Biology:Glutamate synthase (ferredoxin)
From HandWiki
glutamate synthase (ferredoxin) | |||||||||
---|---|---|---|---|---|---|---|---|---|
Identifiers | |||||||||
EC number | 1.4.7.1 | ||||||||
CAS number | 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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
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.
Nomenclature
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,
- glutamate synthase (ferredoxin-dependent), and
- ferredoxin-glutamine oxoglutarate aminotransferase (Fd-GOGAT).
Biological role
This enzyme participates in nitrogen metabolism. It has 5 cofactors: FAD, iron, sulfur, iron-sulfur, and flavoprotein.
See also
References
- "Specific and stable gene transfer to human embryonic stem cells using pseudotyped lentiviral vectors". Stem Cells Dev. 15 (1): 109–17. 2006. doi:10.1089/scd.2006.15.109. PMID 16522168.
- "Alternative route for nitrogen assimilation in higher plants". Nature 251 (5476): 614–6. 1974. doi:10.1038/251614a0. PMID 4423889. Bibcode: 1974Natur.251..614L.
Original source: https://en.wikipedia.org/wiki/Glutamate synthase (ferredoxin).
Read more |