4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB as an oxidative biocatalyst in the synthesis of optically active sulfoxides

doi:10.1016/J.TETASY.2005.11.024

Paper

4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB as an oxidative biocatalyst in the synthesis of optically active sulfoxides

Published Jan 9, 2006 · G. Gonzalo, D. Pazmiño, G. Ottolina

Tetrahedron-asymmetry

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76

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Abstract

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Study Snapshot

Recombinant 4-hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB shows great biocatalytic potential in the synthesis of optically active sulfoxides with excellent enantioselectivity.

PopulationOlder adults (50-71 years)

Sample size24

MethodsObservational

OutcomesBody Mass Index projections

ResultsSocial networks mitigate obesity in older groups.

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Paper

4-Hydroxyacetophenone monooxygenase from Pseudomonas fluorescens ACB as an oxidative biocatalyst in the synthesis of optically active sulfoxides

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References

Oxidations catalyzed by phenylacetone monooxygenase from Thermobifida fusca

Phylacetone monooxygenase from Thermobifida fusca effectively oxidizes various organic sulfides and ketones with excellent enantioselectivity, demonstrating its catalytic potential.

Enzymatic Baeyer–Villiger Oxidation of Benzaldehydes

HAPMO prefers fluorophenol production over benzoic acid formation, suggesting interactions between substrates and enzymes influence the migratory group selection.

Biooxidation of ketones with a cyclobutanone structural motif by recombinant whole-cells expressing 4-hydroxyacetophenone monooxygenase

HAPMO, an enzyme from Pseudomonas fluorescens ACB, exhibits a unique biocatalytic behavior in oxidizing cyclobutanone-containing ketones, with moderate yields and enantiomeric purity.

Identifying determinants of NADPH specificity in Baeyer-Villiger monooxygenases.

The strict NADPH dependency of Baeyer-Villiger monooxygenases is based on recognition of the coenzyme by several basic residues.

A highly enantioselective biocatalytic sulfoxidation by the topsoil bacterium Pseudomonas frederiksbergensis

The topsoil bacterium Pseudomonas frederiksbergensis can produce enantiomeric excess of (S)-sulfoxides from various organic sulfides, with up to 99% enantiomeric excess.

Citations

Expanding the Use of Peroxygenase from Oat Flour in Organic Synthesis: Enantioselective Oxidation of Sulfides

Oat flour-derived peroxygenase shows promise as a biocatalyst for enantioselective oxidation of sulfides to sulfoxides, offering a promising tool in organic synthesis.

Stable Isotope-Guided Metabolomics Reveals Polar-Functionalized Fatty-Acylated RiPPs from Streptomyces.

Solabiomycins show potential as antituberculosis agents due to their antibacterial activity against Gram-positive bacteria, including Mycobacterium tuberculosis H37Rv.

A novel 4-hydroxyacetophenone monooxygenase featuring aromatic substrates preference for enantioselective access to sulfoxides

HAPMO Pf is a promising biocatalyst for the synthesis of aromatic esters and chiral sulfoxides, with high activity toward aromatic ketones and thioethers.

Two enantiocomplementary Baeyer-Villiger monooxygenases newly identified for asymmetric oxyfunctionalization of thioether

Ra BVMO and Am BVMO show potential for asymmetric synthesis of sulfoxides due to their broad substrate spectrum and high catalytic efficiency towards thioanisole.

Enzymatic strategies for asymmetric synthesis

Enzymes offer excellent selectivity in asymmetric synthesis, enabling the production of optically pure chiral compounds at industrial scale.