Chorismate Synthase - How IT Works

How It Works

Reduced flavin (FMN) transfers an electron to the substrate resulting in cleavage of the C--O bond. How this flavin is obtained differs from one organism to another and the process is not completely understood. Following the binding of EPSP, the flavin reaction intermediate is formed, but this process is completed prior to EPSP consumption. After EPSP has been converted to chorismate, and after the phosphate has been released from the enzyme,then the flavin intermediate will decay. The chorismate synthase enzyme can be divided into two categories based on how reduced FMN is obtained. Bifunctional chorismate synthase is present in fungi and require a "second enzymatic activity, an NAD(P)H-dependent flavin reductase"." Monofunctional chorismate synthase is found in plants and E.coli and is only active in an anaerobic environment with "chemically or enzymatically reduced flavin". There is no net redox change in the rection. The flavin molecule is not consumed during the reaction and merely acts as a catalyst.