Sandbox Reserved 1491: Difference between revisions
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Two families of [https://en.wikipedia.org/wiki/Demethylase histone-lysine demethylase] (KDM) have been identified as follows : the '''flavin (FAD)-dependent lysine-specific demethylases''' and the '''Fe(II)-dependent Jumonji C (JmjC) family'''. JmjC is subfamily of histone demethylases which regroups several proteins containing a specific catalytic domain called '''Jmjc''' found in ''' 2xml structure'''<ref>Shi, Y. G., and Y.-i. Tsukada. “The Discovery of Histone Demethylases.” Cold Spring Harbor Perspectives in Biology 5, no. 9 (September 1, 2013): a017947–a017947. https://doi.org/10.1101/cshperspect.a017947.</ref>. KDM4 demethylases belong to the JmjC family and contains six members : KDM4A-F<ref>Labbé, Roselyne M., Andreana Holowatyj, and Zeng-Quan Yang. “Histone Lysine Demethylase (KDM) Subfamily 4: Structures, Functions and Therapeutic Potential.” American Journal of Translational Research 6, no. 1 (2013): 1–15</ref>. | Two families of [https://en.wikipedia.org/wiki/Demethylase histone-lysine demethylase] (KDM) have been identified as follows : the '''flavin (FAD)-dependent lysine-specific demethylases''' and the '''Fe(II)-dependent Jumonji C (JmjC) family'''. JmjC is subfamily of histone demethylases which regroups several proteins containing a specific catalytic domain called '''Jmjc''' found in ''' 2xml structure'''<ref>Shi, Y. G., and Y.-i. Tsukada. “The Discovery of Histone Demethylases.” Cold Spring Harbor Perspectives in Biology 5, no. 9 (September 1, 2013): a017947–a017947. https://doi.org/10.1101/cshperspect.a017947.</ref>. KDM4 demethylases belong to the JmjC family and contains six members : KDM4A-F<ref>Labbé, Roselyne M., Andreana Holowatyj, and Zeng-Quan Yang. “Histone Lysine Demethylase (KDM) Subfamily 4: Structures, Functions and Therapeutic Potential.” American Journal of Translational Research 6, no. 1 (2013): 1–15</ref>. | ||
[[Image:Reactionjpg.jpg | thumb | | [[Image:Reactionjpg.jpg | thumb | upright=3,5 | 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 one methyl group'''<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 one methyl group'''<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>. | ||
