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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
45
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pubmed:dateCreated |
1998-12-10
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pubmed:databankReference | |
pubmed:abstractText |
A novel putative member of the human UDP-galactose:beta-N-acetylglucosamine beta1,4-galactosyltransferase family, designated beta4Gal-T4, was identified by BLAST analysis of expressed sequence tags. The sequence of beta4Gal-T4 encoded a type II membrane protein with significant sequence similarity to other beta1,4-galactosyltransferases. Expression of the full coding sequence and a secreted form of beta4Gal-T4 in insect cells showed that the gene product had beta1,4-galactosyltransferase activity. Analysis of the substrate specificity of the secreted form revealed that the enzyme catalyzed glycosylation of glycolipids with terminal beta-GlcNAc; however, in contrast to beta4Gal-T1, -T2, and -T3, this enzyme did not transfer galactose to asialo-agalacto-fetuin, asialo-agalacto-transferrin, or ovalbumin. The catalytic activity of beta4Gal-T4 with monosaccharide acceptor substrates, N-acetylglucosamine as well as glucose, was markedly activated in the presence of alpha-lactalbumin. The genomic organization of the coding region of beta4Gal-T4 was contained in six exons. All intron/exon boundaries were similarly positioned in beta4Gal-T1, -T2, and -T3. beta4Gal-T4 represents a new member of the beta4-galactosyltransferase family. Its kinetic parameters suggest unique functions in the synthesis of neolactoseries glycosphingolipids.
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pubmed:grant | |
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 |
Nov
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
6
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pubmed:volume |
273
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
29331-40
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:9792633-Amino Acid Sequence,
pubmed-meshheading:9792633-Base Sequence,
pubmed-meshheading:9792633-Chromosome Mapping,
pubmed-meshheading:9792633-Cloning, Molecular,
pubmed-meshheading:9792633-DNA, Complementary,
pubmed-meshheading:9792633-Glycosphingolipids,
pubmed-meshheading:9792633-Humans,
pubmed-meshheading:9792633-Magnetic Resonance Spectroscopy,
pubmed-meshheading:9792633-Molecular Sequence Data,
pubmed-meshheading:9792633-N-Acetyllactosamine Synthase,
pubmed-meshheading:9792633-Protein Conformation,
pubmed-meshheading:9792633-Sequence Homology, Amino Acid
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pubmed:year |
1998
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pubmed:articleTitle |
Cloning of a novel member of the UDP-galactose:beta-N-acetylglucosamine beta1,4-galactosyltransferase family, beta4Gal-T4, involved in glycosphingolipid biosynthesis.
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pubmed:affiliation |
School of Dentistry, University of Copenhagen, Norre Allé 20, 2200 Copenhagen N, Denmark.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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