In enzymology, a glutamate synthase (NADPH) () is an enzyme that catalyzes the chemical reaction L-glutamine + 2-oxoglutarate + NADPH + H+ 2 L-glutamate + NADP+ Thus, the four substrates of this enzyme are L-glutamine, 2-oxoglutarate (α-ketoglutarate), NADPH, and H+, whereas the two products are L-glutamate and NADP+. This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. This enzyme participates in glutamate metabolism and nitrogen metabolism. It has 5 cofactors: FAD, Iron, FMN, Sulfur, and Iron-sulfur. It occurs in bacteria and plants but not animals, and is important as it provides glutamate for the glutamine synthetase reaction. Nomenclature 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, glutamate synthase (NADPH), glutamate synthetase (NADP), glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase, NADP), glutamine-ketoglutaric aminotransferase, L-glutamate synthase, L-glutamate synthetase, L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing, NADPH-dependent glutamate synthase, NADPH-glutamate synthase, and NADPH-linked glutamate synthase. Structural studies As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code . See also Glutamate synthase (NADH) Glutamate synthase (ferredoxin) References Further reading EC 1.4.1 NADPH-dependent enzymes Flavoproteins Iron enzymes Sulfur enzymes Iron-sulfur enzymes Enzymes of known structure