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Literature summary for 1.13.11.72 extracted from

  • Whitteck, J.T.; Cicchillo, R.M.; van der Donk, W.A.
    Hydroperoxylation by hydroxyethylphosphonate dioxygenase (2009), J. Am. Chem. Soc., 131, 16225-16232.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 1.13.11.72

Inhibitors

Inhibitors Comment Organism Structure
Acetylphosphate
-
 Streptomyces viridochromogenes

Organism

Organism UniProt Comment Textmining
Streptomyces viridochromogenes Q5IW40
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
(2R)-hydroxypropylphosphonate + O2
-
 Streptomyces viridochromogenes 2-oxopropylphosphonate + hydroxymethylphosphonate + acetate substrate partitions between conversion to 2-oxopropylphosphonate and hydroxymethylphosphonate ?
1-hydroxy-2,2,2-trifluoroethylphosphonate + O2
-
 Streptomyces viridochromogenes trifluoroacetylphosphonate
-
 ?
1-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes acetylphosphate
-
 ?
2-hydroxyethylphosphonate + O2
-
 Streptomyces viridochromogenes hydroxymethylphosphonate + formate
-
 ?
hydroxymethylphosphonate + O2
-
 Streptomyces viridochromogenes phosphate + formate
-
 ?
additional information results provide strong support for a mechanism that proceeds by hydroperoxylation followed by a Criegee rearrangement with a phosphorus-based migrating group and requires that the O-O bond of molecular oxygen is not cleaved prior to substrate activation. No substrate: O-formyl-hydroxymethylphosphonate, (2S)-hydroxypropylphosphonate Streptomyces viridochromogenes ?
-
 ?

Synonyms

Synonyms Comment Organism
PhdP
-
 Streptomyces viridochromogenes