Methionine synthase
From Proteopedia
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Revision as of 14:12, 3 April 2022
Contents |
Methionine synthase
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The change from homocysteine to methionine is an SN2 reaction where one methyl group from methyltetrahydrofolate (MTHF), located on N-5, is donated. MTHF is a product of MTHFR.
This is a complex reaction as the product, tetrahydrofolate, is a poor leaving group, thus requiring a "supernucleophile" with a protein-bound B-12 vitamin Cobalamin as the methyl carrier.
Vitamin B-12
Oxidation States of Cobalamin
Relevance
Structural highlights
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</StructureSection>
References
- ↑ Kung Y, Ando N, Doukov TI, Blasiak LC, Bender G, Seravalli J, Ragsdale SW, Drennan CL. Visualizing molecular juggling within a B(12)-dependent methyltransferase complex. Nature. 2012 Mar 14. doi: 10.1038/nature10916. PMID:22419154 doi:10.1038/nature10916
- ↑ Bandarian V, Pattridge KA, Lennon BW, Huddler DP, Matthews RG, Ludwig ML. Domain alternation switches B(12)-dependent methionine synthase to the activation conformation. Nat Struct Biol. 2002 Jan;9(1):53-6. PMID:11731805 doi:10.1038/nsb738
- ↑ Szegedi SS, Castro CC, Koutmos M, Garrow TA. Betaine-homocysteine S-methyltransferase-2 is an S-methylmethionine-homocysteine methyltransferase. J Biol Chem. 2008 Apr 4;283(14):8939-45. doi: 10.1074/jbc.M710449200. Epub 2008, Jan 29. PMID:18230605 doi:http://dx.doi.org/10.1074/jbc.M710449200
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