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Literature summary extracted from

  • Booker, S.J.
    Anaerobic functionalization of unactivated C-H bonds (2009), Curr. Opin. Chem. Biol., 13, 58-73.
    View publication on PubMedView publication on EuropePMC

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2.1.1.308 (2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin Streptomyces fradiae Fom3 catalyzes the penultimate step in the biosynthesis of fosfomycin, an antibiotic produced by several species of Streptomyces and Pseudomonas (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin
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Organism

EC Number Organism UniProt Comment Textmining
2.1.1.308 Streptomyces fradiae D2SNF5
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Reaction

EC Number Reaction Comment Organism Reaction ID
2.1.1.308 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: 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 Streptomyces fradiae

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.1.1.308 (2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin Fom3 catalyzes the penultimate step in the biosynthesis of fosfomycin, an antibiotic produced by several species of Streptomyces and Pseudomonas Streptomyces fradiae (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin
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2.1.1.308 (2-hydroxyethyl)phosphonate + S-adenosyl-L-methionine + methylcobalamin C-2 methylation of hydroxyethyl phosphonate Streptomyces fradiae (S)-2-hydroxypropylphosphonate + L-methionine + 5'-deoxyadenosine + cob(II)alamin
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Synonyms

EC Number Synonyms Comment Organism
2.1.1.308 fom3
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Streptomyces fradiae

Cofactor

EC Number Cofactor Comment Organism Structure
2.1.1.308 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 Streptomyces fradiae
2.1.1.308 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 Streptomyces fradiae