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Literature summary for 1.4.1.13 extracted from

  • Meister, A.
    Glutamate synthase from Escherichia coli, Klebsiella aerogenes, and Saccharomyces cerevisiae (1985), Methods Enzymol., 113, 327-337.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
L-2-Amino-4-oxo-5-chloropentanoic acid selective inhibitor of glutamine-dependent activity Escherichia coli
L-2-Amino-4-oxo-5-chloropentanoic acid selective inhibitor of glutamine-dependent activity Klebsiella aerogenes

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.012
-
NADPH
-
Klebsiella aerogenes
0.3
-
L-glutamine
-
Klebsiella aerogenes
0.3
-
alpha-ketoglutarate
-
Klebsiella aerogenes
0.5 2 NH4Cl
-
Klebsiella aerogenes

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
51500
-
x * 175000 + x * 51500, SDS-PAGE Klebsiella aerogenes
175000
-
x * 175000 + x * 51500, SDS-PAGE Klebsiella aerogenes

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-
Klebsiella aerogenes
-
-
-

Purification (Commentary)

Purification (Comment) Organism
using sonication, heat treatment, protamine sulfate precipitation, ammonium sulfate precipitation, gel filtration on G-50, column chromatography on DEAE-Sephadex and gel filtration on Sephadex G-200 and Sepharose 6B Klebsiella aerogenes

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
additional information
-
-
Escherichia coli
additional information
-
-
Klebsiella aerogenes
13.33
-
-
Escherichia coli
20.83
-
-
Klebsiella aerogenes

Storage Stability

Storage Stability Organism
4°C, 200 mM potassium phosphate buffer, pH 7.6, 0.5 mM Na2EDTA Klebsiella aerogenes

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
L-glutamine + 2-oxoglutarate + NADPH + H+ in the reverse reaction ammonia can act instead of glutamine, but more slowly Escherichia coli L-glutamate + NADP+
-
?
L-glutamine + 2-oxoglutarate + NADPH + H+ in the reverse reaction ammonia can act instead of glutamine, but more slowly Klebsiella aerogenes L-glutamate + NADP+
-
?
additional information
-
Escherichia coli ?
-
?
additional information glutamine binding site of the enzyme is located on the heavy subunit of the enzyme, preparations of the enzyme that lack flavins or the flavins and iron sulfide catalyze NH3-dependent reaction but not glutamine-dependent reaction Klebsiella aerogenes ?
-
?
NH3 + 2-oxoglutarate + NADPH + H+
-
Escherichia coli L-glutamate + NADP+
-
?
NH3 + 2-oxoglutarate + NADPH + H+
-
Klebsiella aerogenes L-glutamate + NADP+
-
?

Subunits

Subunits Comment Organism
? x * 175000 + x * 51500, SDS-PAGE Klebsiella aerogenes

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.8
-
glutamine-dependent activity Klebsiella aerogenes
8
-
glutamine-dependent activity Klebsiella aerogenes
9
-
ammonia-dependent activity Klebsiella aerogenes

Cofactor

Cofactor Comment Organism Structure
NADH no activity with NADH Escherichia coli
NADH no activity with NADH Klebsiella aerogenes
NADPH
-
Escherichia coli
NADPH
-
Klebsiella aerogenes