Glutamate synthase (NADH)

In enzymology, a glutamate synthase (NADH) (EC 1.4.1.14) is an enzyme that catalyzes the chemical reaction

glutamate synthase (NADH)
Identifiers
EC no.1.4.1.14
CAS no.65589-88-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
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PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
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NCBIproteins
2 L-glutamate + NAD+ L-glutamine + 2-oxoglutarate + NADH + H+

Glutamate synthase facilitates the ammonium assimilation pathway, which follows the enzymes, nitrite reductase and glutamine synthase.[1] An ammonium produced by the nitrite reductase reaction will be incorporated into carbon skeleton backbone by glutamine synthase.[2] Glutamine will be produced because of the introduction of ammonium in the carbon backbone, which can be converted into glutamate by glutamate synthase of another pathway.[2]

These processes are common in plant roots due to the fact that if the nitrogen deficient conditions exist (with access to ammonium and nitrate ions), there will be a first priority of ammonium uptake.[1] Thus, the two substrates of this enzyme are L-glutamate and NAD+, whereas its 4 products are L-glutamine, 2-oxoglutarate, NADH, 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. This enzyme participates in glutamate metabolism and nitrogen assimilation. It employs one cofactor, FMN.

Nomenclature

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The systematic name of this enzyme class is L-glutamate:NAD+ oxidoreductase (transaminating). Other names in common use include:

  • glutamate (reduced nicotinamide adenine dinucleotide) synthase,
  • glutamate synthase (NADH),
  • L-glutamate synthetase(NADH),
  • NADH-dependent glutamate synthase,
  • NADH-glutamate synthase, and
  • NADH-Glutamine oxoglutarate aminotransferase (NADH-GOGAT).

See also

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References

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  1. ^ a b Konishi, Noriyuki (27 February 2014). "NADH‐dependent glutamate synthase plays a crucial role in assimilating ammonium in the Arabidopsis root". Physiologia Plantarum. 152 (1): 138–151. doi:10.1111/ppl.12177. PMID 24576214.
  2. ^ a b Martinez-Espinosa, R.M. (30 November 2013). "Ferredoxin-dependent glutamate synthase: involvement in ammonium assimilation in Haloferax mediterranei". Extremophiles. 18 (1): 147–159. doi:10.1007/s00792-013-0606-9. PMID 24292444. S2CID 8300669.