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Literature summary for 4.1.1.50 extracted from

  • Lu, Z.J.; Markham, G.D.
    Metal ion activation of S-adenosylmethionine decarboxylase reflects cation charge density (2007), Biochemistry, 46, 8172-8180.
    View publication on PubMed

Metals/Ions

Metals/Ions Comment Organism Structure
Al3+ activation, no significant influence on the rate-limiting step. Km value 0.850 mM Escherichia coli
Ca2+ activation, no significant influence on the rate-limiting step. Km value 0.117 mM Escherichia coli
Co2+ activation, no significant influence on the rate-limiting step. Km value 0.286 mM Escherichia coli
Eu3+ activation, no significant influence on the rate-limiting step. Km value 0.095 mM Escherichia coli
Fe2+ activation, no significant influence on the rate-limiting step. Km value 0.121 mM Escherichia coli
Fe3+ activation, no significant influence on the rate-limiting step. Km value 0.194 mM Escherichia coli
Gd3+ activation, no significant influence on the rate-limiting step. Km value 0.043 mM Escherichia coli
Li+ activation, no significant influence on the rate-limiting step. Km value 0.219 mM Escherichia coli
Mg2+ activation, no significant influence on the rate-limiting step. Km value 0.106 mM Escherichia coli
Mn2+ activation, no significant influence on the rate-limiting step. Km value 0.045 mM Escherichia coli
Tb3+ activation, no significant influence on the rate-limiting step. Km value 0.151 mM Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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Reaction

Reaction Comment Organism Reaction ID
S-adenosyl-L-methionine = S-adenosyl 3-(methylsulfanyl)propylamine + CO2 allosteric metal ion activation Escherichia coli