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rdf:type |
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lifeskim:mentions |
umls-concept:C0004083,
umls-concept:C0008109,
umls-concept:C0033684,
umls-concept:C0085470,
umls-concept:C0087684,
umls-concept:C0205314,
umls-concept:C0441513,
umls-concept:C0596901,
umls-concept:C0596988,
umls-concept:C0678594,
umls-concept:C0679622,
umls-concept:C1527177,
umls-concept:C1527178,
umls-concept:C1749467
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pubmed:issue |
48
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pubmed:dateCreated |
1994-1-6
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pubmed:databankReference |
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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.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0006-2960
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
7
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pubmed:volume |
32
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pubmed:geneSymbol |
gox,
lox,
urf
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12959-67
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pubmed:dateRevised |
2010-10-13
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pubmed:meshHeading |
pubmed-meshheading:8241149-Alcohol Oxidoreductases,
pubmed-meshheading:8241149-Amino Acid Sequence,
pubmed-meshheading:8241149-Bacterial Proteins,
pubmed-meshheading:8241149-Base Sequence,
pubmed-meshheading:8241149-Cell Compartmentation,
pubmed-meshheading:8241149-DNA Mutational Analysis,
pubmed-meshheading:8241149-DNA Primers,
pubmed-meshheading:8241149-Kinetics,
pubmed-meshheading:8241149-Membrane Proteins,
pubmed-meshheading:8241149-Models, Molecular,
pubmed-meshheading:8241149-Molecular Sequence Data,
pubmed-meshheading:8241149-Protein Structure, Tertiary,
pubmed-meshheading:8241149-Pseudomonas putida,
pubmed-meshheading:8241149-Recombinant Fusion Proteins,
pubmed-meshheading:8241149-Sequence Alignment,
pubmed-meshheading:8241149-Sequence Homology, Amino Acid,
pubmed-meshheading:8241149-Spectrum Analysis,
pubmed-meshheading:8241149-Substrate Specificity
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pubmed:year |
1993
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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.
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pubmed:affiliation |
Department of Chemistry and Biochemistry, University of Maryland, College Park 20742.
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pubmed:publicationType |
Journal Article,
Comparative Study,
Research Support, U.S. Gov't, P.H.S.
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