| pubmed-article:8241149 | rdf:type | pubmed:Citation | lld:pubmed |
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| pubmed-article:8241149 | lifeskim:mentions | umls-concept:C0033684 | lld:lifeskim |
| pubmed-article:8241149 | lifeskim:mentions | umls-concept:C1749467 | lld:lifeskim |
| pubmed-article:8241149 | lifeskim:mentions | umls-concept:C0596988 | lld:lifeskim |
| pubmed-article:8241149 | lifeskim:mentions | umls-concept:C0004083 | lld:lifeskim |
| pubmed-article:8241149 | lifeskim:mentions | umls-concept:C1527177 | lld:lifeskim |
| pubmed-article:8241149 | lifeskim:mentions | umls-concept:C0678594 | lld:lifeskim |
| pubmed-article:8241149 | lifeskim:mentions | umls-concept:C0441513 | lld:lifeskim |
| pubmed-article:8241149 | lifeskim:mentions | umls-concept:C0679622 | lld:lifeskim |
| pubmed-article:8241149 | lifeskim:mentions | umls-concept:C0205314 | lld:lifeskim |
| pubmed-article:8241149 | lifeskim:mentions | umls-concept:C1527178 | lld:lifeskim |
| pubmed-article:8241149 | lifeskim:mentions | umls-concept:C0087684 | lld:lifeskim |
| pubmed-article:8241149 | pubmed:issue | 48 | lld:pubmed |
| pubmed-article:8241149 | pubmed:dateCreated | 1994-1-6 | lld:pubmed |
| pubmed-article:8241149 | pubmed:databankReference | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8241149 | pubmed:abstractText | The (S)-mandelate dehydrogenase (MDH) from Pseudomonas putida (ATCC 12633) is the only membrane-associated member of a homologous family of FMN-dependent, alpha-hydroxy acid dehydrogenases/oxidases that includes the structurally characterized glycolate oxidase from spinach (GOX). We have correlated the membrane association of MDH to a polypeptide segment in the interior of the primary sequence. This has been accomplished by construction of a chimeric enzyme in which the putative membrane-binding segment in MDH has been deleted and replaced with the corresponding segment from the soluble GOX. The resulting chimera, MDH-GOX, is soluble and retains partial catalytic activity (approximately 1%) using (S)-mandelate as substrate. In contrast, the activities of both the membrane-associated wild-type MDH and the soluble MDH-GOX are nearly the same when (S)-phenyllactate is used as substrate. To the best of our knowledge, this is the first example of a membrane-associated protein in which an internal polypeptide segment anchors the protein to the membrane. | lld:pubmed |
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| pubmed-article:8241149 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8241149 | pubmed:language | eng | lld:pubmed |
| pubmed-article:8241149 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8241149 | pubmed:citationSubset | IM | lld:pubmed |
| pubmed-article:8241149 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8241149 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
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| pubmed-article:8241149 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8241149 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8241149 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8241149 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
| pubmed-article:8241149 | pubmed:status | MEDLINE | lld:pubmed |
| pubmed-article:8241149 | pubmed:month | Dec | lld:pubmed |
| pubmed-article:8241149 | pubmed:issn | 0006-2960 | lld:pubmed |
| pubmed-article:8241149 | pubmed:author | pubmed-author:JosephDD | lld:pubmed |
| pubmed-article:8241149 | pubmed:author | pubmed-author:PetskoG AGA | lld:pubmed |
| pubmed-article:8241149 | pubmed:author | pubmed-author:KenyonG LGL | lld:pubmed |
| pubmed-article:8241149 | pubmed:author | pubmed-author:GerltJ AJA | lld:pubmed |
| pubmed-article:8241149 | pubmed:author | pubmed-author:MitreNN | lld:pubmed |
| pubmed-article:8241149 | pubmed:author | pubmed-author:BabbittP CPC | lld:pubmed |
| pubmed-article:8241149 | pubmed:author | pubmed-author:KooC WCW | lld:pubmed |
| pubmed-article:8241149 | pubmed:issnType | Print | lld:pubmed |
| pubmed-article:8241149 | pubmed:day | 7 | lld:pubmed |
| pubmed-article:8241149 | pubmed:volume | 32 | lld:pubmed |
| pubmed-article:8241149 | pubmed:geneSymbol | lox | lld:pubmed |
| pubmed-article:8241149 | pubmed:geneSymbol | gox | lld:pubmed |
| pubmed-article:8241149 | pubmed:geneSymbol | urf | lld:pubmed |
| pubmed-article:8241149 | pubmed:owner | NLM | lld:pubmed |
| pubmed-article:8241149 | pubmed:authorsComplete | Y | lld:pubmed |
| pubmed-article:8241149 | pubmed:pagination | 12959-67 | lld:pubmed |
| pubmed-article:8241149 | pubmed:dateRevised | 2010-10-13 | lld:pubmed |
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| pubmed-article:8241149 | pubmed:meshHeading | pubmed-meshheading:8241149-... | lld:pubmed |
| pubmed-article:8241149 | pubmed:year | 1993 | lld:pubmed |
| pubmed-article:8241149 | pubmed:articleTitle | A novel structural basis for membrane association of a protein: construction of a chimeric soluble mutant of (S)-mandelate dehydrogenase from Pseudomonas putida. | lld:pubmed |
| pubmed-article:8241149 | pubmed:affiliation | Department of Chemistry and Biochemistry, University of Maryland, College Park 20742. | lld:pubmed |
| pubmed-article:8241149 | pubmed:publicationType | Journal Article | lld:pubmed |
| pubmed-article:8241149 | pubmed:publicationType | Comparative Study | lld:pubmed |
| pubmed-article:8241149 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
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| http://linkedlifedata.com/r... | pubmed:referesTo | pubmed-article:8241149 | lld:pubmed |
