Glutamate synthase: Difference between revisions
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<StructureSection load=' | <StructureSection load='' size='350' side='right' caption='Ferredoxin-dependent glutamate synthase containing a Fe3S4 cluster complex with FMN, 2-oxoglutarate (PDB code [[1llw]])' scene='72/727110/Cv/1'> | ||
== Function == | == 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. | '''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. | ||
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== Structural highlights == | == Structural highlights == | ||
The <scene name='72/727110/Cv/ | The <scene name='72/727110/Cv/10'>Fd-GS structure contains 4 domains</scene>. The N-terminal domain is an amidotransferase domain and contains an active site where <scene name='72/727110/Cv/11'>residue Cys1</scene> catalyzes the hydrolysis of glutamine to glutarate; a core domain; an FMN-binding domain which <scene name='72/727110/Cv/12'>contains an Fe3S4 cluster</scene> and reduces the intermediate iminoglutarate to 2-oxoglutarate and produces a second molecule of glutarate and a C-terminal domain. <scene name='72/727110/Cv/13'>Residue M475 is located between the FMN and the Fe3S4 cluster</scene>. It is is strictly conserved and may perform the electron transfer between the two centers. <scene name='72/727110/Cv/14'>FMN binding site</scene> The <scene name='72/727110/Cv/15'>2-oxoglutarate binds at the FMN-binding domain</scene><ref>PMID:11967268</ref>. | ||
</StructureSection> | </StructureSection> | ||
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**[[1ea0]] – AbGS α subunit + FMN + oxo-glutarate – ''Azospirillum brasilense''<br /> | **[[1ea0]] – AbGS α subunit + FMN + oxo-glutarate – ''Azospirillum brasilense''<br /> | ||
**[[2vdc]] – AbGS α+β subunits + FAD + FMN + oxoglutarate – CryoEM<br /> | **[[6s6s]], [[6s6t]], [[6s6u]], [[6s6x]] – AbGS α+β subunits + FAD + FMN + Fe3S4 + Fe4S4 – CryoEM<br /> | ||
**[[2vdc]] – AbGS α+β subunits + FAD + FMN + Fe3S4 + Fe4S4 + oxoglutarate – CryoEM<br /> | |||
**[[7mfm]], [[7mft]] – GS + glutamate dehydrogenase – ''Bacillus subtilis'' - CryoEM<br /> | |||
*Fd-dependent glutamate synthase | *Fd-dependent glutamate synthase | ||
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== References == | == References == | ||
<references/> | <references/> | ||
[[Category:Topic Page]] | |||
Latest revision as of 13:27, 14 March 2023
FunctionGlutamate 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 highlightsThe . 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].
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3D structures of glutamate synthase3D structures of glutamate synthase
Updated on 14-March-2023
- Fd-dependent glutamate synthase
ReferencesReferences
- ↑ Vanoni MA, Curti B. Structure-function studies of glutamate synthases: a class of self-regulated iron-sulfur flavoenzymes essential for nitrogen assimilation. IUBMB Life. 2008 May;60(5):287-300. doi: 10.1002/iub.52. PMID:18421771 doi:http://dx.doi.org/10.1002/iub.52
- ↑ Hirasawa M, Tamura G. Flavin and iron-sulfur containing ferredoxin-linked glutamate synthase from spinach leaves. J Biochem. 1984 Apr;95(4):983-94. PMID:6746604
- ↑ van den Heuvel RH, Ferrari D, Bossi RT, Ravasio S, Curti B, Vanoni MA, Florencio FJ, Mattevi A. Structural studies on the synchronization of catalytic centers in glutamate synthase. J Biol Chem. 2002 Jul 5;277(27):24579-83. Epub 2002 Apr 19. PMID:11967268 doi:10.1074/jbc.M202541200