Methionine synthase: Difference between revisions
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Every 2000 or so cycles, cobalamin needs to be <scene name='90/907471/B12_activation_w_sah/2'>reactivated</scene> through methylation by S-adenosyl methionine (SAM). To determine the structure of the reactivation conformation, the mutant H759G was used. This mutation maximises 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. | Every 2000 or so cycles, cobalamin needs to be <scene name='90/907471/B12_activation_w_sah/2'>reactivated</scene> through methylation by S-adenosyl methionine (SAM). To determine the structure of the reactivation conformation, the mutant H759G was used. This mutation maximises 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. | ||
==Methionine 3D structures== | ===Methionine 3D structures=== | ||
[[Methionine 3D structures]] | [[Methionine 3D structures]] | ||
