EC 1.4.7.1 - Glutamate synthase (ferredoxin)

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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)
Systematic name:
L-glutamate:ferredoxin oxidoreductase (transaminating)

Reaction

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00406
Structural data: CSA , EC2PDB
Gene Ontology: GO:0016041
CAS Registry Number: 62213-56-3
UniProtKB/Swiss-Prot: (12) [show] [UniProt]

References

  1. Galván, F., Márquez, A.J. and Vega, J.M.
    Purification and molecular properties of ferredoxin-glutamate synthase from Chlamydomonas reinhardtii.
    Planta 162: 180-187 (1984).
  2. Lea, P.J. and Miflin, B.J.
    Alternative route for nitrogen assimilation in higher plants.
    Nature 251: 614-616 (1974). [PMID: 4423889]
  3. Ravasio, S., Dossena, L., Martin-Figueroa, E., Florencio, F. J., Mattevi, A., Morandi, P., Curti, B., Vanoni, M. A.
    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]
  4. Navarro, F., Martin-Figueroa, E., Candau, P., Florencio, F. J.
    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]
  5. van den Heuvel, R. H., Ferrari, D., Bossi, R. T., Ravasio, S., Curti, B., Vanoni, M. A., Florencio, F. J., Mattevi, A.
    Structural studies on the synchronization of catalytic centers in glutamate synthase.
    J. Biol. Chem. 277: 24579-24583 (2002). [PMID: 11967268]
  6. van den Heuvel, R. H., Svergun, D. I., Petoukhov, M. V., Coda, A., Curti, B., Ravasio, S., Vanoni, M. A., Mattevi, A.
    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]