EC 1.14.11.68 - [histone H3]-trimethyl-L-lysine27 demethylase

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IntEnz Enzyme Nomenclature
EC 1.14.11.68

Names

Accepted name:
[histone H3]-trimethyl-L-lysine27 demethylase
Systematic name:
[histone H3]-N6,N6,N6-trimethyl-L-lysine27,2-oxoglutarate:oxygen oxidoreductase

Reactions

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

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Structural data: CSA , EC2PDB
Gene Ontology: GO:0071558
UniProtKB/Swiss-Prot: (13) [show] [UniProt]

References

  1. De Santa, F., Totaro, M. G., Prosperini, E., Notarbartolo, S., Testa, G., Natoli, G.
    The histone H3 lysine-27 demethylase Jmjd3 links inflammation to inhibition of polycomb-mediated gene silencing.
    Cell 130 : 1083-1094 (2007). [PMID: 17825402]
  2. Hong, S., Cho, Y. W., Yu, L. R., Yu, H., Veenstra, T. D., Ge, K.
    Identification of JmjC domain-containing UTX and JMJD3 as histone H3 lysine 27 demethylases.
    Proc. Natl. Acad. Sci. U.S.A. 104 : 18439-18444 (2007). [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., Shi, Y.
    A histone H3 lysine 27 demethylase regulates animal posterior development.
    Nature 449 : 689-694 (2007). [PMID: 17851529]
  4. Lee, M. G., Villa, R., Trojer, P., Norman, J., Yan, K. P., Reinberg, D., Di Croce, L., Shiekhattar, R.
    Demethylation of H3K27 regulates polycomb recruitment and H2A ubiquitination.
    Science 318 : 447-450 (2007). [PMID: 17761849]
  5. Xiang, Y., Zhu, Z., Han, G., Lin, H., Xu, L., Chen, C. D.
    JMJD3 is a histone H3K27 demethylase.
    Cell Res. 17 : 850-857 (2007). [PMID: 17923864]

[EC 1.14.11.68 created 2019]