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Literature summary extracted from

  • Janssen, D.B.; op den Camp, H.J.M.; Leenen, P.J.M.; van der Drift, C.
    The enzymes of the ammonia assimilation in Pseudomonas aeruginosa (1980), Arch. Microbiol., 124, 197-203.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.4.1.13 1.7
-
 L-glutamine
-
 Pseudomonas aeruginosa
1.4.1.13 2
-
 2-oxoglutarate
-
 Pseudomonas aeruginosa

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.4.1.13 160000
-
 gel filtration Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
1.4.1.13 Pseudomonas aeruginosa
-
-
-
6.3.1.2 Pseudomonas aeruginosa
-
-
-

Posttranslational Modification

EC Number Posttranslational Modification Comment Organism
6.3.1.2 adenylylation the enzyme is regulated by adenylylation/deadenylylation. High levels of deadenyllylated biosynthetically active glutamine synthetase are observed in cultures growing with limiting amounts of nitrogen while synthesis of the enzyme is repressed and that present is adenylylated in cultures with excess nitrogen Pseudomonas aeruginosa

Purification (Commentary)

EC Number Purification (Comment) Organism
1.4.1.13 partial purification using column chromatography on DEAE-cellulose Pseudomonas aeruginosa

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+ ammonia does not replace L-glutamine as amino donor Pseudomonas aeruginosa L-glutamate + NADP+
-
 ?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.4.1.13 7.5
-
-
 Pseudomonas aeruginosa

Cofactor

EC Number Cofactor Comment Organism Structure
1.4.1.13 NADH no activity with NADH Pseudomonas aeruginosa
1.4.1.13 NADPH
-
 Pseudomonas aeruginosa