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Literature summary extracted from

  • Liu, P.; Murakami, K.; Seki, T.; He, X.; Yeung, S.M.; Kuzuyama, T.; Seto, H.; Liu, H.
    Protein purification and function assignment of the epoxidase catalyzing the formation of fosfomycin (2001), J. Am. Chem. Soc., 123, 4619-4620.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.11.1.23
-
 Streptomyces wedmorensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.23 Iron iron-dependent enzyme, one iron per monomer Streptomyces wedmorensis

Molecular Weight [Da]

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

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 * 21210, calculated from sequence Streptomyces wedmorensis

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.23 FAD FMN and FAD greatly enhance production of fosfomycin. The flavin coenzyme is unlikely an integral part of the epoxidase Streptomyces wedmorensis
1.11.1.23 FMN FMN and FAD greatly enhance production of fosfomycin. The flavin coenzyme is unlikely an integral part of the epoxidase Streptomyces wedmorensis