Crystallization (Comment) | Organism |
---|---|
in vitro reconstitution of activity and determination of the crystal structure of Cd2+-substituted PhpD in complex with the 2-hydroxyethylphosphonate substrate | Streptomyces viridochromogenes |
Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | a mononuclear non-heme iron-dependent enzyme | Streptomyces viridochromogenes |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-hydroxyethylphosphonate + O2 | Streptomyces viridochromogenes | - |
hydroxymethylphosphonate + formate | - |
ir | |
2-hydroxyethylphosphonate + O2 | Streptomyces viridochromogenes DSM 40736 | - |
hydroxymethylphosphonate + formate | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Streptomyces viridochromogenes | Q5IW40 | - |
- |
Streptomyces viridochromogenes DSM 40736 | Q5IW40 | - |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2-hydroxyethylphosphonate + O2 = hydroxymethylphosphonate + formate | initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species, catalytic mechanism, detailed overview | Streptomyces viridochromogenes |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-hydroxyethylphosphonate + O2 | - |
Streptomyces viridochromogenes | hydroxymethylphosphonate + formate | - |
ir | |
2-hydroxyethylphosphonate + O2 | an irreversible step involving O2 | Streptomyces viridochromogenes | hydroxymethylphosphonate + formate | - |
ir | |
2-hydroxyethylphosphonate + O2 | - |
Streptomyces viridochromogenes DSM 40736 | hydroxymethylphosphonate + formate | - |
ir | |
2-hydroxyethylphosphonate + O2 | an irreversible step involving O2 | Streptomyces viridochromogenes DSM 40736 | hydroxymethylphosphonate + formate | - |
ir | |
additional information | HEPD oxidizes a relatively unactivated substrate that cannot easily facilitate O2 activation. 2-Hydroxyethylphosphonate does not contain a thiol group that upon binding to the iron can activate it for catalysis, nor does it contain an 2-oxo acid functionality | Streptomyces viridochromogenes | ? | - |
? | |
additional information | HEPD oxidizes a relatively unactivated substrate that cannot easily facilitate O2 activation. 2-Hydroxyethylphosphonate does not contain a thiol group that upon binding to the iron can activate it for catalysis, nor does it contain an 2-oxo acid functionality | Streptomyces viridochromogenes DSM 40736 | ? | - |
? |
Synonyms | Comment | Organism |
---|---|---|
HEPD | - |
Streptomyces viridochromogenes |
phpD | - |
Streptomyces viridochromogenes |
General Information | Comment | Organism |
---|---|---|
evolution | one group of mononuclear non-heme iron-dependent enzymes includes 2-hydroxyethylphosphonate dioxygenase (HEPD) and methylphosphonate synthase (MPnS, EC 1.13.11.73) that both carry out the oxidative cleavage of the carbon-carbon bond of 2-hydroxyethylphosphonate but generate different products. Common properties include the initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species. Sequence homology between HEPD and MPnS combined with identical requirements for catalysis suggests a consensus mechanism in which product identity is determined by branching at an intermediate in the catalytic cycle | Streptomyces viridochromogenes |
additional information | the active site metal is coordinated by 2-His-1-Glu on one face of a pseudooctrahedron | Streptomyces viridochromogenes |