Glutamate synthase (ferredoxin)

In enzymology, a glutamate synthase (ferredoxin) is an enzyme that catalyzes the chemical reaction


 * 2 L-glutamate + 2 oxidized ferredoxin $$\rightleftharpoons$$ L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+

Thus, the two substrates of this enzyme are L-glutamate and oxidized ferredoxin, whereas its 4 products are L-glutamine, 2-oxoglutarate, reduced ferredoxin, and H+.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is L-glutamate:ferredoxin oxidoreductase (transaminating). Other names in common use include ferredoxin-dependent glutamate synthase, ferredoxin-glutamate synthase, and glutamate synthase (ferredoxin-dependent). This enzyme participates in nitrogen metabolism. It has 5 cofactors: FAD, Iron, Sulfur, Iron-sulfur, and Flavoprotein.

Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes, , , , and.