Glutamate synthase (NADPH)
In enzymology, a glutamate synthase is an enzyme that catalyzes the chemical reaction
Thus, the four substrates of this enzyme are L-glutamine, 2-oxoglutarate, 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. Other names in common use include:
- glutamate, synthase,
- glutamate synthase,
- glutamate synthetase,
- glutamine amide-2-oxoglutarate aminotransferase,
- 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.
As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code.
