Glutamate synthase (NADPH)
| glutamate synthase (NADPH) | |||||||||
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| 270px
Glutamate synthase dodekamer, Azospirillum br.
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| Identifiers | |||||||||
| EC number | 1.4.1.13 | ||||||||
| CAS number | Template:CAS | ||||||||
| 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 / EGO | ||||||||
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In enzymology, a glutamate synthase (NADPH) (EC 1.4.1.13) 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.[1][2]
Nomenclature
The systematic name of this enzyme class is L-glutamate:NADP+ oxidoreductase (transaminating). Other names in common use include:
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- 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 1EA0.
See also
References
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