Glutamate synthase (NADPH)

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

The four substrates of this enzyme are L-glutamine, 2-oxoglutarate (α-ketoglutarate), NADPH, and H⁺. They are converted to the products L-glutamamic acid 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