PMID:8939751: Difference between revisions
imported>Wikientrybot change PMID template to TableEdit version |
imported>Wikientrybot replace GO_table_reference with annotationlinks |
||
| Line 38: | Line 38: | ||
==Annotations {{HelpIcon|Help:Literature}}== | ==Annotations {{HelpIcon|Help:Literature}}== | ||
< | <annotationlinks/> | ||
==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ==EcoliWiki Links {{HelpIcon|Help:Literature}} == | ||
Revision as of 19:53, 1 September 2013
| Citation |
No author listed (1996) The structure of the C-terminal domain of methionine synthase: presenting S-adenosylmethionine for reductive methylation of B12. Structure 4:1263-75 |
|---|---|
| Abstract |
In both mammalian and microbial species, B12-dependent methionine synthase catalyzes methyl transfer from methyltetrahydrofolate (CH3-H4folate) to homocysteine. The B12 (cobalamin) cofactor plays an essential role in this reaction, accepting the methyl group from CH3-H4folate to form methylcob(III)alamin and in turn donating the methyl group to homocysteine to generate methionine and cob(I)alamin. Occasionally the highly reactive cob(I)alamin intermediate is oxidized to the catalytically inactive cob(II)alamin form. Reactivation to sustain enzyme activity is achieved by a reductive methylation, requiring S-adenosylmethionine (AdoMet) as the methyl donor and, in Esherichia coli, flavodoxin as an electron donor. The intact system is controlled and organized so that AdoMet, rather than methyltetrahydrofolate, is the methyl donor in the reactivation reaction. AdoMet is not wasted as a methyl donor in the catalytic cycle in which methionine is synthesized from homocysteine. The structures of the AdoMet binding site and the cobalamin-binding domains (previously determined) provide a starting point for understanding the methyl transfer reactions of methionine synthase. |
| Links | |
| Keywords |
5-Methyltetrahydrofolate-Homocysteine S-Methyltransferase/chemistry; Amino Acid Sequence; Binding Sites; Computer Simulation; Conserved Sequence; Crystallography, X-Ray; Enzyme Activation; Escherichia coli/enzymology; Methylation; Models, Molecular; Molecular Sequence Data; Oxidation-Reduction; Peptide Fragments/chemistry; Protein Conformation; S-Adenosylmethionine/chemistry; Sequence Homology, Amino Acid; Vitamin B 12/metabolism |
| edit table |
Significance
You can help EcoliWiki by summarizing why this paper is useful
Useful Materials and Methods
You can help Ecoliwiki by describing the useful materials (strains, plasmids, antibodies, etc) described in this paper.
Annotations
<annotationlinks/>
EcoliWiki Links
Add links to pages that link here (e.g. gene, product, method pages)
References
See Help:References for how to manage references in EcoliWiki.