Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2007-11-26
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jan
pubmed:issn
1090-2104
pubmed:author
pubmed:issnType
Electronic
pubmed:day
11
pubmed:volume
365
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
340-3
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Conserved amino acid sequences in the bacterial sialyltransferases belonging to Glycosyltransferase family 80.
pubmed:affiliation
Glycotechnology Business Unit, Japan Tobacco Inc., 700 Higashibara, Iwata, Shizuoka 438-0802, Japan. takeshi.yamamoto@ims.jti.co.jp
pubmed:publicationType
Journal Article