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Literature summary for 6.3.1.2 extracted from

  • Kimura, K.; Matsuoka, K.; Kobayashi, H.
    Regulation and properties of the glutamine synthetase purified from Photobacterium phosphoreum (1986), J. Biochem., 99, 111-117.
    View publication on PubMed
Search for more literature for 6.3.1.2

Inhibitors

Inhibitors Comment Organism Structure
Ala
-
 Photobacterium phosphoreum
Gly
-
 Photobacterium phosphoreum
Ser
-
 Photobacterium phosphoreum

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information enzyme activity is controlled by adenylylation Photobacterium phosphoreum

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
56000
-
 x * 56000, SDS-PAGE Photobacterium phosphoreum
670000
-
 gel filtration Photobacterium phosphoreum

Organism

Organism UniProt Comment Textmining
Photobacterium phosphoreum
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Photobacterium phosphoreum

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
59.3
-
-
 Photobacterium phosphoreum

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Glu + NH4+
-
 Photobacterium phosphoreum ADP + phosphate + L-Gln
-
 ?

Subunits

Subunits Comment Organism
? x * 56000, SDS-PAGE Photobacterium phosphoreum

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
additional information
-
 pH-optimum varies considerably with the state of adenylylation, and with the divalent cation used to determine the activity Photobacterium phosphoreum