The Enzyme Database

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EC 1.14.11.68     
Accepted name: [histone H3]-trimethyl-L-lysine27 demethylase
Reaction: a [histone H3]-N6,N6,N6-trimethyl-L-lysine27 + 2 2-oxoglutarate + 2 O2 = a [histone H3]-N6-methyl-L-lysine27 + 2 succinate + 2 formaldehyde + 2 CO2 (overall reaction)
(1a) a [histone H3]-N6,N6,N6-trimethyl-L-lysine27 + 2-oxoglutarate + O2 = a [histone H3]-N6,N6-dimethyl-L-lysine27 + succinate + formaldehyde + CO2
(1b) a [histone H3]-N6,N6-dimethyl-L-lysine27 + 2-oxoglutarate + O2 = a [histone H3]-N6-methyl-L-lysine27 + succinate + formaldehyde + CO2
Other name(s): KDM6A (gene name); KDM6C (gene name); UTX (gene name); UTY (gene name); JMJD3 (gene name)
Systematic name: [histone H3]-N6,N6,N6-trimethyl-L-lysine27,2-oxoglutarate:oxygen oxidoreductase
Comments: Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated L-lysine residues at position 27 of histone H3 (H3K27). The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. They can act on tri- and di-methylated forms, but have no activity with the mono-methylated form.
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB
References:
1.  De Santa, F., Totaro, M.G., Prosperini, E., Notarbartolo, S., Testa, G. and Natoli, G. The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing. Cell 130 (2007) 1083–1094. [PMID: 17825402]
2.  Hong, S., Cho, Y.W., Yu, L.R., Yu, H., Veenstra, T.D. and Ge, K. Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases. Proc. Natl. Acad. Sci. USA 104 (2007) 18439–18444. [PMID: 18003914]
3.  Lan, F., Bayliss, P.E., Rinn, J.L., Whetstine, J.R., Wang, J.K., Chen, S., Iwase, S., Alpatov, R., Issaeva, I., Canaani, E., Roberts, T.M., Chang, H.Y. and Shi, Y. A histone H3 lysine 27 demethylase regulates animal posterior development. Nature 449 (2007) 689–694. [PMID: 17851529]
4.  Lee, M.G., Villa, R., Trojer, P., Norman, J., Yan, K.P., Reinberg, D., Di Croce, L. and Shiekhattar, R. Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination. Science 318 (2007) 447–450. [PMID: 17761849]
5.  Xiang, Y., Zhu, Z., Han, G., Lin, H., Xu, L. and Chen, C.D. JMJD3 is a histone H3K27 demethylase. Cell Res. 17 (2007) 850–857. [PMID: 17923864]
[EC 1.14.11.68 created 2019]
 
 


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