Source:http://linkedlifedata.com/resource/pubmed/id/19843168
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
23
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pubmed:dateCreated |
2010-1-12
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pubmed:abstractText |
An important aspect of catalysis performed by cholesterol oxidase (3beta-hydroxysteroid oxidase) concerns the nature of its association with the lipid bilayer that contains the sterol substrate. Efficient catalytic turnover is affected by the association of the protein with the membrane as well as the solubility of the substrate in the lipid bilayer. In this review, the binding of cholesterol oxidase to the lipid bilayer, its turnover of substrates presented in different physical environments, and how these conditions affect substrate specificity, are discussed. The physiological functions of the enzyme in bacterial metabolism, pathogenesis and macrolide biosynthesis are reviewed in this context.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical | |
pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
1742-4658
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:volume |
276
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
6844-56
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pubmed:dateRevised |
2011-8-1
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pubmed:meshHeading |
pubmed-meshheading:19843168-Animals,
pubmed-meshheading:19843168-Binding Sites,
pubmed-meshheading:19843168-Catalysis,
pubmed-meshheading:19843168-Cholesterol Oxidase,
pubmed-meshheading:19843168-Humans,
pubmed-meshheading:19843168-Kinetics,
pubmed-meshheading:19843168-Lipid Bilayers,
pubmed-meshheading:19843168-Models, Molecular,
pubmed-meshheading:19843168-Phylogeny,
pubmed-meshheading:19843168-Protein Conformation,
pubmed-meshheading:19843168-Substrate Specificity
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pubmed:year |
2009
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pubmed:articleTitle |
Cholesterol oxidase: physiological functions.
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pubmed:affiliation |
Laboratory of Biochemistry and Immunology, Department of Biology, Faculty of Sciences, Mohammed V University, Rabat, Morocco.
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pubmed:publicationType |
Journal Article,
Review,
Research Support, Non-U.S. Gov't,
Research Support, N.I.H., Extramural
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