In enzymology, a glutamate synthase (NADPH) (EC 1.4.1.13) is an enzyme that catalyzes the chemical reaction
| glutamate synthase (NADPH) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Glutamate synthase dodekamer, Azospirillum br. | |||||||||
| Identifiers | |||||||||
| EC no. | 1.4.1.13 | ||||||||
| CAS no. | 37213-53-9 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
- 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.[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),
- 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 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. S2CID 33617681.
Further reading edit
- Miller RE, Stadtman ER (1972). "Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein". J. Biol. Chem. 247 (22): 7407–19. PMID 4565085.
- Tempest DW, Meers JL, Brown CM (1970). "Synthesis of glutamate in Aerobacter aerogenes by a hitherto unknown route". Biochem. J. 117 (2): 405–7. doi:10.1042/bj1170405. PMC 1178874. PMID 5420057.
