Glutamate synthase (ferredoxin)
| glutamate synthase (ferredoxin) | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.4.7.1 | ||||||||
| CAS no. | 62213-56-3 | ||||||||
| 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 (ferredoxin) (EC 1.4.7.1) is an enzyme that catalyzes the chemical reaction
- 2 L-glutamate + 2 oxidized ferredoxin L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
Thus, the two substrates of this enzyme are L-glutamate and oxidized ferredoxin, whereas its 4 products are L-glutamine, 2-oxoglutarate, reduced ferredoxin, and H+.
This enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with an iron-sulfur protein as acceptor. The systematic name of this enzyme class is L-glutamate:ferredoxin oxidoreductase (transaminating). Other names in common use include ferredoxin-dependent glutamate synthase, ferredoxin-glutamate synthase, and glutamate synthase (ferredoxin-dependent). This enzyme participates in nitrogen metabolism. It has 5 cofactors: FAD, Iron, Sulfur, Iron-sulfur, and Flavoprotein.
Structural studies
As of late 2007, 5 structures have been solved for this class of enzymes, with PDB accession codes 1LLW, 1LLZ, 1LM1, 1OFD, and 1OFE.
References
- Jang JE, Shaw K, Yu XJ, Petersen D, Pepper K, Lutzko C, Kohn DB (2006). "Specific and stable gene transfer to human embryonic stem cells using pseudotyped lentiviral vectors". Stem. Cells. Dev. 15 (1): 109–17. doi:10.1089/scd.2006.15.109. PMID 16522168.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - Lea PJ, Miflin BJ (1974). "Alternative route for nitrogen assimilation in higher plants". Nature. 251 (5476): 614–6. doi:10.1038/251614a0. PMID 4423889.