| 英文名 |
2-hydroxyethylphosphonate methyltransferase |
| Example Structure |
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| 别名 |
(S)-2-hydroxyethylphosphonate methylase, fom3, methyltransferase fom3 |
| EC Number |
2.1.1.308 |
| CAS编号 |
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| Comments |
Requires cobalamin. The enzyme, isolated from the bacterium Streptomyces wedmorensis, is involved in fosfomycin biosynthesis. It is a radical S-adenosyl-L-methionine (SAM) enzyme that contains a [4Fe-4S] center and a methylcob(III)alamin cofactor. The enzyme uses two molecues of SAM for the reaction. One molecule forms a 5′-deoxyadenosyl radical, while the other is used to methylate the cobalamin cofactor. The 5′-deoxyadenosyl radical abstracts a hydrogen from the C2 position of cytidine 5′-{[(2-hydroxyethyl)phosphonoyl]phosphate} forming a free radical that reacts with the methyl group on methylcob(III)alamin at the opposite side from SAM and the [4Fe-4S] cluster to produce a racemic mix of methylated products and cob(II)alamin. Both the [4Fe-4S] cluster and the cob(II)alamin need to be reduced by an unknown factor(s) before the enzyme could catalyse another cycle. |
| Cofactor |
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| History |
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| Reactions |
S-adenosyl-L-methionine + methylcob(III)alamin + 2-hydroxyethylphosphonate = 5′-deoxyadenosine + L-methionine + cob(III)alamin + (2S)-2-hydroxypropylphosphonate. |
