Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary for 1.11.1.23 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
Search for more literature for 1.11.1.23

Cloned(Commentary)

Cloned (Comment) Organism
-
 Streptomyces wedmorensis

Metals/Ions

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

Molecular Weight [Da]

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

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 * 21210, calculated from sequence Streptomyces wedmorensis

Cofactor

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