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Literature summary extracted from

  • Liu, P.; Liu, A.; Yan, F.; Wolfe, M.D.; Lipscomb, J.D.; Liu, H.W.
    Biochemical and spectroscopic studies on (S)-2-hydroxypropylphosphonic acid epoxidase: a novel mononuclear non-heme iron enzyme (2003), Biochemistry, 42, 11577-11586.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.23 expression in Escherichia coli BL21(DE3) Streptomyces wedmorensis

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.11.1.23 EDTA 10 mM, complete inactivation Streptomyces wedmorensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.23 Iron mononuclear non-heme iron enzyme. Substrate binds near, and perhaps to, the active site Fe2+ and in doing so organizes the center so that effectively one species is present Streptomyces wedmorensis

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
1.11.1.23 21000
-
 4 * 21000, SDS-PAGE Streptomyces wedmorensis
1.11.1.23 21210
-
 4 * 21210, calculated from sequence Streptomyces wedmorensis
1.11.1.23 89000
-
 gel filtration Streptomyces wedmorensis

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.11.1.23 (S)-2-hydroxypropylphosphonic acid + 2 NADH + O2 Streptomyces wedmorensis
-
 cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+ i.e. fosfomycin ?

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.23 Streptomyces wedmorensis Q56185
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.11.1.23
-
 Streptomyces wedmorensis

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.23 (S)-2-hydroxypropylphosphonic acid + 2 NADH + O2
-
 Streptomyces wedmorensis cis-(1R,2S)-epoxypropylphosphonic acid + 2 H2O + 2 NAD+ i.e. fosfomycin ?

Subunits

EC Number Subunits Comment Organism
1.11.1.23 tetramer 4 * 21000, SDS-PAGE Streptomyces wedmorensis
1.11.1.23 tetramer 4 * 21210, calculated from sequence Streptomyces wedmorensis

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.23 FAD FMN or FAD increase level of fosfomycin production. The effect of FMN is slightly better than that of FAD. The flavin coenzyme is not likely to be an integral part of the epoxidase itself, but it may serve as a surrogate for the putative electron mediator in the in vitro assay Streptomyces wedmorensis
1.11.1.23 FMN FMN or FAD increase level of fosfomycin production. The effect of FMN is slightly better than that of FAD. The flavin coenzyme is not likely to be an integral part of the epoxidase itself, but it may serve as a surrogate for the putative electron mediator in the in vitro assay Streptomyces wedmorensis
1.11.1.23 NADH NADH is a necessary component for (S)-2-hydroxypropylphosphonic acid epoxidation and the overall catalysis is a four-electron redox reaction Streptomyces wedmorensis