1.11.1.23: (S)-2-hydroxypropylphosphonic acid epoxidase
This is an abbreviated version!
For detailed information about (S)-2-hydroxypropylphosphonic acid epoxidase, go to the full flat file.
Reaction
Synonyms
(S)-2-HPP epoxidase, (S)-2-hydroxypropylphosphonate epoxidase, (S)-2-hydroxypropylphosphonic acid epoxidase, (S-HPP) epoxidase, 2-hydroxypropylphosphonic acid epoxidase, EC 1.14.19.7, fom4, fosfomycin-producing epoxidase, HPP epoxidase, HppE, Ps-HppE
ECTree
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Metals Ions
Metals Ions on EC 1.11.1.23 - (S)-2-hydroxypropylphosphonic acid epoxidase
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Fe2+
Iron
Zn2+
the recombinant enzyme is active, when reconstituted with Zn2+ or Fe2+
Fe2+
Fe2+ is the only metal ion that is effective to reconstitute HppE activity. Zn2+ cannot replace Fe2+ in the HppE reaction
Fe2+
the recombinant enzyme is active, when reconstituted with Zn2+ or Fe2+
-
mononuclear non-heme iron-containing enzyme. Contains about one iron per monomer. Substrate and NO can bind to the ferrous center of the reduced HppE enzyme to form a stable complex
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
Iron
O2 binds to the iron, and substrates bind in a single orientation that strongly perturbs the iron environment. Both functional groups of (S)-2-hydroxypropylphosphonic acid bind to Fe(II) ion at the same time as NO, suggesting that the chelated substrate binding mode dominates in solution. The Fe(II)-substrate chelate structure is important to active fosfomycin formation. This fixed orientation may align the substrate next to the iron-bound activated oxygen species thought to mediate hydrogen atom abstraction from the nearest substrate carbon