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Literature summary for 6.3.1.2 extracted from

  • Harth, G.; Horwitz, M.A.
    Expression and efficient export of enzymatically active Mycobacterium tuberculosis glutamine synthetase in Mycobacterium smegmatis and evidence that the information for export is contained within the protein (1997), J. Biol. Chem., 272, 22728-22735.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
expression in Escherichia coli YMC21E, but no release of the active enzyme Mycobacterium tuberculosis
expression in Mycobacterium smegmatis results in a release of more than 95% of all recombinant enzyme. No hybrid molecules containing Mycobacterium tuberculosis and Mycobacterium smegmatis glutamine synthetase subunits are detected Mycobacterium tuberculosis

Localization

Localization Comment Organism GeneOntology No. Textmining
extracellular extracellular release is correlated with pathogenicity. The information to target the protein for export must be contained in its amino acid sequence and/or conformation Mycobacterium tuberculosis
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Organism

Organism UniProt Comment Textmining
Mycobacterium tuberculosis P9WN39
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Mycobacterium tuberculosis H37Rv P9WN39
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Mycolicibacterium smegmatis
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + L-Glu + NH4+
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Mycolicibacterium smegmatis ADP + phosphate + L-Gln
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?
ATP + L-Glu + NH4+
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Mycobacterium tuberculosis ADP + phosphate + L-Gln
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?
ATP + L-Glu + NH4+
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Mycobacterium tuberculosis H37Rv ADP + phosphate + L-Gln
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?