Methionine synthase
From Proteopedia
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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. | 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. | ||
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== Structural highlights == | == Structural highlights == | ||
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Methionine synthase (MetH) is a B12-dependent enzyme that methylates homocysteine to regenerate methionine. The <scene name='90/907471/Superposition_1/2'>full structure of MetH</scene> has yet to be determined but we understand it contains 4 domains of B12 cobalamin (in pink), methyltetrahydrofolate (blue), homocysteine (yellow), and SAH (as part of the SAM cycle; in red). Each domain with an important function required for catalytic and reactivation cycles. | Methionine synthase (MetH) is a B12-dependent enzyme that methylates homocysteine to regenerate methionine. The <scene name='90/907471/Superposition_1/2'>full structure of MetH</scene> has yet to be determined but we understand it contains 4 domains of B12 cobalamin (in pink), methyltetrahydrofolate (blue), homocysteine (yellow), and SAH (as part of the SAM cycle; in red). Each domain with an important function required for catalytic and reactivation cycles. | ||
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== Vitamin B-12 == | == Vitamin B-12 == | ||
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Methionine deficiency can result in diseases such as birth abnormalities. | Methionine deficiency can result in diseases such as birth abnormalities. | ||
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== References == | == References == | ||
Revision as of 18:38, 5 April 2022
Contents |
Methionine synthase
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Vitamin B-12
Oxidation States of Cobalamin
Co(I) - active, unstable, high energy
Co(II) - common oxidation state
Relevance
Methionine deficiency can result in diseases such as birth abnormalities.
References
- ↑ Barra L, Fontenelle C, Ermel G, Trautwetter A, Walker GC, Blanco C. Interrelations between glycine betaine catabolism and methionine biosynthesis in Sinorhizobium meliloti strain 102F34. J Bacteriol. 2006 Oct;188(20):7195-204. doi: 10.1128/JB.00208-06. PMID:17015658 doi:http://dx.doi.org/10.1128/JB.00208-06
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Kia Yang, Karsten Theis, Michal Harel, Anna Postnikova, Michael O'Shaughnessy
