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Literature summary for 1.4.7.1 extracted from

  • Wu, F.; Yu, P.; Yang, X.; Han, Z.; Wang, M.; Mao, L.
    Exploring ferredoxin-dependent glutamate synthase as an enzymatic bioelectrocatalyst (2018), J. Am. Chem. Soc., 140, 12700-12704 .
    View publication on PubMed

Application

Application Comment Organism
synthesis bioelectrosynthesis or bioelectrooxidation of glutamate with recombinant Fd-GltS from cyanobacteria. Bioelectrocatalytic oxidation of glutamate is oxygen independent. A sodium dithionite-methyl viologen (MV2+) system is used as the artificial reducing equivalents. Dithionite acts as the primary electron donor and reduces colorless MV2+ to the purple MV+-radical with a strong absorption at 604 nm. The system is capable of catalyzing either forward synthesis or backward oxidation by choosing different redox mediators Synechocystis sp. PCC 6803

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli Synechocystis sp. PCC 6803

Organism

Organism UniProt Comment Textmining
Synechocystis sp. PCC 6803 P55038 isoform GtlS
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 2-oxoglutarate + 2 reduced methyl viologen + 2 H+
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Synechocystis sp. PCC 6803 2 L-glutamate + 2 oxidized methyl viologen
-
?

Subunits

Subunits Comment Organism
? x * 170000, SDS-PAGE Synechocystis sp. PCC 6803

Synonyms

Synonyms Comment Organism
GltS
-
Synechocystis sp. PCC 6803

Cofactor

Cofactor Comment Organism Structure
FMN purified Fd-GltS shows absorption peaks of FMN and [3Fe4S] cluster at 345, 417, 440 and 476 nm Synechocystis sp. PCC 6803
[3Fe-4S]-center purified Fd-GltS shows absorption peaks of FMN and [3Fe4S] cluster at 345, 417, 440 and 476 nm Synechocystis sp. PCC 6803