Glutamate synthase (NADH)
glutamate synthase (NADH) | |||||||||
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Identifiers | |||||||||
EC number | 1.4.1.14 | ||||||||
CAS number | 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 / EGO | ||||||||
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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+
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
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
References
- 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.
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