enzymology, a glutamate synthase (NADPH) ( EC 184.108.40.206) is an enzyme that catalyzes the chemical reaction
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. [1 ] [2 ]
Nomenclature [ edit ]
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),
L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing,
NADPH-dependent glutamate synthase,
NADPH-glutamate synthase, and
NADPH-linked glutamate synthase.
Structural studies [ edit ]
As of late 2007, only one
structure has been solved for this class of enzymes, with the PDB accession code 1EA0.
See also [ edit ]
References [ edit ]
^ Temple SJ, Vance CP, Gantt JS (1998). "Glutamate synthase and nitrogen assimilation". Trends in Plant Science 3 (2): 51–56. doi: 10.1016/S1360-1385(97)01159-X.
^ Vanoni MA, Curti B (May 2008). "Structure-function studies of glutamate synthases: a class of self-regulated iron-sulfur flavoenzymes essential for nitrogen assimilation". IUBMB Life 60 (5): 287–300. doi: 10.1002/iub.52. PMID 18421771.
Further reading [ edit ]