Chorismate mutase from Bacillus subtilis

Chook, Y.M., Ke, H. and Lipscomb, W.N. (1993) Crystal Structures of the Monofunctional Chorismate Mutase from Bacillus subtilis and its Complex with a Transition State Analog, Proc. Nat. Acad. Sci. USA, 90, 8600-8603. 

Why is 1F7 10 -times iess active than chorismate mutase The antibody molecule s distinctive architecture does not appear to impose intrinsic structural limitations on catalysis. Indeed, comparison of the active sites of the antibody and the monofunctional enzyme from Bacillus subtilis [26] suggests that the differences between them are more a matter of degree than of kind. Upon complex formation, the hapten is buried to a similar extent in both proteins, and similar types of interactions are available for orienting the flexible substrate correctly for reaction. Furthermore, the enzyme and the antibody seem to promote the rearrangement of chorismate via the same concerted transition state as the uncatalyzed reaction. Other formal mechanistic possibilities, such as a two-step heterolytic process assisted by an enzymic nucleophile, can be ruled out by the lack of appropriate functional groups in the respective active sites [25,26]. 

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