通过逐出结构 Zn(II)抑制组蛋白赖氨酸去甲基酶 JMJD2A。
Inhibition of the histone lysine demethylase JMJD2A by ejection of structural Zn(II).
机构信息
Department of Chemistry and the Oxford Centre for Integrative Systems Biology, Chemistry Research Laboratory, University of Oxford, 12 Mansfield Road, Oxford, UK OX1 3TA.
出版信息
Chem Commun (Camb). 2009 Nov 14(42):6376-8. doi: 10.1039/b916357c. Epub 2009 Sep 28.
JMJD2A, a 2-oxoglutarate dependent N(epsilon)-methyl lysine histone demethylase, is inhibited by disruption of its Zn-binding site by Zn-ejecting compounds including disulfiram and ebselen; this observation may enable the development of inhibitors selective for this subfamily of 2OG dependent oxygenases that do not rely on binding to the highly-conserved Fe(ii)-containing active site.
JMJD2A 是一种依赖 2-氧戊二酸的 N(ε)-甲基赖氨酸组蛋白去甲基酶，其锌结合位点被锌逐出化合物（包括双硫仑和依布硒啉）破坏后会受到抑制；这一观察结果可能使选择性针对该 2OG 依赖性加氧酶亚家族的抑制剂的开发成为可能，而这些抑制剂不依赖于与高度保守的含 Fe(ii)活性位点结合。
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