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Literature summary for 2.1.1.13 extracted from

  • Rudiger, H.
    On the cation sensibility of the vitamin B12-dependent methionine synthetase (5-methyltetrahydrofolate-homocysteine-methyltransferase from Escherichia coli) (1973), FEBS Lett., 35, 295-298.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
K+ at 67 mM 1.4 fold activity Escherichia coli
Li+ at 67 mM, 1.3fold activity Escherichia coli
Na+ at 67 mM 1.5 fold activity Escherichia coli
NH4+ at 67 mM 1.5 fold activity Escherichia coli
S-adenosylmethionine at about 0.0001 mM Escherichia coli
TrisHCl at 67 mM 1.2 fold activity Escherichia coli

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
N5-methyltetrahydrofolate + L-homocysteine
-
Escherichia coli tetrahydrofolate + L-methionine
-
?

Cofactor

Cofactor Comment Organism Structure
vitamin B12 enzyme contains a derivative of vitamin B12 as prosthetic group Escherichia coli