ExplorEnz: EC 1.14.11.69

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1.14.11.69

Accepted name:

[histone H3]-trimethyl-L-lysine³⁶ demethylase

Reaction:

a [histone H3]-N⁶,N⁶,N⁶-trimethyl-L-lysine³⁶ + 2 2-oxoglutarate + 2 O₂ = a [histone H3]-N⁶-methyl-L-lysine³⁶ + 2 succinate + 2 formaldehyde + 2 CO₂ (overall reaction)
(1a) a [histone H3]-N⁶,N⁶,N⁶-trimethyl-L-lysine³⁶ + 2-oxoglutarate + O₂ = a [histone H3]-N⁶,N⁶-dimethyl-L-lysine³⁶ + succinate + formaldehyde + CO₂
(1b) a [histone H3]-N⁶,N⁶-dimethyl-L-lysine³⁶ + 2-oxoglutarate + O₂ = a [histone H3]-N⁶-methyl-L-lysine³⁶ + succinate + formaldehyde + CO₂

Other name(s):

KDM4A (gene name); KDM4B (gene name); RPH1 (gene name); JHDM3A (gene name); JHDM3B (gene name); JMJD2A (gene name); JMJD2B (gene name)

Systematic name:

[histone H3]-N⁶,N⁶,N⁶-trimethyl-L-lysine³⁶,2-oxoglutarate:oxygen oxidoreductase

Comments:

Requires iron(II). This entry describes a group of enzymes that demethylate N-methylated Lys³⁶ residues in the tail of the histone protein H3 (H3K36). This lysine residue can exist in three methylation states (mono-, di- and trimethylated), but this group of enzymes only act on the the tri- and di-methylated forms. The enzymes are dioxygenases and act by hydroxylating the methyl group, forming an unstable hemiaminal that leaves as formaldehyde. Since trimethylation of H3K36 enhances transcription, this enzyme acts as a transcription repressor. The enzymes that possess this activity often also catalyse the activity of EC 1.14.11.66, [histone H3]-trimethyl-L-lysine⁹ demethylase. cf. EC 1.14.11.27, [histone H3]-dimethyl-L-lysine³⁶ demethylase.

Links to other databases:

BRENDA, EXPASY, Gene, KEGG, MetaCyc, PDB

References:

1.	Whetstine, J.R., Nottke, A., Lan, F., Huarte, M., Smolikov, S., Chen, Z., Spooner, E., Li, E., Zhang, G., Colaiacovo, M. and Shi, Y. Reversal of histone lysine trimethylation by the JMJD2 family of histone demethylases. Cell 125 (2006) 467–481. [PMID: 16603238]
2.	Klose, R.J., Yamane, K., Bae, Y., Zhang, D., Erdjument-Bromage, H., Tempst, P., Wong, J. and Zhang, Y. The transcriptional repressor JHDM3A demethylates trimethyl histone H3 lysine 9 and lysine 36. Nature 442 (2006) 312–316. [PMID: 16732292]
3.	Kim, T. and Buratowski, S. Two Saccharomyces cerevisiae JmjC domain proteins demethylate histone H3 Lys³⁶ in transcribed regions to promote elongation. J. Biol. Chem. 282 (2007) 20827–20835. [PMID: 17525156]
4.	Couture, J.F., Collazo, E., Ortiz-Tello, P.A., Brunzelle, J.S. and Trievel, R.C. Specificity and mechanism of JMJD2A, a trimethyllysine-specific histone demethylase. Nat. Struct. Mol. Biol. 14 (2007) 689–695. [PMID: 17589523]
5.	Lin, C.H., Li, B., Swanson, S., Zhang, Y., Florens, L., Washburn, M.P., Abmayr, S.M. and Workman, J.L. Heterochromatin protein 1a stimulates histone H3 lysine 36 demethylation by the Drosophila KDM4A demethylase. Mol. Cell 32 (2008) 696–706. [PMID: 19061644]
6.	Colmenares, S.U., Swenson, J.M., Langley, S.A., Kennedy, C., Costes, S.V. and Karpen, G.H. Drosophila histone demethylase KDM4A has enzymatic and non-enzymatic roles in controlling heterochromatin integrity. Dev Cell 42 (2017) 156–169.e5. [PMID: 28743002]

[EC 1.14.11.69 created 2019]