A SINGLE PROTEIN CATALYZES BOTH N-DEACETYLATION AND N-SULFATION DURING THE BIOSYNTHESIS OF HEPARAN-SULFATE
A SINGLE PROTEIN CATALYZES BOTH N-DEACETYLATION AND N-SULFATION DURING THE BIOSYNTHESIS OF HEPARAN-SULFATE
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DOI：
10.1073/pnas.90.9.3885
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发表时间：
1993-05-01
影响因子：
11.1
通讯作者：
HIRSCHBERG, CB
中科院分区：
文献类型：
--
作者：
WEI, Z;SWIEDLER, SJ;HIRSCHBERG, CB
硫酸乙酰肝素是一种高度硫酸化的碳水化合物聚合物，可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取决于一系列修饰多糖骨架的生物合成反应;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一个单一的蛋白质，具有N-脱乙酰酶和N-磺基转移酶的活动。这是通过证明两种活性都存在于含有酶的高尔基体-内腔部分的纯化的可溶性融合蛋白中来实现的。我们建议将该蛋白质重新命名为大鼠肝脏高尔基硫酸乙酰肝素N-脱乙酰基酶/N-磺基转移酶。
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.