EC 1 - Oxidoreductases
EC 1.4 - Acting on the CH-NH2 group of donors
EC 1.4.7 - With an iron-sulfur protein as acceptor
EC 1.4.7.1 - Glutamate synthase (ferredoxin)
IntEnz view
ENZYME view
IntEnz Enzyme Nomenclature
EC 1.4.7.1
Names
Accepted name:
glutamate synthase (ferredoxin)
Other
names:
ferredoxin-dependent glutamate synthase
ferredoxin-glutamate synthase
glutamate synthase (ferredoxin-dependent)
ferredoxin-glutamate synthase
glutamate synthase (ferredoxin-dependent)
Systematic name:
L-glutamate:ferredoxin oxidoreductase (transaminating)
Reactions
- (1) 2 L-glutamate + 2 oxidized ferredoxin = L-glutamine + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
- (1a) L-glutamate + NH3 = L-glutamine + H2O
- (1b) L-glutamate + 2 oxidized ferredoxin + H2O = NH3 + 2-oxoglutarate + 2 reduced ferredoxin + 2 H+
Cofactors
Comments:
Binds a [3Fe-4S] cluster as well as FAD and FMN. The protein is composed of two domains, one hydrolysing L-glutamine to NH3 and L-glutamate (cf. EC 3.5.1.2, glutaminase), the other combining the produced NH3 with 2-oxoglutarate to produce a second molecule of L-glutamate. The NH3 is channeled through a 24 Å channel in the active protein. No hydrolysis of glutamine takes place without ferredoxin and 2-oxoglutarate being bound to the protein [5,6].
Links to other databases
Protein domains and families:
PROSITE:PDOC00406
Gene Ontology:
GO:0016041
CAS Registry Number:
62213-56-3
References
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Purification and molecular properties of ferredoxin-glutamate synthase from Chlamydomonas reinhardtii.Planta 162 : 180-187 (1984).
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Alternative route for nitrogen assimilation in higher plants.Nature 251 : 614-616 (1974). [PMID: 4423889]
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Properties of the recombinant ferredoxin-dependent glutamate synthase of Synechocystis PCC6803. Comparison with the Azospirillum brasilense NADPH-dependent enzyme and its isolated alpha subunit.Biochemistry 41 : 8120-8133 (2002). [PMID: 12069605]
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Ferredoxin-dependent iron-sulfur flavoprotein glutamate synthase (GlsF) from the Cyanobacterium synechocystis sp. PCC 6803: expression and assembly in Escherichia coli.Arch. Biochem. Biophys. 379 : 267-276 (2000). [PMID: 10898944]
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Structural studies on the synchronization of catalytic centers in glutamate synthase.J. Biol. Chem. 277 : 24579-24583 (2002). [PMID: 11967268]
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The active conformation of glutamate synthase and its binding to ferredoxin.J. Mol. Biol. 330 : 113-128 (2003). [PMID: 12818206]
[EC 1.4.7.1 created 1976, modified 2012]