| pubmed-article:18474673 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18474673 | lifeskim:mentions | umls-concept:C0025519 | lld:lifeskim |
| pubmed-article:18474673 | lifeskim:mentions | umls-concept:C0006463 | lld:lifeskim |
| pubmed-article:18474673 | lifeskim:mentions | umls-concept:C0010654 | lld:lifeskim |
| pubmed-article:18474673 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
| pubmed-article:18474673 | lifeskim:mentions | umls-concept:C1314939 | lld:lifeskim |
| pubmed-article:18474673 | pubmed:issue | 8 | lld:pubmed |
| pubmed-article:18474673 | pubmed:dateCreated | 2008-7-22 | lld:pubmed |
| pubmed-article:18474673 | pubmed:abstractText | The present work documents the first example of an enzyme-catalyzed beta-elimination of a thioether from a sulfonium cysteine S-conjugate. beta-(S-Tetrahydrothiophenium)-L-alanine (THT-A) is the cysteine S-conjugate of busulfan. THT-A slowly undergoes a nonenzymatic beta-elimination reaction at pH 7.4 and 37 degrees C to yield tetrahydrothiophene, pyruvate, and ammonia. This reaction is accelerated by 1) rat liver, kidney, and brain homogenates, 2) isolated rat liver mitochondria, and 3) pyridoxal 5'-phosphate (PLP). A PLP-dependent enzyme in rat liver cytosol that catalyzes a beta-lyase reaction with THT-A was identified as cystathionine gamma-lyase. This unusual drug metabolism pathway represents an alternate route for intermediates in the mercapturate pathway. | lld:pubmed |
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| pubmed-article:18474673 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18474673 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18474673 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18474673 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:18474673 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18474673 | pubmed:month | Aug | lld:pubmed |
| pubmed-article:18474673 | pubmed:issn | 1521-009X | lld:pubmed |
| pubmed-article:18474673 | pubmed:author | pubmed-author:CooperArthur... | lld:pubmed |
| pubmed-article:18474673 | pubmed:author | pubmed-author:KrasnikovBori... | lld:pubmed |
| pubmed-article:18474673 | pubmed:author | pubmed-author:PetrosWilliam... | lld:pubmed |
| pubmed-article:18474673 | pubmed:author | pubmed-author:PintoJohn TJT | lld:pubmed |
| pubmed-article:18474673 | pubmed:author | pubmed-author:CalleryPatric... | lld:pubmed |
| pubmed-article:18474673 | pubmed:author | pubmed-author:YounisIslam... | lld:pubmed |
| pubmed-article:18474673 | pubmed:author | pubmed-author:NiatsetskayaZ... | lld:pubmed |
| pubmed-article:18474673 | pubmed:issnType | Electronic | lld:pubmed |
| pubmed-article:18474673 | pubmed:volume | 36 | lld:pubmed |
| pubmed-article:18474673 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18474673 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18474673 | pubmed:pagination | 1546-52 | lld:pubmed |
| pubmed-article:18474673 | pubmed:dateRevised | 2009-11-18 | lld:pubmed |
| pubmed-article:18474673 | pubmed:meshHeading | pubmed-meshheading:18474673... | lld:pubmed |
| pubmed-article:18474673 | pubmed:meshHeading | pubmed-meshheading:18474673... | lld:pubmed |
| pubmed-article:18474673 | pubmed:meshHeading | pubmed-meshheading:18474673... | lld:pubmed |
| pubmed-article:18474673 | pubmed:meshHeading | pubmed-meshheading:18474673... | lld:pubmed |
| pubmed-article:18474673 | pubmed:meshHeading | pubmed-meshheading:18474673... | lld:pubmed |
| pubmed-article:18474673 | pubmed:meshHeading | pubmed-meshheading:18474673... | lld:pubmed |
| pubmed-article:18474673 | pubmed:meshHeading | pubmed-meshheading:18474673... | lld:pubmed |
| pubmed-article:18474673 | pubmed:meshHeading | pubmed-meshheading:18474673... | lld:pubmed |
| pubmed-article:18474673 | pubmed:meshHeading | pubmed-meshheading:18474673... | lld:pubmed |
| pubmed-article:18474673 | pubmed:meshHeading | pubmed-meshheading:18474673... | lld:pubmed |
| pubmed-article:18474673 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18474673 | pubmed:articleTitle | Metabolism of the cysteine S-conjugate of busulfan involves a beta-lyase reaction. | lld:pubmed |
| pubmed-article:18474673 | pubmed:affiliation | Department of Biochemistry and Molecular Biology, New York Medical College, Valhalla, New York, USA. | lld:pubmed |
| pubmed-article:18474673 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18474673 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
| pubmed-article:18474673 | pubmed:publicationType | Research Support, N.I.H., Extramural | lld:pubmed |
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