Chang, Wei-chen published the artcileReaction of HppE with Substrate Analogues: Evidence for Carbon-Phosphorus Bond Cleavage by a Carbocation Rearrangement, Recommanded Product: 3,3,3-Trifluoropropan-1-ol, the publication is Journal of the American Chemical Society (2013), 135(22), 8153-8156, database is CAplus and MEDLINE.
(S)-2-Hydroxypropylphosphonic acid ((S)-2-HPP) epoxidase (HppE) is an unusual mononuclear non-heme iron enzyme that catalyzes the oxidative epoxidation of (S)-2-HPP in the biosynthesis of the antibiotic fosfomycin. Recently, HppE has been shown to accept (R)-1-hydroxypropylphosphonic acid as a substrate and convert it to an aldehyde product in a reaction involving a biol. unprecedented 1,2-phosphono migration. In this study, a series of substrate analogs were designed, synthesized, and used as mechanistic probes to study this novel enzymic transformation. The resulting data, together with insights obtained from d. functional theory calculations, are consistent with a mechanism of HppE-catalyzed phosphono group migration that involves the formation of a carbocation intermediate. As such, this reaction represents a new paradigm for biol. C-P bond cleavage.
Journal of the American Chemical Society published new progress about 2240-88-2. 2240-88-2 belongs to alcohols-buliding-blocks, auxiliary class Trifluoromethyl,Fluoride,Aliphatic hydrocarbon chain,Alcohol, name is 3,3,3-Trifluoropropan-1-ol, and the molecular formula is C3H5F3O, Recommanded Product: 3,3,3-Trifluoropropan-1-ol.
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