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Voglmeir, J; Voglauer, R; Wilson, IBH.
(2007): XT-II, the second isoform of human peptide-O-xylosyltransferase, displays enzymatic activity
J BIOL CHEM, 282, 5984-5990; ISSN 0021-9258 FullText FullText_BOKU

Peptide O-xylosyltransferase (EC is the first enzyme required for the generation of chondroitin and heparan sulfate glycosaminoglycan chains of proteoglycans. Cloning of cDNAs has previously shown that, whereas invertebrates, generally have a single xylosyltransferase gene, vertebrate genornes encode two similar proteins, xylosyltransferase I and II (XT-I and XT-II). To date enzymatic activity has only been demonstrated for the human XT-I, Caenorhabditis SQV-6, and Drosojghila OXT isoforms. In the present study, we demonstrate that a soluble form of human XT-II expressed in the xylosyltransferase-deficient pgsA-745 (S745) Chinese hamster ovary cell line is indeed capable of catalyzing the transfer of xylose to a variety of peptide substrates; its enzyme activity was also proven using a Pichia-expressed form of XT-II. Its pH, temperature, and cation dependences are similar to those of XT-I expressed in either mammalian cells or yeast. Our data suggest that XT-I and XT-II are, at least in vitro, functionally identical.
Authors BOKU Wien:
Grillari Regina
Voglmeir Josef
Wilson Iain B.H.
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Find related publications in this database (using NML MeSH Indexing)
Animals -
CHO Cells -
Catalysis -
Cations -
Cloning, Molecular -
Cricetinae -
Cricetulus -
Humans -
Hydrogen-Ion Concentration -
Pentosyltransferases - metabolism
Peptides - metabolism
Protein Isoforms - metabolism
Solubility - metabolism
Temperature - metabolism
Xylose - metabolism

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