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. 2018 Aug 1;10(4):371-373.
doi: 10.1093/jmcb/mjy010.

Jumonji domain-containing protein family: the functions beyond lysine demethylation

Yuan Meng  1 , Hongzhi Li  2 , Changwei Liu  1 , Li Zheng  1 , Binghui Shen  1
Affiliations

Jumonji domain-containing protein family: the functions beyond lysine demethylation

Yuan Meng et al. J Mol Cell Biol. .
No abstract available

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Figures

Figure 1
Figure 1
Structure similarity, biochemical activities, and catalytic mechanism of JmjC domain-containing protein family. (A) 3D structure depicting the polypeptide backbone of the JmjC domain of JMJD5 (PDB 4gjy) and residues required for iron binding. (B) Structural similarity heatmap for JmjC proteins based on TM-score. The maximum TM-score is used to compare protein structure similarity. (C) Biochemical activities of JmjC proteins. +, oxygenase activity has been detected. (D) Schematics showing the catalytic mechanism of lysine/arginine demethylation mediated by JmjC proteins, including the steps for hydroxylation of the C–H bond and N-methyl group demethylation, via C-hydroxylation, followed by the fragmentation of a hemiaminal intermediate.
See this image and copyright information in PMC

References

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