Linked Life Data

9363434

Source:http://linkedlifedata.com/resource/pubmed/id/9363434

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
7
pubmed:dateCreated
1998-2-10
pubmed:abstractText
As an extension of previous study (de Vries et al., 1995, J. Biol. Chem., 270, 8712-8722) the acceptor specificity of recombinant FucT VI, expressed in insect cells as soluble enzyme, and purified from the growth medium by affinity chromatography, was analyzed toward a broad panel of oligosaccharide and glycoprotein substrates. It was found that FucT VI effectively utilizes any type-2-chain based structure (Gal beta 1-->4GlcNAc-R). Neutral as well as sialylated structures are fucosylated with high efficiency. To identify polar groups on acceptors that function in enzyme binding, deoxygenated substrate analogs were tested as acceptors. FucT VI had an absolute requirement for a hydroxyl at C-6 of galactose in addition to the accepting hydroxyl at C-3. Thus, FucT VI, although different from FucT III, IV, and V in acceptor properties, seems to bind the acceptor in a similar way.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0959-6658
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
921-7
pubmed:dateRevised
2008-8-15
pubmed:meshHeading
pubmed:year
1997
pubmed:articleTitle
Acceptor specificity of GDP-Fuc:Gal beta 1-->4GlcNAc-R alpha 3-fucosyltransferase VI (FucT VI) expressed in insect cells as soluble, secreted enzyme.
pubmed:affiliation
Department of Medical Chemistry, Vrije Universiteit Amsterdam, The Netherlands.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't