Source:http://linkedlifedata.com/resource/pubmed/id/17997982
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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2007-11-26
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pubmed:abstractText |
Sialyltransferases are key enzymes for the biosynthesis of sialyl-glycoproteins and sialyl-lipids and the genes encoding sialyltransferases have been cloned from mammalian and bacterial source. In the mammalian sialyltransferase, existence of three conserved regions, named sialyl motifs, has been demonstrated. On the other hand, two short motifs, named D/E-D/E-G motif and HP motif, have been reported in the bacterial sialyltransferases very recently. From the results of multiple alignments among the sialyltransferases belonging to Glycosyltransferase family 80 and crystal structures of two reported sialyltransferases, it is clearly demonstrated that the third conserved-functional motif exists in the bacterial sialyltransferases that have been classified into Glycosyltransferase family 80 in this study.
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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 |
Jan
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pubmed:issn |
1090-2104
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pubmed:author | |
pubmed:issnType |
Electronic
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pubmed:day |
11
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pubmed:volume |
365
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
340-3
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pubmed:meshHeading |
pubmed-meshheading:17997982-Amino Acid Sequence,
pubmed-meshheading:17997982-Bacterial Proteins,
pubmed-meshheading:17997982-Conserved Sequence,
pubmed-meshheading:17997982-Glycosyltransferases,
pubmed-meshheading:17997982-Molecular Sequence Data,
pubmed-meshheading:17997982-Sequence Analysis, Protein,
pubmed-meshheading:17997982-Sequence Homology, Amino Acid,
pubmed-meshheading:17997982-Sialyltransferases,
pubmed-meshheading:17997982-Vibrionaceae
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pubmed:year |
2008
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pubmed:articleTitle |
Conserved amino acid sequences in the bacterial sialyltransferases belonging to Glycosyltransferase family 80.
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pubmed:affiliation |
Glycotechnology Business Unit, Japan Tobacco Inc., 700 Higashibara, Iwata, Shizuoka 438-0802, Japan. takeshi.yamamoto@ims.jti.co.jp
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pubmed:publicationType |
Journal Article
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