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Literature summary extracted from

  • McLuskey, K.; Cameron, S.; Hammerschmidt, F.; Hunter, W.N.
    Structure and reactivity of hydroxypropylphosphonic acid epoxidase in fosfomycin biosynthesis by a cation- and flavin-dependent mechanism (2005), Proc. Natl. Acad. Sci. USA, 102, 14221-14226.
    View publication on PubMedView publication on EuropePMC

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.11.1.23 crystal structures of holoenzyme and the complex with fosfomycin are determined and reveal a two-domain combination and Zn2+ in the active site Streptomyces wedmorensis

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.11.1.23 Fe2+ the recombinant enzyme is active, when reconstituted with Zn2+ or Fe2+ Streptomyces wedmorensis
1.11.1.23 Zn2+ the recombinant enzyme is active, when reconstituted with Zn2+ or Fe2+ 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

Reaction

EC Number Reaction Comment Organism Reaction ID
1.11.1.23 (S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O a straightforward epoxidase mechanism is proposed that depends on the Lewis acid properties of divalent cations and the redox properties of FMN Streptomyces wedmorensis
a

Synonyms

EC Number Synonyms Comment Organism
1.11.1.23 HppE
-
 Streptomyces wedmorensis

Cofactor

EC Number Cofactor Comment Organism Structure
1.11.1.23 FMN a straightforward epoxidase mechanism is proposed that depends on the Lewis acid properties of divalent cations and the redox properties of FMN Streptomyces wedmorensis