In enzymology, a glutamate synthase (ferredoxin) (EC 1.4.7.1) is an enzyme that catalyzes the chemical reaction
glutamate synthase (ferredoxin) | |||||||||
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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 | ||||||||
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- 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+.
Classification
editThis enzyme belongs to the family of oxidoreductases, specifically those acting on the CH-NH2 group of donors with an iron-sulfur protein as acceptor.
Nomenclature
editThe 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,
- glutamate synthase (ferredoxin-dependent), and
- ferredoxin-glutamine oxoglutarate aminotransferase (Fd-GOGAT).
Biological role
editThis enzyme participates in nitrogen metabolism. It has 5 cofactors: FAD, iron, sulfur, iron-sulfur, and flavoprotein.
See also
editReferences
edit- 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.
- Lea PJ, Miflin BJ (1974). "Alternative route for nitrogen assimilation in higher plants". Nature. 251 (5476): 614–6. Bibcode:1974Natur.251..614L. doi:10.1038/251614a0. PMID 4423889. S2CID 4184284.