%0 Journal Article
%T Review and new insights into the catalytic structural domains of the Fe(ll) and 2-Oxoglutarate families.
%A Yang S
%A Xing J
%A Liu D
%A Song Y
%A Yu H
%A Xu S
%A Zuo Y
%J Int J Biol Macromol
%V 278
%N 0
%D 2024 Aug 15
%M 39153678
%F 8.025
%R 10.1016/j.ijbiomac.2024.134798
%X 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.