Linked Life Data

11555621

Source:http://linkedlifedata.com/resource/pubmed/id/11555621

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2001-9-13
pubmed:databankReference
pubmed:abstractText
UDP-GlcNAc:alpha3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I (GnTI; EC 2.4.1.101) is a medial-Golgi enzyme that is essential for the processing of oligomannose to hybrid and complex N-glycans. On the basis of highly conserved sequences obtained from previously cloned mammalian GnTI genes, cDNAs for two closely related GnTI isoenzymes were isolated from a Xenopus laevis ovary cDNA library. As typical for glycosyltransferases, both proteins exhibit a type II transmembrane protein topology with a short N-terminal cytoplasmic tail (4 amino acids); a transmembrane domain of 22 residues; a stem region with a length of 81 (isoenzyme A) and 77 (isoenzyme B) amino acids, respectively; and a catalytic domain consisting of 341 residues. The two proteins differ not only in length but also at 13 (stem) and 18 (catalytic domain) positions, respectively. The overall identity of the catalytic domains of the X. laevis GnTI isoenzymes with their mammalian and plant orthologues ranges from 30% (Nicotiana tabacum) to 67% (humans). Isoenzymes A and B are encoded by two separate genes that were both found to be expressed in all tissues examined, albeit in varying amounts and ratios. On expression of the cDNAs in the baculovirus/insect cell system, both isoenzymes were found to exhibit enzymatic activity. Isoenzyme B is less efficiently folded in vivo and thus appears of lower physiological relevance than isoenzyme A. However, substitution of threonine at position 223 with alanine was sufficient to confer isoenzyme B with properties similar to those observed for isoenzyme A.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
0959-6658
pubmed:author
pubmed:issnType
Print
pubmed:volume
11
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
769-78
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:11555621-Alanine, pubmed-meshheading:11555621-Amino Acid Sequence, pubmed-meshheading:11555621-Amino Acid Substitution, pubmed-meshheading:11555621-Animals, pubmed-meshheading:11555621-Base Sequence, pubmed-meshheading:11555621-Blotting, Northern, pubmed-meshheading:11555621-Blotting, Southern, pubmed-meshheading:11555621-DNA, Complementary, pubmed-meshheading:11555621-DNA Probes, pubmed-meshheading:11555621-Isoenzymes, pubmed-meshheading:11555621-Molecular Sequence Data, pubmed-meshheading:11555621-Mutagenesis, Site-Directed, pubmed-meshheading:11555621-N-Acetylglucosaminyltransferases, pubmed-meshheading:11555621-Recombinant Proteins, pubmed-meshheading:11555621-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:11555621-Sequence Homology, Amino Acid, pubmed-meshheading:11555621-Threonine, pubmed-meshheading:11555621-Xenopus laevis
pubmed:year
2001
pubmed:articleTitle
Tissues of the clawed frog Xenopus laevis contain two closely related forms of UDP-GlcNAc:alpha3-D-mannoside beta-1,2-N-acetylglucosaminyltransferase I.
pubmed:affiliation
Zentrum für Angewandte Genetik, Universität für Bodenkultur Wien, Muthgasse 18, A-1190 Vienna, Austria.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't