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Literature summary extracted from

  • Schmidt, C.N.G.; Jervis, L.
    Affinity purification of glutamate synthase from Escherichia coli (1980), Anal. Biochem., 104, 127-129.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.13 2',5'-ADP act as a competitive ihibitor Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.13 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.13 using sulfate precipitation, gel filtration and column chromatography on 2',5'-ADP-Sepharose Escherichia coli

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.4.1.13 additional information
-
-
Escherichia coli

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+
-
Escherichia coli L-glutamate + NADP+
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.13 NADPH
-
Escherichia coli

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.4.1.13 0.106
-
2',5'-ADP
-
Escherichia coli