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Article

Mutations in the B12-binding region of methionine synthase: how the protein controls methylcobalamin reactivity.

Biochemistry - 20 Feb 1996

Jarrett J T, Amaratunga M, Drennan C L, Scholten J D, Sands R H, Ludwig M L, Matthews R G

Abstract excerpt

Vitamin B12-dependent methionine synthase catalyzes the transfer of a methyl group from methyltetrahydrofolate to homocysteine via the enzyme-bound cofactor methylcobalamin. To carry out this reaction, the enzyme must alternately stabilize six-coordinate methylcobalamin and four-coordinate cob(I)alamin oxidation states. The lower axial ligand to the cobalt in free methylcobalamin is the dimethylbenzimidazole...

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Identifiers

PMID: 8652590
DOI: 10.1021/bi952389m

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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