Literature summary 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.

Inhibitors

EC Number	Inhibitors	Comment	Organism	Structure
2.5.1.16	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
2.5.1.16	additional information	no inhibition by 1,4-diaminobutane	Escherichia coli
2.5.1.16	S-Adenosyl(5')-3-methylthiopropanol	kinetics	Escherichia coli
2.5.1.16	S-adenosyl-(5')-3-methylthio-1-propylamine	competitive substrate inhibition	Escherichia coli
2.5.1.16	S-Inosyl(5')-3-methylthiopropylamine	not S-inosyl(5')-3-methylthiopropanol	Escherichia coli

Organism

EC Number	Organism	UniProt	Comment	Textmining
2.5.1.16	Escherichia coli	-	-	-

Temperature Optimum [°C]

EC Number	Temperature Optimum [°C]	Temperature Optimum Maximum [°C]	Comment	Organism
2.5.1.16	37	-	assay at	Escherichia coli

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Release 2023.1 (January 2023)