EC Number |
Reaction |
Reference |
---|
1.11.1.23 | (S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O |
- |
- |
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 |
706480 |
1.11.1.23 | (S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O |
an iron-redox mechanism is proposed in which the active site bound Fe2+ serves as a Lewis acid to activate the 2-OH group of (S)-2-hydroxypropylphosphonic acid, and the epoxide ring is formed by the attack of the 2-OH group at C-1 coupled with the transfer of the C-1 hydrogen as a hydride ion to the bound FMN |
702208 |
1.11.1.23 | (S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O |
electron transfer is presumed to be the predominant rate-limiting step. Proposed mechanism: the reaction likely begins with hydrogen atom abstraction from the C-1 position by an activated oxygen species. The C-1 centered radical intermediate can then cyclize to form fosfomycin and the reduced iron center |
702244 |
1.11.1.23 | (S)-2-hydroxypropylphosphonate + H2O2 = (1R,2S)-1,2-epoxypropylphosphonate + 2 H2O |
Tyr105 is a key residue, which plays a role in the activation of dioxygen required for the enzymatic activity of HppE |
704157 |