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首页> 外文期刊>Achievements in the Life Sciences >Molecular Cloning and Homology Modeling of Novel Tyrosylprotein Sulfotransferase of Marine Mollusk
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Molecular Cloning and Homology Modeling of Novel Tyrosylprotein Sulfotransferase of Marine Mollusk

机译:海洋软体动物新型酪氨酰蛋白质磺基转移酶的分子克隆和同源性建模

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Abstract 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.
机译:摘要在哺乳动物中发现的酪氨酰蛋白质磺基转移酶基因已在海洋软体动物小花小立陶宛中广泛发现。该基因的高度保守性表明{TPST}在生物世界的代谢中具有重要的功能。克隆和编码软体动物中{TPST}的cDNA,并根据与酪氨酸蛋白磺基转移酶2(TPST-2)的氨基酸序列相似性分配酶。根据人TPST-2催化结构域的晶体结构,构建了来自假单胞菌{TPST}催化结构域的推定同源性模型。假定的二聚体结构模型表明活性位点涉及两个单体,而二聚体包含两个活性中心。

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