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Literature summary for 6.3.1.2 extracted from

  • Mary, J.; Revet, B.
    Isolation and characterization of a protein with high affinity for DNA: the glutamine synthetase of Thermus thermophilus 111 (1999), J. Mol. Biol., 286, 121-134.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
additional information enzyme interacts with double-stranded DNA Thermus thermophilus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
53700
-
SDS-PAGE Thermus thermophilus
537000
-
12 * 537000, subunit mass by SDS-PAGE, native structure by negative-stain electron microscopy, consists of two hexameric rings Thermus thermophilus

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + glutamate + NH4+ Thermus thermophilus central enzyme of nitrogen metabolism ADP + phosphate + L-glutamine
-
?
ATP + glutamate + NH4+ Thermus thermophilus 111 central enzyme of nitrogen metabolism ADP + phosphate + L-glutamine
-
?

Organism

Organism UniProt Comment Textmining
Thermus thermophilus
-
-
-
Thermus thermophilus 111
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Thermus thermophilus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + glutamate + NH4+
-
Thermus thermophilus ADP + phosphate + L-glutamine
-
?
ATP + glutamate + NH4+ central enzyme of nitrogen metabolism Thermus thermophilus ADP + phosphate + L-glutamine
-
?
ATP + glutamate + NH4+
-
Thermus thermophilus 111 ADP + phosphate + L-glutamine
-
?
ATP + glutamate + NH4+ central enzyme of nitrogen metabolism Thermus thermophilus 111 ADP + phosphate + L-glutamine
-
?

Subunits

Subunits Comment Organism
dodecamer 12 * 537000, subunit mass by SDS-PAGE, native structure by negative-stain electron microscopy, consists of two hexameric rings Thermus thermophilus