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 (Comment) | Organism |
---|---|
expression in Escherichia coli | Synechocystis sp. PCC 6803 |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Synechocystis sp. PCC 6803 | P55038 | isoform GtlS | - |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
L-glutamine + 2-oxoglutarate + 2 reduced methyl viologen + 2 H+ | - |
Synechocystis sp. PCC 6803 | 2 L-glutamate + 2 oxidized methyl viologen | - |
? |
Subunits | Comment | Organism |
---|---|---|
? | x * 170000, SDS-PAGE | Synechocystis sp. PCC 6803 |
Synonyms | Comment | Organism |
---|---|---|
GltS | - |
Synechocystis sp. PCC 6803 |
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 |