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Literature summary extracted from

  • 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 (2000), Arch. Biochem. Biophys., 379, 267-276.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.7.1 expression in Escherichia coli Synechocystis sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.7.1 2-oxoglutarate at high concentrations Synechocystis sp.
1.4.7.1 6-diazo-5-oxo-norleucine 0.05 mM, 99% inhibition Synechocystis sp.
1.4.7.1 azaserine 0.05 mM, 62% inhibition Synechocystis sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.7.1 0.0035
-
 reduced ferredoxin native enzyme Synechocystis sp.
1.4.7.1 0.0045
-
 reduced ferredoxin recombinant enzyme Synechocystis sp.
1.4.7.1 0.5
-
 2-oxoglutarate native enzyme Synechocystis sp.
1.4.7.1 0.6
-
 2-oxoglutarate recombinant enzyme Synechocystis sp.
1.4.7.1 2.2
-
 L-glutamine recombinant enzyme Synechocystis sp.
1.4.7.1 2.5
-
 L-glutamine native enzyme Synechocystis sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.7.1 Iron enzyme contains a single [3Fe-4S] cluster Synechocystis sp.

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.7.1 175000
-
 recombinant enzyme, gel filtration Synechocystis sp.
1.4.7.1 178000
-
 native enzyme, gel filtration Synechocystis sp.

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.4.7.1 L-glutamine + 2-oxoglutarate + reduced ferredoxin Synechocystis sp.
-
 L-glutamate + oxidized ferredoxin
-
 ?

Organism

EC Number Organism UniProt Comment Textmining
1.4.7.1 Synechocystis sp.
-
 PCC 6803, cyanobacterium
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.7.1 recombinant enzyme, affinity chromatography on ferredoxin-Sepharose, native enzyme, partially purified Synechocystis sp.

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.7.1 36.6
-
 recombinant enzyme Synechocystis sp.

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.7.1 L-glutamine + 2-oxoglutarate + reduced ferredoxin
-
 Synechocystis sp. L-glutamate + oxidized ferredoxin
-
 ?
1.4.7.1 L-glutamine + 2-oxoglutarate + reduced ferredoxin + H+
-
 Synechocystis sp. L-glutamate + oxidized ferredoxin
-
 r
1.4.7.1 L-glutamine + 2-oxoglutarate + reduced methylviologen
-
 Synechocystis sp. L-glutamate + oxidized methylviologen
-
 ?

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.4.7.1 55
-
 50% activity remains after 20 min, recombinant enzyme Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.7.1 FMN one FMN per enzyme molecule Synechocystis sp.