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Selected Publication:

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

Abstract:
Peptide O-xylosyltransferase (EC 2.4.2.26) 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.
BOKU Gendermonitor:

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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