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Literature summary for 2.5.1.16 extracted from

  • Zappia, V.; Cacciapuoti, G.; Pontoni, G.; Oliva, A.
    Mechanism of propylamine-transfer reactions. Kinetic and inhibition studies on spermidine synthase from Escherichia coli (1980), J. Biol. Chem., 255, 7276-7280.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
deaminated analogs of decarboxy-S-adenosyl-(5')-3-methylthiopropylamine competitive inhibition with 1,4-diaminobutane and non-competitive with decarboxy-S-adenosyl-(5')-3-methylthiopropylamine Escherichia coli
additional information no inhibition by 1,4-diaminobutane Escherichia coli
S-Adenosyl(5')-3-methylthiopropanol kinetics Escherichia coli
S-adenosyl-(5')-3-methylthio-1-propylamine competitive substrate inhibition Escherichia coli
S-Inosyl(5')-3-methylthiopropylamine not S-inosyl(5')-3-methylthiopropanol Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
37
-
assay at Escherichia coli