Glutamate synthase (NADPH)

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


 * 2 L-glutamate + NADP+ $$\rightleftharpoons$$ L-glutamine + 2-oxoglutarate + NADPH + H+

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

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. The systematic name of this enzyme class is L-glutamate:NADP+ oxidoreductase (transaminating). Other names in common use include glutamate (reduced nicotinamide adenine dinucleotide phosphate), synthase, L-glutamate synthase, L-glutamate synthetase, glutamate synthetase (NADP), NADPH-dependent glutamate synthase, glutamine-ketoglutaric aminotransferase, NADPH-glutamate synthase, NADPH-linked glutamate synthase, glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase,, NADP), L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing, and glutamate synthase (NADPH). This enzyme participates in glutamate metabolism and nitrogen metabolism. It has 5 cofactors: FAD, Iron, FMN, Sulfur, and Iron-sulfur.

Structural studies
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code.