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Literature summary for 1.11.1.23 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
Search for more literature for 1.11.1.23

Cloned(Commentary)

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

Inhibitors

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

Metals/Ions

Metals/Ions Comment Organism Structure
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]

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

Natural Substrates/ Products (Substrates)

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

Organism UniProt Comment Textmining
Streptomyces wedmorensis Q56185
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Streptomyces wedmorensis

Substrates and Products (Substrate)

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 ?

Subunits

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

Cofactor

Cofactor Comment Organism Structure
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
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
NADH NADH is a necessary component for (S)-2-hydroxypropylphosphonic acid epoxidation and the overall catalysis is a four-electron redox reaction Streptomyces wedmorensis