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.
Disease
Relevance
Structural highlights
The Fd-GS structure contains 4 domains. The N-terminal domain is an amidotransferase domain and contains an active site where residue 1Cys catalyzes the hydrolysis of glutamine to glutarate; a core domain; an FMN-binding domain which contains an Fe3S4 cluster and reduces the intermediate iminoglutarate to 2-oxoglutarate and produces a second molecule of glutarate and a C-terminal domain. Residue M475 is located between the FMN and the Fe3S4 cluster. It is is strictly conserved and may perform the electron transfer between the two centers. The 2-oxoglutarate binds at the FMN-binding domain[3].
