Evaluation of phenylcyclopropylamine compounds by enzymatic assay of lysine-specific demethylase 2 in the presence of NPAC peptide

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• 作者：Taeko Kakizawa^a ; Tamio Mizukami^b ; Yukihiro Itoh^c ; Makoto Hasegawa^b ; Ryuzo Sasaki^b ; Takayoshi Suzuki^c ; ^{suzukit@koto.kpu-m.ac.jp" class="auth_mail" title="E-mail the corresponding author}
• 关键词：Inhibitor ; Lysine-specific demethylases 1 and 2 (LSD1 and LSD2) ; NPAC peptide ; Histone H3K4 demethylation
• 刊名：Bioorganic & Medicinal Chemistry Letters
• 出版年：2016
• 出版时间：15 February 2016
• 年：2016
• 卷：26
• 期：4
• 页码：1193-1195
• 全文大小：780 K

文摘

Lysine-specific demethylase 2 (LSD2) demethylates mono- and dimethylated Lys-4 of histone H3 (H3K4me1 and H3K4me2). NPAC protein is known to interact with LSD2 and promote its H3K4 demethylase activity. In this study, we established a demethylation assay system that utilizes recombinant LSD2 in the presence of a synthetic NPAC peptide. Several phenylcyclopropylamine (PCPA)-based inhibitors were examined for their LSD2 inhibitory activity in the LSD2 enzymatic assay with the NPAC peptide. The assay results showed that the PCPA derivatives, including NCD41, selectively inhibited LSD1 in preference to LSD2.