Methionine synthase: Difference between revisions

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 Methionine synthase (MetH) is a B12-dependent enzyme that methylates homocysteine to regenerate methionine. The change from homocysteine to methionine is a methyl group. This reaction is regulated by methyltetrahydrofolate (a product from MTFHR) as a methyl donor and B12 as the methyl carrier.
-The <scene name='90/907471/Superposition_1/2'>full structure of MetH</scene> has yet to be determined but we understand it contains 4 domains for its catalytic and its reactivation cycles requiring B12 cobalamin (in pink), methyltetrahydrofolate (blue), homocysteine (yellow), and SAH (as part of the SAM cycle; in red).
+The <scene name='90/907471/Superposition_1/2'>full structure of MetH</scene> has yet to be determined but we understand it contains 4 domains of B12 cobalamin (in pink), methyltetrahydrofolate (blue), homocysteine (yellow), and SAH (as part of the SAM cycle; in red). Each domain with an important function required for catalytic and reactivation cycles.
-With activation of methionine synthase, the first domain of B12 is initially in a “capped” position preventing unwanted chemistry from occurring. To uncap the B12 domain, methyltransferase comes in to also assist with the methyl transfer from methyltetrahydrofolate allowing B12 to accept and carry the methyl.
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