Tags

Type your tag names separated by a space and hit enter

Prochiral sulfoxidation as a probe for flavin-containing monooxygenases.
Methods Mol Biol. 2006; 320:163-72.MM

Abstract

Asymmetric aryl alkyl sulfides (R-S-R') are metabolized by flavin-containing monooxygenase (FMO) and cytochrome P450 enzymes to enantiomerically enriched sulfoxide products (R-SO-R') that are readily analyzed with a host of commercially available chiral stationary phases. Prochiral sulfoxidation of probe compounds based on p-tolyl methyl sulfide is a particularly useful method for discriminating among FMO1, FMO3, and FMO5, because the stereochemistry of the resulting products is isoform dependent, but apparently species independent. If studies are performed with crude tissue microsomal preparations, the cytochrome P450 component must be quenched to unmask catalysis specifically by the FMO component of the tissue. This chapter details experimental protocols for stereochemical analysis of sulfoxides generated from methyl, ethyl, n-propyl, and n-butyl p-tolyl sulfide by purified FMO isoforms and tissue microsomal preparations.

Authors+Show Affiliations

Yeung CK
Department of Medicinal Chemistry, University of Washington, Seattle, USA.
Rettie AE
No affiliation info available

MeSH

Chromatography, High Pressure LiquidMolecular ProbesOxygenasesSpectrophotometry, UltravioletStereoisomerismSulfoxides

Pub Type(s)

Journal Article

Language

eng

PubMed ID

16719389

Citation

Yeung, Catherine K., and Allan E. Rettie. "Prochiral Sulfoxidation as a Probe for Flavin-containing Monooxygenases." Methods in Molecular Biology (Clifton, N.J.), vol. 320, 2006, pp. 163-72.
Yeung CK, Rettie AE. Prochiral sulfoxidation as a probe for flavin-containing monooxygenases. Methods Mol Biol. 2006;320:163-72.
Yeung, C. K., & Rettie, A. E. (2006). Prochiral sulfoxidation as a probe for flavin-containing monooxygenases. Methods in Molecular Biology (Clifton, N.J.), 320, 163-72.
Yeung CK, Rettie AE. Prochiral Sulfoxidation as a Probe for Flavin-containing Monooxygenases. Methods Mol Biol. 2006;320:163-72. PubMed PMID: 16719389.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Prochiral sulfoxidation as a probe for flavin-containing monooxygenases. AU - Yeung,Catherine K, AU - Rettie,Allan E, PY - 2006/5/25/pubmed PY - 2006/6/22/medline PY - 2006/5/25/entrez SP - 163 EP - 72 JF - Methods in molecular biology (Clifton, N.J.) JO - Methods Mol Biol VL - 320 N2 - Asymmetric aryl alkyl sulfides (R-S-R') are metabolized by flavin-containing monooxygenase (FMO) and cytochrome P450 enzymes to enantiomerically enriched sulfoxide products (R-SO-R') that are readily analyzed with a host of commercially available chiral stationary phases. Prochiral sulfoxidation of probe compounds based on p-tolyl methyl sulfide is a particularly useful method for discriminating among FMO1, FMO3, and FMO5, because the stereochemistry of the resulting products is isoform dependent, but apparently species independent. If studies are performed with crude tissue microsomal preparations, the cytochrome P450 component must be quenched to unmask catalysis specifically by the FMO component of the tissue. This chapter details experimental protocols for stereochemical analysis of sulfoxides generated from methyl, ethyl, n-propyl, and n-butyl p-tolyl sulfide by purified FMO isoforms and tissue microsomal preparations. SN - 1064-3745 UR - https://www.unboundmedicine.com/medline/citation/16719389/Prochiral_sulfoxidation_as_a_probe_for_flavin_containing_monooxygenases_ DB - PRIME DP - Unbound Medicine ER -