Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 2.1.1.308 extracted from

  • Woodyer, R.D.; Li, G.; Zhao, H.; van der Donk, W.A.
    New insight into the mechanism of methyl transfer during the biosynthesis of fosfomycin (2007), Chem. Commun. (Camb. ), 4, 359-361.
    View publication on PubMed
Search for more literature for 2.1.1.308

Metals/Ions

Metals/Ions Comment Organism Structure
Fe2+ 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 Streptomyces fradiae

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
(2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin Streptomyces fradiae the enzyme is required for fosfomycin production (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin
-
 ?

Organism

Organism UniProt Comment Textmining
Streptomyces fradiae D2SNF5
-
-

Reaction

Reaction Comment Organism Reaction ID
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 proposed mechanism: one electron is transferred from the reduced iron–sulfur cluster to S-adenosyl-L-methionine to form an adenosyl radical and methionine. The adenosyl radical abstracts the pro-R hydrogen atom from C2 of (S)-2-hydroxyethylphosphonate, and the resulting substrate radical reacts with methylcobalamin yielding (S)-2-hydroxypropylphosphonate and cob(II)alamin. The enzyme is then returned to the active state by reduction of the 4Fe4S cluster back to the +1 state and binding of S-adenosyl-L-methionine and methylcobalamin. Alternatively, cob(II)alamin might be reduced to cob(I)alamin and methylated while bound to the enzyme Streptomyces fradiae
a

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin the enzyme is required for fosfomycin production Streptomyces fradiae (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin
-
 ?
(2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin no activity with (R)-2-hydroxyethylphosphonate Streptomyces fradiae (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin
-
 ?

Synonyms

Synonyms Comment Organism
fom3
-
 Streptomyces fradiae
methyltransferase fom3
-
 Streptomyces fradiae

Cofactor

Cofactor Comment Organism Structure
methylcobalamin 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 Streptomyces fradiae
S-adenosyl-L-methionine 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 Streptomyces fradiae