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Literature summary for 2.1.1.13 extracted from

  • Kolhouse, J.F.; Utley, C.; Stabler, S.P.; Allen, R.H.
    Mechanism of conversion of human apo- to holomethionine synthase by various forms of cobalamin (1991), J. Biol. Chem., 266, 23010-23015.
    View publication on PubMed
Search for more literature for 2.1.1.13

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
 B
-
Escherichia coli B / ATCC 11303
-
 B
-
Homo sapiens
-
-
-
Rattus norvegicus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Homo sapiens

Reaction

Reaction Comment Organism Reaction ID
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine mechanism Escherichia coli
a
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine mechanism Homo sapiens
a
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine mechanism Rattus norvegicus
a

Source Tissue

Source Tissue Comment Organism Textmining
lymphocyte
-
 Homo sapiens
-
pancreas
-
 Homo sapiens
-

Cofactor

Cofactor Comment Organism Structure
vitamin B12 mechanism of conversion of apo- to holomethionine synthase by various forms of cobalamin Escherichia coli
vitamin B12 mechanism of conversion of apo- to holomethionine synthase by various forms of cobalamin Homo sapiens
vitamin B12 mechanism of conversion of apo- to holomethionine synthase by various forms of cobalamin Rattus norvegicus
vitamin B12 enzyme contains a derivative of vitamin B12 as prosthetic group Escherichia coli
vitamin B12 enzyme contains a derivative of vitamin B12 as prosthetic group Homo sapiens
vitamin B12 enzyme contains a derivative of vitamin B12 as prosthetic group Rattus norvegicus
vitamin B12 methylcobalamin tightly bound and required Homo sapiens
vitamin B12 methylcobalamin tightly bound and required Rattus norvegicus