Glutamate synthase (NADPH)

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In enzymology, a glutamate synthase (NADPH) (EC 1.4.1.13) is an enzyme that catalyzes the chemical reaction

2 L-glutamate + NADP⁺ $\rightleftharpoons$ L-glutamine + 2-oxoglutarate + NADPH + H⁺

Thus, the two substrates of this enzyme are L-glutamate and NADP⁺, whereas its 4 products are L-glutamine, 2-oxoglutarate, NADPH, and H⁺.

This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with NAD+ or NADP+ as acceptor. 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, L-glutamate synthase, L-glutamate synthetase, glutamate synthetase (NADP), NADPH-dependent glutamate synthase, glutamine-ketoglutaric aminotransferase, NADPH-glutamate synthase, NADPH-linked glutamate synthase, glutamine amide-2-oxoglutarate aminotransferase (oxidoreductase,, NADP), L-glutamine:2-oxoglutarate aminotransferase, NADPH oxidizing, and glutamate synthase (NADPH). This enzyme participates in glutamate metabolism and nitrogen metabolism. It has 5 cofactors: FAD, Iron, FMN, Sulfur, and Iron-sulfur.

1 Structural studies
2 References
3 External links
- 3.1 Gene Ontology (GO) codes

[edit] Structural studies

As of late 2007, only one structure has been solved for this class of enzymes, with the PDB accession code 1EA0.

[edit] References

IUBMB entry for 1.4.1.13
BRENDA references for 1.4.1.13 (Recommended.)
PubMed references for 1.4.1.13
PubMed Central references for 1.4.1.13
Google Scholar references for 1.4.1.13
Miller RE, Stadtman ER (1972). "Glutamate synthase from Escherichia coli. An iron-sulfide flavoprotein". J. Biol. Chem. 247: 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: 405–7. PMID 5420057.