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rdf:type |
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lifeskim:mentions |
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pubmed:dateCreated |
2010-6-18
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pubmed:abstractText |
Cholesterol oxidase is an alcohol dehydrogenase/oxidase flavoprotein that catalyzes the dehydrogenation of C(3)-OH of cholesterol. It has two major biotechnological applications, i.e. in the determination of serum (and food) cholesterol levels and as biocatalyst providing valuable intermediates for industrial steroid drug production. Cholesterol oxidases of type I are those containing the FAD cofactor tightly but not covalently bound to the protein moiety, whereas type II members contain covalently bound FAD. This is the first report on the over-expression in Escherichia coli of type II cholesterol oxidase from Brevibacterium sterolicum (BCO).
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pubmed:commentsCorrections |
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-10447682,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-10822008,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-11359791,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-11397813,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-11693912,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-11761328,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-12399041,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-1369073,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-14555654,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-15817448,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-16233128,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-16260759,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-16856877,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-17237971,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-17849088,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-19015844,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-19843167,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-19843168,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-19843169,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-5432063,
http://linkedlifedata.com/resource/pubmed/commentcorrection/20409334-7763933
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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:issn |
1472-6750
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pubmed:author |
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pubmed:issnType |
Electronic
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pubmed:volume |
10
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
33
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pubmed:dateRevised |
2010-9-30
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pubmed:meshHeading |
pubmed-meshheading:20409334-Amino Acid Sequence,
pubmed-meshheading:20409334-Bioreactors,
pubmed-meshheading:20409334-Brevibacterium,
pubmed-meshheading:20409334-Cholesterol Oxidase,
pubmed-meshheading:20409334-Cloning, Molecular,
pubmed-meshheading:20409334-Culture Media,
pubmed-meshheading:20409334-DNA, Complementary,
pubmed-meshheading:20409334-Escherichia coli,
pubmed-meshheading:20409334-Flavin-Adenine Dinucleotide,
pubmed-meshheading:20409334-Molecular Sequence Data,
pubmed-meshheading:20409334-Plasmids,
pubmed-meshheading:20409334-Recombinant Proteins
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pubmed:year |
2010
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pubmed:articleTitle |
Production of recombinant cholesterol oxidase containing covalently bound FAD in Escherichia coli.
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pubmed:affiliation |
Dipartimento di Biotecnologie e Scienze Molecolari, Università degli Studi dell'Insubria via JH Dunant 3, 21100 Varese, Italy.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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