Methionine synthase: Difference between revisions
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=== Domain organization === | === Domain organization === | ||
Methionine synthase contains four domains, each with a unique function that bind to Cob(I)alamin as the methyl carrier. In the N-terminal, 5-MTHFR donates a methyl in the catalytic cycle to Cob(I)alamin, which then donates it to homocysteine to form methionine. However, every 2,000 cycles or so, Cob(I)alamin becomes oxidized and requires reduction and remethylation. In the C-terminal, S-adenosylmethionine or SAM donates methyl | Methionine synthase contains four domains, each with a unique function that bind to Cob(I)alamin as the methyl carrier. In the N-terminal, 5-MTHFR donates a methyl in the catalytic cycle to Cob(I)alamin, which then donates it to homocysteine to form methionine. However, every 2,000 cycles or so, Cob(I)alamin becomes oxidized (as shown below in the darker yellow color) and now requires reduction and remethylation triggering the reactivation cycle. In the C-terminal, S-adenosylmethionine or SAM donates methyl with Flavodoxin as the electron donor<ref name="Bandarian et al">DOI: 10.1038/nsb738</ref>. | ||
[[Image:Methionine synthase domains.gif]] | [[Image:Methionine synthase domains.gif]] | ||
