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Literature summary for 1.13.11.73 extracted from

  • Peck, S.C.; van der Donk, W.A.
    Go it alone four-electron oxidations by mononuclear non-heme iron enzymes (2017), J. Biol. Inorg. Chem., 22, 381-394 .
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.11.73

Metals/Ions

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/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
2-hydroxyethylphosphonate + O2 Nitrosopumilus maritimus
-
 methylphosphonate + HCO3-
-
 ir

Organism

Organism UniProt Comment Textmining
Nitrosopumilus maritimus
-
-
-

Reaction

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
a

Substrates and Products (Substrate)

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

Synonyms Comment Organism
methylphosphonate synthase
-
 Nitrosopumilus maritimus
mpnS
-
 Nitrosopumilus maritimus

General Information

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