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It differs from cyanocobalamin in that the cyano group at the cobalt is replaced with a methyl group. [1] Methylcobalamin features an octahedral cobalt(III) centre and can be obtained as bright red crystals. [2] From the perspective of coordination chemistry, methylcobalamin is notable as a rare example of a compound that contains metal–alkyl ...
Methionine is activated to S-adenosyl methionine, which aids in purine and thymidine synthesis, myelin production, protein/neurotransmitters/fatty acid/phospholipid production and DNA methylation. 5-methyl tetrahydrofolate provides a methyl group, which is released to the reaction with homocysteine, resulting in methionine.
Methionine synthase transfers the methyl group to the vitamin and then transfers the methyl group to homocysteine, converting that to methionine. Methionine synthase , coded by MTR gene, is a methyltransferase enzyme which uses the MeB 12 and reaction type 2 to transfer a methyl group from 5-methyltetrahydrofolate to homocysteine , thereby ...
The mechanism of the cobalamin-independent (MetE) form, by contrast, proceeds through a direct methyl transfer from the activated N 5-MeTHF to zinc thiolate homocysteine. Although the mechanism is considerably simpler, the direct transfer reaction is much less favorable than the cobalamin-mediated reactions and as a result the turnover rate for ...
In molecular biology, the vitamin B12-binding domain is a protein domain which binds to cobalamin (vitamin B12). It can bind two different forms of the cobalamin cofactor, with cobalt bonded either to a methyl group (methylcobalamin) or to 5'-deoxyadenosine (adenosylcobalamin).
Carotenoid transcription is activated by sunlight, due to the response from AdoCbl. [3] There are other photoreceptors across different bacterial communities, aside from CarH, that also have reactive capability when bound to AdoCbl. For instance, AerR is another factor that uses AdoCbl to give off purple pigmentation.