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Literature summary extracted from

  • Taylor, R.T.; Hanna, M.L.
    Escherichia coli B N5-methyltetrahydrofolate-homocysteine cobalamin methyltransferase: binding of the folate substrate to the enzyme (1972), Arch. Biochem. Biophys., 151, 401-413.
    View publication on PubMed

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.1.1.13 0.035
-
5-methyltetrahydrofolate
-
Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
2.1.1.13 Escherichia coli
-
B
-
2.1.1.13 Escherichia coli B / ATCC 11303
-
B
-

Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.13 5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine mechanism Escherichia coli

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.13 additional information binding of the folate substrate Escherichia coli ?
-
?
2.1.1.13 additional information binding of the folate substrate Escherichia coli B / ATCC 11303 ?
-
?
2.1.1.13 N5-methyltetrahydrofolate + L-homocysteine
-
Escherichia coli tetrahydrofolate + L-methionine
-
?
2.1.1.13 N5-methyltetrahydrofolate + L-homocysteine
-
Escherichia coli B / ATCC 11303 tetrahydrofolate + L-methionine
-
?

Cofactor

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