| pubmed-article:18406355 | rdf:type | pubmed:Citation | lld:pubmed |
| pubmed-article:18406355 | lifeskim:mentions | umls-concept:C0014628 | lld:lifeskim |
| pubmed-article:18406355 | lifeskim:mentions | umls-concept:C1522492 | lld:lifeskim |
| pubmed-article:18406355 | lifeskim:mentions | umls-concept:C0971871 | lld:lifeskim |
| pubmed-article:18406355 | pubmed:issue | 11 | lld:pubmed |
| pubmed-article:18406355 | pubmed:dateCreated | 2008-5-9 | lld:pubmed |
| pubmed-article:18406355 | pubmed:abstractText | Epoxide hydrolases catalyze hydrolytic epoxide ring-opening, most often via formation of a covalent hydroxyalkyl-enzyme intermediate. A mutant of Agrobacterium radiobacter epoxide hydrolase, in which the phenylalanine residue that flanks the invariant catalytic aspartate nucleophile is replaced by a threonine, exhibited inactivation during conversion when the (R)-enantiomer of para-nitrostyrene epoxide was used as substrate. HPLC analysis of tryptic fragments of the epoxide hydrolase, followed by MALDI-TOF and TOF/TOF analysis, indicated that inactivation was due to conversion of the nucleophilic aspartate into isoaspartate, which represents a novel mechanism of catalysis-induced autoinactivation. Inactivation occurred at a lower rate with the (S)-enantiomer of para-nitrostyrene epoxide, indicating that it is related to the structure of the covalent hydroxyalkyl-enzyme intermediate. | lld:pubmed |
| pubmed-article:18406355 | pubmed:language | eng | lld:pubmed |
| pubmed-article:18406355 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18406355 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:18406355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18406355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18406355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18406355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18406355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18406355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18406355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18406355 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:18406355 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:18406355 | pubmed:month | May | lld:pubmed |
| pubmed-article:18406355 | pubmed:issn | 0014-5793 | lld:pubmed |
| pubmed-article:18406355 | pubmed:author | pubmed-author:JanssenDick... | lld:pubmed |
| pubmed-article:18406355 | pubmed:author | pubmed-author:PermentierHja... | lld:pubmed |
| pubmed-article:18406355 | pubmed:author | pubmed-author:van LooBertB | lld:pubmed |
| pubmed-article:18406355 | pubmed:author | pubmed-author:KingmaJaapJ | lld:pubmed |
| pubmed-article:18406355 | pubmed:author | pubmed-author:BaldasciniHel... | lld:pubmed |
| pubmed-article:18406355 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:18406355 | pubmed:day | 14 | lld:pubmed |
| pubmed-article:18406355 | pubmed:volume | 582 | lld:pubmed |
| pubmed-article:18406355 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:18406355 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:18406355 | pubmed:pagination | 1581-6 | lld:pubmed |
| pubmed-article:18406355 | pubmed:dateRevised | 2011-11-17 | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:meshHeading | pubmed-meshheading:18406355... | lld:pubmed |
| pubmed-article:18406355 | pubmed:year | 2008 | lld:pubmed |
| pubmed-article:18406355 | pubmed:articleTitle | Inactivation of epoxide hydrolase by catalysis-induced formation of isoaspartate. | lld:pubmed |
| pubmed-article:18406355 | pubmed:affiliation | Biochemical Laboratory, Groningen Biomolecular Sciences and Biotechnology Institute, University of Groningen, Nijenborgh 4, 9747 AG Groningen, The Netherlands. | lld:pubmed |
| pubmed-article:18406355 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:18406355 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
| http://linkedlifedata.com/r... | entrezgene:pubmed | pubmed-article:18406355 | lld:entrezgene |
