Wei Z, Swiedler S J, Ishihara M, Orellana A, Hirschberg C B
Glycomed Inc., Alameda, CA 94501.
Proc Natl Acad Sci U S A. 1993 May 1;90(9):3885-8. doi: 10.1073/pnas.90.9.3885.
Heparan sulfate is a highly sulfated carbohydrate polymer that binds to and modulates the activities of numerous proteins. The formation of these protein-binding domains in heparan sulfate is dependent on a series of biosynthetic reactions that modify the polysaccharide backbone; the initiating and rate-limiting steps of this process are the N-deacetylation and N-sulfation of N-acetylglucosamine residues in the polymer. We now report that in the rat liver, biosynthesis of heparan sulfate utilizes a single protein that possesses both N-deacetylase and N-sulfotransferase activities. This was accomplished by demonstrating that both activities resided in a purified soluble fusion protein containing the Golgi-lumenal portion of the enzyme. We propose that this protein be renamed the rat liver Golgi heparan sulfate N-deacetylase/N-sulfotransferase.
硫酸乙酰肝素是一种高度硫酸化的碳水化合物聚合物，它能与多种蛋白质结合并调节其活性。硫酸乙酰肝素中这些蛋白质结合结构域的形成依赖于一系列修饰多糖主链的生物合成反应；该过程的起始和限速步骤是聚合物中N-乙酰葡糖胺残基的N-脱乙酰化和N-硫酸化。我们现在报告，在大鼠肝脏中，硫酸乙酰肝素的生物合成利用了一种同时具有N-脱乙酰酶和N-硫酸转移酶活性的单一蛋白质。这是通过证明这两种活性都存在于一种纯化的可溶性融合蛋白中来实现的，该融合蛋白包含该酶的高尔基体腔部分。我们建议将这种蛋白质重新命名为大鼠肝脏高尔基体硫酸乙酰肝素N-脱乙酰酶/N-硫酸转移酶。
