Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Iron | O2 binds to the iron, and substrates bind in a single orientation that strongly perturbs the iron environment. Both functional groups of (S)-2-hydroxypropylphosphonic acid bind to Fe(II) ion at the same time as NO, suggesting that the chelated substrate binding mode dominates in solution. The Fe(II)-substrate chelate structure is important to active fosfomycin formation. This fixed orientation may align the substrate next to the iron-bound activated oxygen species thought to mediate hydrogen atom abstraction from the nearest substrate carbon | Streptomyces wedmorensis |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2 | Streptomyces wedmorensis | - |
cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+ | i.e. fosfomycin | ? |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces wedmorensis | Q56185 | - |
- |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2 | - |
Streptomyces wedmorensis | cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+ | i.e. fosfomycin | ? | |
(S)-2-hydroxypropylphosphonic acid + 2 NADH + O2 | bidentate mode of substrate binding to the active site iron in the solution state is established. The binding of the hydroxyl group of the substrates determines the site of oxidation. Use of (R)-2-hydroxypropylphosphonic acid yields the 2-keto-adduct rather than the epoxide | Streptomyces wedmorensis | cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+ | i.e. fosfomycin | ? |
Synonyms | Comment | Organism |
---|---|---|
fom4 | - |
Streptomyces wedmorensis |
HppE | - |
Streptomyces wedmorensis |