2.1.1.308: cytidylyl-2-hydroxyethylphosphonate methyltransferase
This is an abbreviated version!
For detailed information about cytidylyl-2-hydroxyethylphosphonate methyltransferase, go to the full flat file.
Reaction
2 S-adenosyl-L-methionine + + = + + + +
Synonyms
(S)-2-hydroxyethylphosphonate methylase, 2-hydroxyethylphosphonate methyltransferase, fom3, methyltransferase fom3
ECTree
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Cofactor
Cofactor on EC 2.1.1.308 - cytidylyl-2-hydroxyethylphosphonate methyltransferase
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a B12-derived cofactor. A conserved domain search of the Fom3 sequence shows that it has two conserved domains. The N-terminal domain is identified as a B12-like binding domain, whereas the C-terminal domain shows homology to the radical-SAM protein family, containing three conserved Cys residues that serve as ligands to a [4Fe-4S] cluster
methylcobalamin
proposed mechanism: a 5'-deoxyadenosine radical generated from reductive cleavage of S-adenosyl-L-methionine is used to abstract the hydrogen atom from the C-H bond of the substrate resulting in a substrate radical that reacts with methylcobalamin yielding (S)-2-hydroxypropylphosphonate and cob(II)alamin
a conserved domain search of the Fom3 sequence shows it has two conserved domains. The N-terminal domain is identified as a B12-like binding domain, whereas the C-terminal domain shows homology to the radical-SAM protein family, containing three conserved Cys residues that serve as ligands to a [4Fe-4S] cluster
S-adenosyl-L-methionine
proposed mechanism: a 5'-deoxyadenosine radical generated from reductive cleavage of S-adenosyl-L-methionine is used to abstract the hydrogen atom from the C-H bond of the substrate resulting in a substrate radical that reacts with methylcobalamin yielding (S)-2-hydroxypropylphosphonate and cob(II)alamin