new inhibitors [which may have potential as antibiotics or herbicides] are stronger than any previously available, and the degree of inhibition is consistent with bacteriostatic activity recently observed in some of the compounds.

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