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Literature summary for 6.3.1.8 extracted from

  • Bollinger, J.M.; Kwon, D.S.; Huisman, G.W.; Kolter, R.; Walsh, C.T.
    Glutathionylspermidine metabolism in Escherichia coli. Purification, cloning, overproduction, and characterization of a bifunctional glutathionylspermidine synthetase/amidase (1995), J. Biol. Chem., 270, 14031-14041.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
-
Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
the two activities of the bifunctional enzyme reside in distinct domains
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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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Purification (Commentary)

Purification (Comment) Organism
-
Escherichia coli

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
7.4
-
-
Escherichia coli