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Literature summary for 3.5.1.78 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
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

Organism

Organism UniProt Comment Textmining
Escherichia coli
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bifunctional enzyme glutathionylspermidine synthetase/amidase
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
glutathionylspermidine + H2O
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Escherichia coli glutathione + spermidine
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