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Literature summary extracted from

  • Hirasawa, M.; Solis, J.; Vaidyanathan, N.; Srivastava, A.P.; Wynn, R.M.; Sutton, R.B.; Knaff, D.B.
    Identification of the ferredoxin interaction sites on ferredoxin-dependent glutamate synthase from Synechocystis sp. PCC 6803 (2017), Photosynth. Res., 134, 317-328 .
    View publication on PubMed

Protein Variants

EC Number Protein Variants Comment Organism
1.4.7.1 H1144Q ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 18.7fold Synechocystis sp.
1.4.7.1 additional information residues Gln467, His1144, Asn1147, Arg1162, and Trp676 constitute key binding residues in the interface of a glutamate synthase:ferredoxin complex. All interfacial mutants studied are able to form a complex under low ionic strength, but show significantly less ferredoxin-dependent activities, while still retaining enzymatic activity Synechocystis sp.
1.4.7.1 N1147A ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 47.4fold Synechocystis sp.
1.4.7.1 Q467A ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 5.5fold Synechocystis sp.
1.4.7.1 R1162A ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 4.7fold Synechocystis sp.
1.4.7.1 W676A ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 6.7fold Synechocystis sp.
1.4.7.1 W676F ratio between the ferredoxin-dependent and the methyl viologen-dependent GOGAT activities is decreased by 7.9fold Synechocystis sp.

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.7.1 0.0006
-
 oxidized ferredoxin wild-type, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0009
-
 oxidized ferredoxin mutant W676F, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0013
-
 L-glutamine wild-type, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0018
-
 L-glutamine mutant R1162A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0019
-
 2-oxoglutarate mutant N1147A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0027
-
 L-glutamine mutant H1144Q, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0028
-
 L-glutamine mutant Q467A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0028
-
 oxidized ferredoxin mutant Q467A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0032
-
 oxidized ferredoxin mutant H1144Q, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0044
-
 oxidized ferredoxin mutant N1147A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0056
-
 oxidized ferredoxin mutant R1162A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0071
-
 oxidized ferredoxin mutant W676A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.0194
-
 L-glutamine mutant N1147A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.023
-
 L-glutamine mutant W676A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.04
-
 2-oxoglutarate wild-type, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.043
-
 L-glutamine mutant W676F, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.051
-
 2-oxoglutarate mutant Q467A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.112
-
 2-oxoglutarate mutant H1144Q, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.125
-
 2-oxoglutarate mutant R1162A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.128
-
 2-oxoglutarate mutant W676A, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.
1.4.7.1 0.51
-
 2-oxoglutarate mutant W676F, pH not specified in the publication, temperature not specified in the publication Synechocystis sp.

Organism

EC Number Organism UniProt Comment Textmining
1.4.7.1 Synechocystis sp. P55037 isoform GltB
-

Substrates and Products (Substrate)

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

Synonyms

EC Number Synonyms Comment Organism
1.4.7.1 gltB
-
 Synechocystis sp.

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.7.1 Ferredoxin 1:2 molar ratio between the wild-type glutamate synthase and ferredoxin Synechocystis sp.