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ENZYME entry: EC

Accepted Name
Cytidylyl-2-hydroxyethylphosphonate methyltransferase.
Reaction catalysed
2 S-adenosyl-L-methionine + cytidine 5'-((hydroxy(2-hydroxyethyl)phosphonoyl)phosphate) + reduced acceptor <=> S-adenosyl-L-homocysteine + 5'-deoxyadenosine + L-methionine + cytidine 5'-((hydroxy(2-hydroxypropyl)phosphonoyl)phosphate) + oxidized acceptor
  • 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 catalyze another cycle.
PRIAM enzyme-specific profiles2.1.1.308
KEGG Ligand Database for Enzyme Nomenclature2.1.1.308
IUBMB Enzyme Nomenclature2.1.1.308
MEDLINEFind literature relating to
Rhea expert-curated reactions2.1.1.308
Q56184, FOM3_STRWE

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