Methionine synthase

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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.
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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<ref>DOI: 10.1038/nsb738</ref>.
</StructureSection>
</StructureSection>
== Vitamin B-12 ==
== Vitamin B-12 ==
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== Relevance ==
== Relevance ==
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Methionine deficiency can result in diseases such as birth abnormalities.
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Methionine deficiency can result in diseases such as birth abnormalities<ref>DOI: 10.1038/nature10916</ref>.
== References ==
== References ==
<ref>DOI: 10.1128/JB.00208-06</ref>
<ref>DOI: 10.1128/JB.00208-06</ref>
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<references/>
<references/>

Revision as of 18:40, 5 April 2022

Contents

Methionine synthase

B-12 dependent fragment of E. coli methionine synthase with Cobalt (in pink)

Drag the structure with the mouse to rotate

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[2].

References

[3]

  1. 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
  2. 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
  3. 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

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