Methionine synthase: Difference between revisions
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=== 3. Cobalamin activation === | === 3. Cobalamin activation === | ||
<scene name='90/907471/B12_activation_w_sah/1'>B12 activation</scene> | <scene name='90/907471/B12_activation_w_sah/1'>B12 activation</scene>. This structure uses the mutant H759G to maximise the fraction of enzyme with the B12 domain in the cap-off conformation bound to the activation domain. The approach of the B12 domain and the activation domain has to be carefully regulated because methylating homocysteine with methyl groups from S-adenosyl methionine results in a futile cycle. Thus, this step should be reserved to rescue B12 out of the +2 cobalt oxidation state, and then methylation of homocysteine using a methyl group from 5-me THF resumes. | ||
=== 4. Cap domain === | === 4. Cap domain === | ||
