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Literature summary extracted from

  • Stabile, H.; Curti, B.; Vanoni, M.A.
    Functional properties of recombinant Azospirillum brasilense glutamate synthase, a complex iron-sulfur flavoprotein (2000), Eur. J. Biochem., 267, 2720-2730.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.4.1.13 expression of the holoenzyme in Escherichia coli Azospirillum brasilense

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.4.1.13 2',5'-diphosphoadenylic acid competitive inhibitor with respect to NADPH Azospirillum brasilense
1.4.1.13 2'-phosphoadenosine-5'-diphospho-5'-beta-D-ribose
-
Azospirillum brasilense
1.4.1.13 2'-phosphoadenylic acid competitive inhibitor with respect to NADPH Azospirillum brasilense
1.4.1.13 3-Aminopyridine adenine dinucleotide phosphate
-
Azospirillum brasilense
1.4.1.13 acetyl-NADP+
-
Azospirillum brasilense
1.4.1.13 NADP+
-
Azospirillum brasilense
1.4.1.13 thio-NADP+
-
Azospirillum brasilense

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.4.1.13 Iron iron-sulfur protein Azospirillum brasilense
1.4.1.13 Iron contains 12.05 mol Fe2+ per mol alphabeta protomer Azospirillum brasilense

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.13 200000
-
approximate value, the alphabeta protomeric form prevails at low protein concentration and at high ionic strength, gel filtration Azospirillum brasilense
1.4.1.13 800000
-
approximate value, the tetrameric form is found at high protein concentration and low ionic strength, gel filtration Azospirillum brasilense

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.13 Azospirillum brasilense
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.13 of the recombinant enzyme from overproducing Escherichia coli cells, using ion exchange chromatography on Q-Sepharose, gel filtration on Sephacryl S-300 and affinity chromatography on 2',5' ADP-Sepharose 4B colum Azospirillum brasilense

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
-
-
Azospirillum brasilense
1.4.1.13 17.9
-
-
Azospirillum brasilense

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+
-
Azospirillum brasilense L-glutamate + NADP+
-
?
1.4.1.13 additional information the recombinant enzyme has diaphorase activity, it can oxidize NADPH and transfer electrons to synthetic electron acceptors like iodonitrotetrazolium and ferricyanide Azospirillum brasilense ?
-
?

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.13 flavin flavoenzyme Azospirillum brasilense
1.4.1.13 flavin contains FAD and FMN Azospirillum brasilense
1.4.1.13 flavin 0.83 mol FAD and 0.86 mol FMN per mol alphabeta protomer Azospirillum brasilense
1.4.1.13 additional information the enzyme contains three different iron-sulfur clusters, one 3Fe-4S center on the alpha subunit and two 4Fe-4S clusters of unknown location, 11.7 mol sulfur per mol alphabeta protomer Azospirillum brasilense
1.4.1.13 NADPH
-
Azospirillum brasilense

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
1.4.1.13 additional information
-
additional information
-
Azospirillum brasilense
1.4.1.13 0.00023
-
thio-NADP+
-
Azospirillum brasilense
1.4.1.13 0.0024
-
3-Aminopyridine adenine dinucleotide phosphate
-
Azospirillum brasilense
1.4.1.13 0.0028
-
2'-phosphoadenosine 5'-diphospho-5-beta-D-ribose
-
Azospirillum brasilense
1.4.1.13 0.0058
-
acetyl-NADP+
-
Azospirillum brasilense
1.4.1.13 0.0059
-
NADP+
-
Azospirillum brasilense
1.4.1.13 0.048
-
2',5'-diphosphoadenylic acid
-
Azospirillum brasilense
1.4.1.13 0.186
-
2'-phosphoadenylic acid
-
Azospirillum brasilense