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Information on EC 2.1.1.13 - methionine synthase

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EC Tree
     2 Transferases
         2.1 Transferring one-carbon groups
             2.1.1 Methyltransferases
                2.1.1.13 methionine synthase
IUBMB Comments
Contains zinc and cobamide. The enzyme becomes inactivated occasionally during its cycle by oxidation of Co(I) to Co(II). Reactivation by reductive methylation is catalysed by the enzyme itself, with S-adenosyl-L-methionine as the methyl donor and a reducing system. For the mammalian enzyme, the reducing system involves NADPH and EC 1.16.1.8, [methionine synthase] reductase. In bacteria, the reducing agent is flavodoxin, and no further catalyst is needed (the flavodoxin is kept in the reduced state by NADPH and EC 1.18.1.2, ferredoxin---NADP+ reductase). Acts on the monoglutamate as well as the triglutamate folate, in contrast with EC 2.1.1.14, 5-methyltetrahydropteroyltriglutamate---homocysteine S-methyltransferase, which acts only on the triglutamate.
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Word Map
The enzyme appears in viruses and cellular organisms
Synonyms
mets, methionine synthase, methionine synthetase, cobalamin-dependent methionine synthase, 5-methyltetrahydrofolate-homocysteine methyltransferase, b12-dependent methionine synthase, met6p, 5-methyltetrahydrofolate homocysteine methyltransferase, folate-dependent methionine synthase, tetrahydropteroylglutamate methyltransferase, more
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
5-methyltetrahydrofolate + L-homocysteine = tetrahydrofolate + L-methionine
show the reaction diagram
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