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Literature summary for 1.4.1.13 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

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Purification (Commentary)

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

Specific Activity [micromol/min/mg]

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

Substrates and Products (Substrate)

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

Cofactor

Cofactor Comment Organism Structure
NADPH
-
Escherichia coli

Ki Value [mM]

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