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. . Fd-dependent glutamate synthase catalyzes the reverse reaction converting L-glutamate and oxidized ferredoxin to L-glutamine, 2-oxoglutarate and oxidized ferredoxin. 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 .

spinqualitylabelsall models Ferredoxin-dependent glutamate synthase containing a Fe3S4 cluster complex with FMN, 2-oxoglutarate (PDB code 1llw) Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image

3D structures of glutamate synthase3D structures of glutamate synthase

Updated on 04-August-2020

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• Glutamate synthase

• • 1ea0 – AbGS α subunit + FMN + oxo-glutarate – Azospirillum brasilense
    
  • 6s6s, 6s6t, 6s6u, 6s6x – AbGS α+β subunits + FAD + FMN + Fe3S4 + Fe4S4 – CryoEM
    
  • 2vdc – AbGS α+β subunits + FAD + FMN + Fe3S4 + Fe4S4 + oxoglutarate – CryoEM
    
• Fd-dependent glutamate synthase
  • 1llw, 1ofd – SyGS + FMN + 2-αoxoglutarate – Synechocystis
    
  • 1llz, 1lm1 – SyGS + FMN
    
  • 1ofe – SyGS + FMN + 2-oxglutarate + oxo-norleucine