pubmed-article:12835264 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:12835264 | lifeskim:mentions | umls-concept:C0015576 | lld:lifeskim |
pubmed-article:12835264 | lifeskim:mentions | umls-concept:C0680022 | lld:lifeskim |
pubmed-article:12835264 | lifeskim:mentions | umls-concept:C0030016 | lld:lifeskim |
pubmed-article:12835264 | lifeskim:mentions | umls-concept:C0205396 | lld:lifeskim |
pubmed-article:12835264 | lifeskim:mentions | umls-concept:C0072653 | lld:lifeskim |
pubmed-article:12835264 | pubmed:issue | 10 | lld:pubmed |
pubmed-article:12835264 | pubmed:dateCreated | 2003-7-1 | lld:pubmed |
pubmed-article:12835264 | pubmed:abstractText | Fungal pyranose oxidase is a flavoenzyme whose preferred substrate among several monosaccharides is D-glucose. After a comprehensive analysis of conserved features in a structure-based multiple sequence alignment of homologous proteins, we could classify this enzyme into the GMC oxidoreductase family. The identified homology also suggests a three-dimensional protein structure similar to the functionally related glucose oxidase. | lld:pubmed |
pubmed-article:12835264 | pubmed:language | eng | lld:pubmed |
pubmed-article:12835264 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12835264 | pubmed:citationSubset | IM | lld:pubmed |
pubmed-article:12835264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12835264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12835264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12835264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12835264 | pubmed:chemical | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:12835264 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:12835264 | pubmed:month | Jul | lld:pubmed |
pubmed-article:12835264 | pubmed:issn | 1367-4803 | lld:pubmed |
pubmed-article:12835264 | pubmed:author | pubmed-author:LengauerThoma... | lld:pubmed |
pubmed-article:12835264 | pubmed:author | pubmed-author:AlbrechtMario... | lld:pubmed |
pubmed-article:12835264 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:12835264 | pubmed:day | 1 | lld:pubmed |
pubmed-article:12835264 | pubmed:volume | 19 | lld:pubmed |
pubmed-article:12835264 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:12835264 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:12835264 | pubmed:pagination | 1216-20 | lld:pubmed |
pubmed-article:12835264 | pubmed:dateRevised | 2006-11-15 | lld:pubmed |
pubmed-article:12835264 | pubmed:meshHeading | pubmed-meshheading:12835264... | lld:pubmed |
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pubmed-article:12835264 | pubmed:meshHeading | pubmed-meshheading:12835264... | lld:pubmed |
pubmed-article:12835264 | pubmed:meshHeading | pubmed-meshheading:12835264... | lld:pubmed |
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pubmed-article:12835264 | pubmed:meshHeading | pubmed-meshheading:12835264... | lld:pubmed |
pubmed-article:12835264 | pubmed:year | 2003 | lld:pubmed |
pubmed-article:12835264 | pubmed:articleTitle | Pyranose oxidase identified as a member of the GMC oxidoreductase family. | lld:pubmed |
pubmed-article:12835264 | pubmed:affiliation | Max-Planck-Institute for Informatics, Stuhlsatzenhausweg 85, 66123 Saarbrücken, Germany. mario.albrecht@mpi-sb.mpg.de | lld:pubmed |
pubmed-article:12835264 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:12835264 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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