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A disulfide-stabilized conformer of methionine synthase reveals an unexpected role for the histidine ligand of the cobalamin cofactor

B(12)-dependent methionine synthase (MetH) from Escherichia coli is a large modular protein that is alternately methylated by methyltetrahydrofolate to form methylcobalamin and demethylated by homocysteine to form cob(I)alamin. Major domain rearrangements are required to allow cobalamin to react wit...

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Detaylı Bibliyografya
Asıl Yazarlar: Datta, Supratim, Koutmos, Markos, Pattridge, Katherine A., Ludwig, Martha L., Matthews, Rowena G.
Materyal Türü: Artigo
Dil:Inglês
Baskı/Yayın Bilgisi: National Academy of Sciences 2008
Konular:
Online Erişim:https://ncbi.nlm.nih.gov/pmc/articles/PMC2393809/
https://ncbi.nlm.nih.gov/pubmed/18332423
https://ncbi.nlm.nih.govhttp://dx.doi.org/10.1073/pnas.0800329105
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