Abstract：
Histone lysine demethylase (KDM), AlkB homolog (ALKBH), and Ten-Eleven Translocation (TET) proteins are members of the 2-Oxoglutarate (2OG) and ferrous iron-dependent oxygenases, each of which harbors a catalytic domain centered on a double-stranded β-helix whose topology restricts the regions directly involved in substrate binding. However, they have different catalytic functions, and the deeply structural biological reasons are not yet clear. In this review, the catalytic domain features of the three protein families are summarized from both sequence and structural perspectives. The construction of the phylogenetic tree and comparison of the structure show ten relatively conserved β-sheets and three key regions with substantial structural differences. We summarize the relationship between three key regions of remarkable differences and the substrate compatibility of the three protein families. This review facilitates research into substrate-selective inhibition and bioengineering by providing new insights into the catalytic domains of KDM, ALKBH, and TET proteins.
摘要：
组蛋白赖氨酸去甲基酶(KDM),AlkB同源物(ALKBH),和10-11易位（TET）蛋白是2-氧戊二酸（2OG）和亚铁依赖性加氧酶的成员，每个都包含一个以双链β螺旋为中心的催化结构域，其拓扑结构限制了直接参与底物结合的区域。然而,它们具有不同的催化功能，深层结构生物学原因尚不清楚。在这次审查中,从序列和结构两方面总结了这三个蛋白家族的催化域特征。系统发育树的构建和结构的比较显示了十个相对保守的β-折叠和三个具有实质性结构差异的关键区域。我们总结了三个显著差异的关键区域与三个蛋白质家族的底物相容性之间的关系。这篇综述通过提供对KDM催化域的新见解，促进了对底物选择性抑制和生物工程的研究。ALKBH,和TET蛋白。
