海洋软体动物新型酪氨酸蛋白硫转移酶的分子克隆与同源性建模

Maria S. Avtushenko , Svetlana N. Kovalchuk , Galina N. Likhatskaya , Tatyana N. Zvyagintseva , Thomas Haertlé
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引用次数: 0

摘要

酪氨酸蛋白硫转移酶基因是在哺乳动物中发现的,在海洋软体动物中广泛存在。该基因的高度保守性表明TPST在生物代谢中的功能重要性。对编码TPST的cDNA进行克隆和测序,根据氨基酸序列相似性确定该酶为tyrosylprotein sulfotransferase-2 (TPST-2)。根据人TPST-2催化结构域的晶体结构,构建了锡特卡纳菌TPST催化结构域的推测同源性模型。假设的二聚体结构模型表明,活性位点涉及两个单体,二聚体含有两个活性中心。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
Molecular Cloning and Homology Modeling of Novel Tyrosylprotein Sulfotransferase of Marine Mollusk

The gene of tyrosylprotein sulfotransferase, which was discovered in mammals, has been widely found in marine mollusk Littorina sitkana. High conservation of this gene indicates the functional importance of TPST in the metabolism of the living world. The cDNA encoding TPST in the mollusk was cloned and sequenced, and the enzyme was assigned on the basis of amino acid sequence similarity as tyrosylprotein sulfotransferase-2 (TPST-2). The putative homology model for the catalytic domain of TPST from L. sitkana was constructed according to crystal structure of the catalytic domain of the human TPST-2. The putative model of dimer structure showed that the active site involved two monomers and the dimer contains two active centers.

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