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ENZYME entry: EC

Accepted Name
cytidylyl-2-hydroxyethylphosphonate methyltransferase
Reaction catalysed
AH2 + cytidine 5'-{[hydroxy(2-hydroxyethyl)phosphonoyl]phosphate} + 2 S-adenosyl-L-methionine <=> 5'-deoxyadenosine + A + cytidine 5'-({hydroxy[(S)-2-hydroxypropyl]phosphonoyl}phosphate) + 2 H(+) + L-methionine + S-adenosyl-L-homocysteine
  • 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 with inversion of configuration to produce the (S)-isomer of the methylated product 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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