Metals/Ions | Comment | Organism | Structure |
---|---|---|---|
Fe2+ | a mononuclear non-heme iron-dependent enzyme. MPnS contains iron-binding residues at only the two histidines, raising the specter that either MPnS is a 2-His only enzyme or that the third ligand is not well conserved in the alignment | Nitrosopumilus maritimus |
Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-hydroxyethylphosphonate + O2 | Nitrosopumilus maritimus | - |
methylphosphonate + HCO3- | - |
ir |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Nitrosopumilus maritimus | - |
- |
- |
Reaction | Comment | Organism | Reaction ID |
---|---|---|---|
2-hydroxyethylphosphonate + O2 = methylphosphonate + HCO3- | initial substrate oxidation by a ferric-superoxo-intermediate and a second oxidation by a ferryl species, catalytic mechanism, detailed overview | Nitrosopumilus maritimus |
Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|
2-hydroxyethylphosphonate + O2 | - |
Nitrosopumilus maritimus | methylphosphonate + HCO3- | - |
ir | |
2-hydroxyethylphosphonate + O2 | the pro-(R) hydrogen at C2 of 2-hydroxyethylphosphonate is quantitatively incorporated by enzyme MPnS into methylphosphonate. AN irreversible step involving O2 | Nitrosopumilus maritimus | methylphosphonate + HCO3- | - |
ir |
Synonyms | Comment | Organism |
---|---|---|
methylphosphonate synthase | - |
Nitrosopumilus maritimus |
mpnS | - |
Nitrosopumilus maritimus |
General Information | Comment | Organism |
---|---|---|
evolution | one group of mononuclear non-heme iron-dependent enzymes includes 2-hydroxyethylphosphonate dioxygenase (HEPD, EC 1.13.11.72) and methylphosphonate synthase (MPnS) 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 | Nitrosopumilus maritimus |
additional information | apo MPnS homology modeling using the crystal structure of Cd2+-substituted HEPD, EC 1.13.11.72, in complex with substrate 2-hydroxyethylphosphonate, PDB ID 3GBF | Nitrosopumilus maritimus |