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Literature summary for 1.4.1.13 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
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Cloned(Commentary)

Cloned (Comment) Organism
overproduction of the holoenzyme and of the alpha subunit in Escherichia coli Azospirillum brasilense

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.23
-
 L-glutamine holoenzyme, buffer: Hepes, pH 8.5 or 7.5 Azospirillum brasilense
0.63
-
 L-glutamine alpha subunit, buffer: Hepes, pH 7.5 Azospirillum brasilense
0.73
-
 L-glutamine holoenzyme, buffer: CAPS, pH 9.5 Azospirillum brasilense
0.92
-
 L-glutamine alpha subunit, buffer: Hepes, pH 8.5 Azospirillum brasilense
1.5
-
 L-glutamine alpha subunit, buffer: CAPS, pH 9.5 Azospirillum brasilense

Metals/Ions

Metals/Ions Comment Organism Structure
Iron iron-sulfur protein Azospirillum brasilense

Organism

Organism UniProt Comment Textmining
Azospirillum brasilense
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 2-oxoglutarate + NADPH + H+
-
 Azospirillum brasilense L-glutamate + NADP+
-
 ?

Cofactor

Cofactor Comment Organism Structure
flavin flavoenzyme Azospirillum brasilense
flavin contains FAD and FMN Azospirillum brasilense
NADPH
-
 Azospirillum brasilense