Sandbox Reserved 1491: Difference between revisions

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[[Image:Reactionjpg.jpg | thumb | upright=3 | Enzymatic reaction of demethylation of H3K9(me3) and H3K36(me3) by KDM4C ]]

'''KDM4C/JMJD2''' is a protein which converts specifically trimethylated histone residues to the dimethylated form. Indeed, it catalyzes the demethylation of both '''Lysine 9 and Lysine 36 of histone 3''' (respectively H3K9me3 and H3K36me3 by hydroxylation of the lysine methyl group. This reaction leads to a dissociation of the methyl group from the lysine histone tail. KDM4C employs [https://en.wikipedia.org/wiki/Alpha-Ketoglutaric_acid 2-oxoglutarate] (OG), Fe2+ and oxygen as cosubstrates to promote its enzymatic reaction, thus the '''dissociation of methyl groups'''<ref>Leurs, Ulrike, Brian Lohse, Kasper D. Rand, Shonoi Ming, Erik S. Riise, Philip A. Cole, Jesper L. Kristensen, and Rasmus P. Clausen. “Substrate- and Cofactor-Independent Inhibition of Histone Demethylase KDM4C.” ACS Chemical Biology 9, no. 9 (September 19, 2014): 2131–38. https://doi.org/10.1021/cb500374f.</ref>.

'''KDM4C/JMJD2''' is a protein which converts specifically trimethylated histone residues to the dimethylated form. Indeed, it catalyzes the demethylation of both '''Lysine 9 and Lysine 36 of histone 3''' (respectively H3K9me3 and H3K36me3 by hydroxylation of the lysine methyl group. This reaction leads to a dissociation of the methyl group from the lysine histone tail.

KDM4C employs [https://en.wikipedia.org/wiki/Alpha-Ketoglutaric_acid 2-oxoglutarate] (OG), Fe2+ and oxygen as cosubstrates to promote its enzymatic reaction, thus the '''dissociation of methyl groups'''<ref>Leurs, Ulrike, Brian Lohse, Kasper D. Rand, Shonoi Ming, Erik S. Riise, Philip A. Cole, Jesper L. Kristensen, and Rasmus P. Clausen. “Substrate- and Cofactor-Independent Inhibition of Histone Demethylase KDM4C.” ACS Chemical Biology 9, no. 9 (September 19, 2014): 2131–38. https://doi.org/10.1021/cb500374f.</ref>.

Sandbox Reserved 1491: Difference between revisions

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 [[Image:Reactionjpg.jpg | thumb | upright=3 | Enzymatic reaction of demethylation of H3K9(me3) and H3K36(me3) by KDM4C ]]
-'''KDM4C/JMJD2''' is a protein which converts specifically trimethylated histone residues to the dimethylated form. Indeed, it catalyzes the demethylation of both '''Lysine 9 and Lysine 36 of histone 3''' (respectively H3K9me3 and H3K36me3 by hydroxylation of the lysine methyl group. This reaction leads to a dissociation of the methyl group from the lysine histone tail. KDM4C employs [https://en.wikipedia.org/wiki/Alpha-Ketoglutaric_acid 2-oxoglutarate] (OG), Fe2+ and oxygen as cosubstrates to promote its enzymatic reaction, thus the '''dissociation of methyl groups'''<ref>Leurs, Ulrike, Brian Lohse, Kasper D. Rand, Shonoi Ming, Erik S. Riise, Philip A. Cole, Jesper L. Kristensen, and Rasmus P. Clausen. “Substrate- and Cofactor-Independent Inhibition of Histone Demethylase KDM4C.” ACS Chemical Biology 9, no. 9 (September 19, 2014): 2131–38. https://doi.org/10.1021/cb500374f.</ref>.
+'''KDM4C/JMJD2''' is a protein which converts specifically trimethylated histone residues to the dimethylated form. Indeed, it catalyzes the demethylation of both '''Lysine 9 and Lysine 36 of histone 3''' (respectively H3K9me3 and H3K36me3 by hydroxylation of the lysine methyl group. This reaction leads to a dissociation of the methyl group from the lysine histone tail.
+KDM4C employs [https://en.wikipedia.org/wiki/Alpha-Ketoglutaric_acid 2-oxoglutarate] (OG), Fe2+ and oxygen as cosubstrates to promote its enzymatic reaction, thus the '''dissociation of methyl groups'''<ref>Leurs, Ulrike, Brian Lohse, Kasper D. Rand, Shonoi Ming, Erik S. Riise, Philip A. Cole, Jesper L. Kristensen, and Rasmus P. Clausen. “Substrate- and Cofactor-Independent Inhibition of Histone Demethylase KDM4C.” ACS Chemical Biology 9, no. 9 (September 19, 2014): 2131–38. https://doi.org/10.1021/cb500374f.</ref>.