| pubmed-article:14976351 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:14976351 | lifeskim:mentions | umls-concept:C0014442 | lld:lifeskim |
| pubmed-article:14976351 | lifeskim:mentions | umls-concept:C0043335 | lld:lifeskim |
| pubmed-article:14976351 | lifeskim:mentions | umls-concept:C0205419 | lld:lifeskim |
| pubmed-article:14976351 | lifeskim:mentions | umls-concept:C1414643 | lld:lifeskim |
| pubmed-article:14976351 | lifeskim:mentions | umls-concept:C0220825 | lld:lifeskim |
| pubmed-article:14976351 | pubmed:issue | 2 | lld:pubmed |
| pubmed-article:14976351 | pubmed:dateCreated | 2004-4-9 | lld:pubmed |
| pubmed-article:14976351 | pubmed:abstractText | The flavin-containing monooxygenase gene family (FMO1-6) in humans encodes five functional isoforms that catalyze the monooxygenation of numerous N-, P- and S-containing drugs and toxicants. A previous single nucleotide polymorphism (SNP) analysis of FMO1 in African-Americans identified seven novel SNPs. To determine the functional relevance of the coding FMO1 variants (H97Q, I303V, I303T, R502X), they were heterologously expressed using a baculovirus system. Catalytic efficiency and stereoselectivity of N- and S-oxygenation was determined in the FMO1 variants using several substrates. The I303V variant showed catalytic constants equal to wild-type FMO1 for methimazole and methyl p-tolyl sulfide. Catalytic efficiency (V(max)/K(m)) of methyl p-tolyl sulfide oxidation by R502X was unaltered. In contrast, methimazole oxidation by R502X was not detected. Both H97Q and I303T had elevated catalytic efficiency with regards to methyl p-tolyl sulfide (162% and 212%, respectively), but slightly reduced efficiency with regards to methimazole (81% and 78%). All the variants demonstrated the same stereoselectivity for methyl p-tolyl sulfide oxidation as wild-type FMO1. FMO1 also metabolized the commonly used insecticide fenthion to its (+)-sulfoxide, with relatively high catalytic efficiency. FMO3 metabolized fenthion to its sulfoxide at a lower catalytic efficiency than FMO1 (27%) and with less stereoselectivity (74% (+)-sulfoxide). Racemic fenthion sulfoxide was a weaker inhibitor of acetylcholinesterase than its parent compound (IC(50) 0.26 and 0.015 mM, respectively). The (+)- and (-)-sulfoxides were equally potent inhibitors of acetylcholinesterase. These data indicate that all the currently known FMO1 variants are catalytically active, but alterations in kinetic parameters were observed. | lld:pubmed |
| pubmed-article:14976351 | pubmed:language | eng | lld:pubmed |
| pubmed-article:14976351 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976351 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:14976351 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976351 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976351 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14976351 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:14976351 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:14976351 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:14976351 | pubmed:month | Apr | lld:pubmed |
| pubmed-article:14976351 | pubmed:issn | 1096-6080 | lld:pubmed |
| pubmed-article:14976351 | pubmed:author | pubmed-author:SchlenkDaniel... | lld:pubmed |
| pubmed-article:14976351 | pubmed:author | pubmed-author:FurnesBjarteB | lld:pubmed |
| pubmed-article:14976351 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:14976351 | pubmed:volume | 78 | lld:pubmed |
| pubmed-article:14976351 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:14976351 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:14976351 | pubmed:pagination | 196-203 | lld:pubmed |
| pubmed-article:14976351 | pubmed:dateRevised | 2010-9-17 | lld:pubmed |
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| pubmed-article:14976351 | pubmed:meshHeading | pubmed-meshheading:14976351... | lld:pubmed |
| pubmed-article:14976351 | pubmed:year | 2004 | lld:pubmed |
| pubmed-article:14976351 | pubmed:articleTitle | Evaluation of xenobiotic N- and S-oxidation by variant flavin-containing monooxygenase 1 (FMO1) enzymes. | lld:pubmed |
| pubmed-article:14976351 | pubmed:affiliation | Environmental Toxicology Program, University of California, Riverside, California 92521, USA. bfurnes@citrus.ucr.edu | lld:pubmed |
| pubmed-article:14976351 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:14976351 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:14976351 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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