| 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, glutamate synthase (NADH) (EC 1.4.1.14) is an enzyme that catalyzes the chemical reaction
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 because if the nitrogen deficient conditions exist (with access to ammonium and nitrate ions), there will be a first priority of ammonium uptake. [1] [3] The reaction only proceeds in the direction of glutamic acid production: it converts one unit of glutamine and one 2-oxoglutarate into two units of product, using reduced nicotinamide adenine dinucleotide (NADH) as cofactor. [4]
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 uses the cofactor, flavin mononucleotide. [4]
The systematic name of this enzyme class is L-glutamate:NAD+ oxidoreductase (transaminating). Other names in common use include: