glutamate synthase (NADPH)
Glutamate synthase dodekamer, Azospirillum br.
Identifiers
EC no.1.4.1.13
CAS no.37213-53-9
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
Search
PMCarticles
PubMedarticles
NCBIproteins

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:

  • 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

  1. 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.
  2. 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


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