Heterologous expression and biochemical characterization of soluble human xylosyltransferase II
作者： Javier Carrera Casanova , Joachim Kuhn , Knut Kleesiek , Christian Götting
DOI: 10.1016/J.BBRC.2007.10.206
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摘要: Abstract Human xylosyltransferase II (EC 2.4.2.26, XT-II) represents an isoform of I (XT-I). Recently, we and others provided first evidence that XT-II is capable initiating the biosynthesis glycosaminoglycan chains in proteoglycans. Here, a soluble form human was expressed yeast Pichia pastoris substrate specificity for various acceptors investigated, pointing to modified bikunin peptide be optimal acceptor (KM = 1.9 μM). Furthermore, biochemical characterization showed this enzyme strongly inhibited by nucleotides glycosaminoglycans. Its temperature optimum, stability, ion dependency were further examined, demonstrating necessity Mg2+ or Mn2+ ions its enzymatic activity. Our data show time XT-I are xylosyltransferases with similar but not identical properties, their potential role modulating cellular proteoglycan pool.
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