EC Number | Cloned (Comment) | Organism |
---|---|---|
1.13.11.72 | recombinant expression of wild-type and mutant enzymes in Escherichia coli | Streptomyces viridochromogenes |
EC Number | Protein Variants | Comment | Organism |
---|---|---|---|
1.13.11.72 | E176A | site-directed mutagenesis, the mutant enzyme shows similar activity as the wild-type enzyme. Like the wild-type enzyme, the mutant HEPD-E176A produces hydroxymethylphosphonate and formate as its only detectable products upon incubation with Fe(II), hydroxyethylphosphonate, and O2 | Streptomyces viridochromogenes |
EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
---|---|---|---|---|---|---|
1.13.11.72 | additional information | - |
additional information | stopped-flow and multi-turnover steady-state kinetics | Streptomyces viridochromogenes |
EC Number | Metals/Ions | Comment | Organism | Structure |
---|---|---|---|---|
1.13.11.72 | Fe2+ | required for catalysis, the mechanism involves activation of an O-H bond by the ferryl complex | Streptomyces viridochromogenes |
EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | Streptomyces viridochromogenes | - |
hydroxymethylphosphonate + formate | - |
? | |
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | Streptomyces viridochromogenes DSM 40736 | - |
hydroxymethylphosphonate + formate | - |
? |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
1.13.11.72 | Streptomyces viridochromogenes | Q5IW40 | - |
- |
1.13.11.72 | Streptomyces viridochromogenes DSM 40736 | Q5IW40 | - |
- |
EC Number | Purification (Comment) | Organism |
---|---|---|
1.13.11.72 | recombinant wild-type and mutant enzymes from Escherichia coli | Streptomyces viridochromogenes |
EC Number | Reaction | Comment | Organism | Reaction ID |
---|---|---|---|---|
1.13.11.72 | 2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate | the reaction proceeds via a transient iron(IV)-oxo (ferryl) complex, a mechanism that involves activation of an O-H bond by the ferryl complex is proposed. The isotope-sensitive C-H-cleavage step is not primarily rate-limiting for the overall catalytic cycle. The reaction does exhibit a significant 2H-kinetic isotope effect on kcat/Km for O2, which implies reversible formation of the C-H-cleaving intermediate | Streptomyces viridochromogenes |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | - |
Streptomyces viridochromogenes | hydroxymethylphosphonate + formate | - |
? | |
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | the reaction proceeds via a transient iron(IV)-oxo (ferryl) complex, the mechanism involves activation of an O-H bond by the ferryl complex. Maximal accumulation of the intermediate requires both the presence of deuterium in the substrate and, importantly, the use of 2H2O as solvent | Streptomyces viridochromogenes | hydroxymethylphosphonate + formate | - |
? | |
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | - |
Streptomyces viridochromogenes DSM 40736 | hydroxymethylphosphonate + formate | - |
? | |
1.13.11.72 | 2-hydroxyethylphosphonate + O2 | the reaction proceeds via a transient iron(IV)-oxo (ferryl) complex, the mechanism involves activation of an O-H bond by the ferryl complex. Maximal accumulation of the intermediate requires both the presence of deuterium in the substrate and, importantly, the use of 2H2O as solvent | Streptomyces viridochromogenes DSM 40736 | hydroxymethylphosphonate + formate | - |
? |
EC Number | Subunits | Comment | Organism |
---|---|---|---|
1.13.11.72 | ? | x * 30000, recombinant enzyme, SDS-PAGE | Streptomyces viridochromogenes |
EC Number | Synonyms | Comment | Organism |
---|---|---|---|
1.13.11.72 | HEPD | - |
Streptomyces viridochromogenes |
EC Number | General Information | Comment | Organism |
---|---|---|---|
1.13.11.72 | physiological function | 2-hydroxyethylphosphonate dioxygenase (HEPD) cleaves the C1-C2 bond of its substrate to afford hydroxymethylphosphonate on the biosynthetic pathway to the commercial herbicide phosphinothricin | Streptomyces viridochromogenes |