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Literature summary 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

EC Number Inhibitors Comment Organism Structure
3.5.1.78 gamma-Glu-Ala-Gly-CHO most probably captures Cys59 and accumulates as the tetrahedral adduct in the amidase active site. Binding of phosphinophosphate in the Gsp synthetase active site potentiates the inhibition affinity for the aldehyde at the Gsp amidase active site by two orders of magnitude Escherichia coli
6.3.1.8 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

EC Number Organism UniProt Comment Textmining
3.5.1.78 Escherichia coli
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 bifunctional enzyme glutathionylspermidine synthetase/amidase
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6.3.1.8 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
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.5.1.78 glutathionylspermidine + H2O
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 Escherichia coli glutathione + spermidine
-
 ?
6.3.1.8 gamma-L-Glu-L-Cys-Gly + spermidine + ATP
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 Escherichia coli N1-(gamma-L-Glu-L-Cys-Gly)-spermidine + ADP + phosphate
-
 ?