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Literature summary for 6.3.1.2 extracted from

  • Gill, H.S.; Pfluegl, G.M.; Eisenberg, D.
    Multicopy crystallographic refinement of a relaxed glutamine synthetase from Mycobacterium tuberculosis highlights flexible loops in the enzymatic mechanism and its regulation (2002), Biochemistry, 41, 9863-9872.
    View publication on PubMed
Search for more literature for 6.3.1.2

Application

Application Comment Organism
medicine potential target for anti-mycobacterial therapy Mycobacterium tuberculosis

Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli YMC21E Mycobacterium tuberculosis

Crystallization (Commentary)

Crystallization (Comment) Organism
-
 Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular
-
 Mycobacterium tuberculosis
-
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ required, two ions bound to enzyme Mycobacterium tuberculosis
Mn2+ required, two ions bound to enzyme Mycobacterium tuberculosis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
58000
-
 recombinant protein, SDS-PAGE Mycobacterium tuberculosis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ATP + glutamate + NH4+ Mycobacterium tuberculosis central enzyme of nitrogen metabolism, postulated to be necessary for the synthesis of the cell wall component poly(L-glutamine-L-glutamate) ADP + phosphate + L-glutamine
-
 ?
ATP + glutamate + NH4+ Mycobacterium tuberculosis H37Rv central enzyme of nitrogen metabolism, postulated to be necessary for the synthesis of the cell wall component poly(L-glutamine-L-glutamate) ADP + phosphate + L-glutamine
-
 ?

Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WN39
-
-
Mycobacterium tuberculosis H37Rv P9WN39
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Mycobacterium tuberculosis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + glutamate + NH4+
-
 Mycobacterium tuberculosis ADP + phosphate + L-glutamine
-
 ?
ATP + glutamate + NH4+ central enzyme of nitrogen metabolism, postulated to be necessary for the synthesis of the cell wall component poly(L-glutamine-L-glutamate) Mycobacterium tuberculosis ADP + phosphate + L-glutamine
-
 ?
ATP + glutamate + NH4+
-
 Mycobacterium tuberculosis H37Rv ADP + phosphate + L-glutamine
-
 ?
ATP + glutamate + NH4+ central enzyme of nitrogen metabolism, postulated to be necessary for the synthesis of the cell wall component poly(L-glutamine-L-glutamate) Mycobacterium tuberculosis H37Rv ADP + phosphate + L-glutamine
-
 ?

Subunits

Subunits Comment Organism
dodecamer crystal structure analysis, composed of two hexameric rings Mycobacterium tuberculosis

Cofactor

Cofactor Comment Organism Structure
AMP bound by hydrophobic forces Mycobacterium tuberculosis
citrate bound by six protein ligands Mycobacterium tuberculosis