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Literature summary for 3.5.1.78 extracted from

  • Lin, C.H.; Kwon, D.S.; Bollinger, J.M.; Walsh, C.T.
    Evidence for a glutathionyl-enzyme intermediate in the amidase activity of the bifunctional glutathionylspermidine synthetase/amidase from Escherichia coli (1997), Biochemistry, 36, 14930-14938.
    View publication on PubMed
Search for more literature for 3.5.1.78

Protein Variants

Protein Variants Comment Organism
additional information site-directed mutagenesis indicates that Cys59 is essential for amidase activity Escherichia coli

Inhibitors

Inhibitors Comment Organism Structure
iodoacetamide
-
 Escherichia coli

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
-
 additional information
-
 Escherichia coli
5.5
-
 glutathionylspermidine C173A mutant amidase fragment Escherichia coli

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
glutathionylspermidine + H2O Escherichia coli
-
 glutathione + spermidine
-
 ?

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 bifunctional enzyme glutathionylspermidine synthetase/amidase
-

Reaction

Reaction Comment Organism Reaction ID
glutathionylspermidine + H2O = glutathione + spermidine evidence for a glutathionyl-enzyme intermediate in the amidase activity of the bifunctional enzyme Escherichia coli
a
glutathionylspermidine + H2O = glutathione + spermidine glutathionylspermidine + H2O = glutathione + spermidine, , nucleophilic attack mechanism involving Cys as the catalytic nucleophile Escherichia coli
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
gamma-Glu-Ala-Gly-4-nitroanilide + H2O
-
 Escherichia coli ?
-
 ?
glutathionylspermidine + H2O
-
 Escherichia coli glutathione + spermidine
-
 ?