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Literature summary extracted from

  • 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 (2002), Biochemistry, 41, 8120-8133.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.13 overproduction of the holoenzyme and of the alpha subunit in Escherichia coli Azospirillum brasilense
1.4.7.1
-
 Synechocystis sp.

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.7.1 6-diazo-5-oxo-norleucine reversible inactivator Synechocystis sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.13 0.23
-
 L-glutamine holoenzyme, buffer: Hepes, pH 8.5 or 7.5 Azospirillum brasilense
1.4.1.13 0.63
-
 L-glutamine alpha subunit, buffer: Hepes, pH 7.5 Azospirillum brasilense
1.4.1.13 0.73
-
 L-glutamine holoenzyme, buffer: CAPS, pH 9.5 Azospirillum brasilense
1.4.1.13 0.92
-
 L-glutamine alpha subunit, buffer: Hepes, pH 8.5 Azospirillum brasilense
1.4.1.13 1.5
-
 L-glutamine alpha subunit, buffer: CAPS, pH 9.5 Azospirillum brasilense
1.4.7.1 0.044
-
 L-glutamate L-glutamate:iodonitrotetrazolium oxidoreductase activity at pH 9.5 Synechocystis sp.
1.4.7.1 0.1
-
 reduced iodonitrotetrazolium L-glutamate:iodonitrotetrazolium oxidoreductase activity at pH 9.5 Synechocystis sp.

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.1.13 Iron iron-sulfur protein Azospirillum brasilense
1.4.7.1 Iron
-
 Synechocystis sp.

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.13 Azospirillum brasilense
-
-
-
1.4.7.1 Synechocystis sp.
-
-
-

Reaction

EC Number Reaction Comment Organism Reaction ID
1.4.7.1 2 L-glutamate + oxidized ferredoxin = L-glutamine + 2-oxoglutarate + reduced ferredoxin + 2 H+ proposed electron-transfer pathway Synechocystis sp.
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.4.1.13 L-glutamine + 2-oxoglutarate + NADPH + H+
-
 Azospirillum brasilense L-glutamate + NADP+
-
 ?
1.4.7.1 L-glutamate + oxidized iodonitrotetrazolium enzyme exhibits L-glutamate:iodonitrotetrazolium oxidoreductase activity at pH 7.5-9.5 Synechocystis sp. 2-oxoglutarate + NH3 + reduced iodonitrotetrazolium
-
 ?
1.4.7.1 L-glutamine + 2-oxoglutarate + reduced iodonitrotetrazolium + H+
-
 Synechocystis sp. L-glutamate + oxidized iodonitrotetrazolium
-
 r
1.4.7.1 L-glutamine + 2-oxoglutarate + reduced methylviologen significantly higher activity with ferredoxin than with methyl viologen Synechocystis sp. L-glutamate + oxidized methylviologen
-
 ?

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.4.7.1 3.67
-
 L-glutamate L-glutamate:iodonitrotetrazolium oxidoreductase activity at pH 9.5 Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.13 flavin flavoenzyme Azospirillum brasilense
1.4.1.13 flavin contains FAD and FMN Azospirillum brasilense
1.4.1.13 NADPH
-
 Azospirillum brasilense
1.4.7.1 FMN
-
 Synechocystis sp.