IntEnz - EC 1.14.11.68

EC 1 - Oxidoreductases

EC 1.14 - Acting on paired donors, with incorporation or reduction of molecular oxygen. The oxygen incorporated need not be derived from O₂

EC 1.14.11 - With 2-oxoglutarate as one donor, and incorporation of one atom each of oxygen into both donors

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

(1) 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
(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

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: (14) [show] [UniProt]

References

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]
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]
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]
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]
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]