Glutamate synthase (NADH)
| glutamate synthase (NADH) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.1.14 | ||||||||
| CAS no. | 65589-88-0 | ||||||||
| 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 | ||||||||
| |||||||||
In enzymology, a glutamate synthase (NADH) (EC 1.4.1.14) is an enzyme that catalyzes the chemical reaction
- 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
[edit]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
[edit]References
[edit]- ^ 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.
- ^ 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.
- Boland MJ, Benny AG (1977). "Enzymes of nitrogen metabolism in legume nodules. Purification and properties of NADH-dependent glutamate synthase from lupin nodules". Eur. J. Biochem. 79 (2): 355–62. doi:10.1111/j.1432-1033.1977.tb11816.x. PMID 21790.
