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Literature summary for 6.3.1.2 extracted from

  • Moss, J.; Stanley, S.J.; Levine, R.L.
    Inactivation of bacterial glutamine synthetase by ADP-ribosylation (1990), J. Biol. Chem., 265, 21056-21060.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
additional information inactivation by ADP-ribosylation. The site of ADP-ribosylation is Arg172 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
additional information the site of ADP-ribosylation is Arg172 Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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wild-type and site-directed mutants H4A, H4C, M8L, H12L, H12D
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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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Escherichia coli ADP + phosphate + L-Gln
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