16051-76-6Relevant articles and documents
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Isbell et al.
, p. 755 (1969)
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Reaction of HppE with substrate analogues: Evidence for carbon-phosphorus bond cleavage by a carbocation rearrangement
Chang, Wei-Chen,Mansoorabadi, Steven O.,Liu, Hung-Wen
supporting information, p. 8153 - 8156 (2013/07/05)
(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 biologically unprecedented 1,2-phosphono migration. In this study, a series of substrate analogues were designed, synthesized, and used as mechanistic probes to study this novel enzymatic transformation. The resulting data, together with insights obtained from density 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 biological C-P bond cleavage.
Stereochemical probe for the mechanism of P-C bond cleavage catalyzed by the Bacillus cereus phosphonoacetaldehyde hydrolase
Lee, Sheng-Lian,Hepburn, Timothy W.,Swartz, William H.,Ammon, Herman L.,Mariano, Patrick S.,Dunaway-Mariano, Debra
, p. 7346 - 7354 (2007/10/02)
The enzyme, the phosphonoacetaldehyde hydrolase (phosphonatase) of Bacillus cereus, catalyzes the conversion of phosphonoacetaldehyde to phosphate and acetaldehyde. Previous studies have shown that phosphonatase labilizes the C-P bond in the substrate by
