glutamate synthase (NADH) | |||||||||
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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 | ||||||||
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In enzymology, a 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] 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.
The systematic name of this enzyme class is L-glutamate:NAD+ oxidoreductase (transaminating). Other names in common use include: