pubmed-article:9873599 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:9873599 | lifeskim:mentions | umls-concept:C0008391 | lld:lifeskim |
pubmed-article:9873599 | lifeskim:mentions | umls-concept:C0443286 | lld:lifeskim |
pubmed-article:9873599 | lifeskim:mentions | umls-concept:C0733755 | lld:lifeskim |
pubmed-article:9873599 | pubmed:issue | 19 | lld:pubmed |
pubmed-article:9873599 | pubmed:dateCreated | 1999-2-2 | lld:pubmed |
pubmed-article:9873599 | pubmed:abstractText | Cholesterol oxidase stereospecifically isomerizes cholest-5-en-3-one to cholest-4-en-3-one. When the base catalyst for isomerization, Glu361, is mutated to Asp, the rate of deprotonation of cholest-5-en-3-one is not affected, but protonation of the dienolic intermediate becomes rate-limiting. This may be a consequence of the large distance between the catalytic base and carbon-6 of the intermediate in the mutant enzyme. | lld:pubmed |
pubmed-article:9873599 | pubmed:grant | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873599 | pubmed:language | eng | lld:pubmed |
pubmed-article:9873599 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873599 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:9873599 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873599 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873599 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873599 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873599 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:9873599 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:9873599 | pubmed:month | Oct | lld:pubmed |
pubmed-article:9873599 | pubmed:issn | 0960-894X | lld:pubmed |
pubmed-article:9873599 | pubmed:author | pubmed-author:SampsonN SNS | lld:pubmed |
pubmed-article:9873599 | pubmed:author | pubmed-author:KassI JIJ | lld:pubmed |
pubmed-article:9873599 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:9873599 | pubmed:day | 6 | lld:pubmed |
pubmed-article:9873599 | pubmed:volume | 8 | lld:pubmed |
pubmed-article:9873599 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:9873599 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:9873599 | pubmed:pagination | 2663-8 | lld:pubmed |
pubmed-article:9873599 | pubmed:dateRevised | 2007-11-14 | lld:pubmed |
pubmed-article:9873599 | pubmed:meshHeading | pubmed-meshheading:9873599-... | lld:pubmed |
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pubmed-article:9873599 | pubmed:meshHeading | pubmed-meshheading:9873599-... | lld:pubmed |
pubmed-article:9873599 | pubmed:year | 1998 | lld:pubmed |
pubmed-article:9873599 | pubmed:articleTitle | The importance of GLU361 position in the reaction catalyzed by cholesterol oxidase. | lld:pubmed |
pubmed-article:9873599 | pubmed:affiliation | Department of Chemistry, State University of New York, Stony Brook, NY 11794-3400, USA. | lld:pubmed |
pubmed-article:9873599 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:9873599 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:9873599 | pubmed:publicationType | Research Support, U.S. Gov't, Non-P.H.S. | lld:pubmed |
pubmed-article:9873599 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
http://linkedlifedata.com/r... | http://linkedlifedata.com/r... | pubmed-article:9873599 | lld:chembl |
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