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rdf:type |
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lifeskim:mentions |
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pubmed:issue |
10
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pubmed:dateCreated |
2003-7-1
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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.
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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 |
Jul
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pubmed:issn |
1367-4803
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:day |
1
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pubmed:volume |
19
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
1216-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:12835264-Amino Acid Sequence,
pubmed-meshheading:12835264-Basidiomycota,
pubmed-meshheading:12835264-Carbohydrate Dehydrogenases,
pubmed-meshheading:12835264-Conserved Sequence,
pubmed-meshheading:12835264-Databases, Protein,
pubmed-meshheading:12835264-Fungal Proteins,
pubmed-meshheading:12835264-Glucose Dehydrogenases,
pubmed-meshheading:12835264-Models, Molecular,
pubmed-meshheading:12835264-Molecular Sequence Data,
pubmed-meshheading:12835264-Oxidoreductases,
pubmed-meshheading:12835264-Protein Conformation,
pubmed-meshheading:12835264-Protein Structure, Secondary,
pubmed-meshheading:12835264-Sequence Alignment,
pubmed-meshheading:12835264-Sequence Analysis, Protein,
pubmed-meshheading:12835264-Sequence Homology, Amino Acid,
pubmed-meshheading:12835264-Species Specificity
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pubmed:year |
2003
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pubmed:articleTitle |
Pyranose oxidase identified as a member of the GMC oxidoreductase family.
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pubmed:affiliation |
Max-Planck-Institute for Informatics, Stuhlsatzenhausweg 85, 66123 Saarbrücken, Germany. mario.albrecht@mpi-sb.mpg.de
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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