Dierks Thomas, Schmidt Bernhard, Borissenko Ljudmila V, Peng Jianhe, Preusser Andrea, Mariappan Malaiyalam, von Figura Kurt
Biochemie II, Universität Göttingen, Germany.
Cell. 2003 May 16;113(4):435-44. doi: 10.1016/s0092-8674(03)00347-7.
C(alpha)-formylglycine (FGly) is the catalytic residue in the active site of eukaryotic sulfatases. It is posttranslationally generated from a cysteine in the endoplasmic reticulum. The genetic defect of FGly formation causes multiple sulfatase deficiency (MSD), a lysosomal storage disorder. We purified the FGly generating enzyme (FGE) and identified its gene and nine mutations in seven MSD patients. In patient fibroblasts, the activity of sulfatases is partially restored by transduction of FGE encoding cDNA, but not by cDNA carrying an MSD mutation. The gene encoding FGE is highly conserved among pro- and eukaryotes and has a paralog of unknown function in vertebrates. FGE is localized in the endoplasmic reticulum and is predicted to have a tripartite domain structure.
α-甲酰甘氨酸(FGly)是真核生物硫酸酯酶活性位点的催化残基。它是在内质网中由半胱氨酸经翻译后修饰产生的。FGly形成的遗传缺陷会导致多种硫酸酯酶缺乏症(MSD),这是一种溶酶体贮积病。我们纯化了FGly生成酶(FGE),并鉴定了其基因以及7例MSD患者中的9种突变。在患者成纤维细胞中,通过转导编码FGE的cDNA可部分恢复硫酸酯酶的活性,但携带MSD突变的cDNA则不能。编码FGE的基因在原核生物和真核生物中高度保守,并且在脊椎动物中有一个功能未知的旁系同源基因。FGE定位于内质网,预计具有三重结构域结构。