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Literature summary for 6.3.1.8 extracted from

  • Lin, C.H.; Chen, S.; Kwon, D.S.; Coward, J.K.; Walsh, C.T.
    Aldehyde and phosphinate analogs of glutathione and glutathionylspermidine: potent, selective binding inhibitors of the E. coli bifunctional glutathionylspermidine synthetase/amidase (1997), Chem. Biol., 4, 859-866.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
N1-glutathionylspermidine analogs selective inhibitors against EC 6.3.1.8 and EC 3.5.1.78 activities provide evidence of interdomain communication in the bifunctional enzyme Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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the enzyme is bifunctional and also catalyzes the glutathionylspermidine amidase reaction, EC 3.5.1.78, resulting in a net hydrolysis of ATP
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
gamma-L-Glu-L-Cys-Gly + spermidine + ATP
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Escherichia coli N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
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