Glutamate synthase

Function

Glutamate synthase (GS) is an iron-sulfur flavoprotein which catalyzes the reverse reaction which converts L-glutamine, 2-oxoglutarate and NADPH to L-glutarate and NADP. ^[1]. Fd-dependent glutamate synthase catalyzes the reverse reaction converting L-glutamate and oxidized ferredoxin to L-glutamine, 2-oxoglutarate and oxidized ferredoxin^[2]. Fd-GS uses FMN as a cofactor.

Structural highlights

The . The N-terminal domain is an amidotransferase domain and contains an active site where catalyzes the hydrolysis of glutamine to glutarate; a core domain; an FMN-binding domain which and reduces the intermediate iminoglutarate to 2-oxoglutarate and produces a second molecule of glutarate and a C-terminal domain. . It is is strictly conserved and may perform the electron transfer between the two centers. The ^[3].