CDC25A-inhibitory RE derivatives bind to pocket adjacent to the catalytic site

Ayako Tsuchiya, Miwako Asanuma, Go Hirai, Kana Oonuma, Muhammad Muddassar, Eri Nishizawa, Yusuke Koyama, Yuko Otani, Kam Y.J. Zhang, Mikiko Sodeoka

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7 Citations (Scopus)


RE derivatives, which are cell-permeable and non-electrophilic dual-specificity protein phosphatase inhibitors developed in our laboratory, inhibit CDC25A/B non-competitively, as determined by means of kinetic experiments. To identify the binding site of RE derivatives, we designed and synthesized the new probe molecule RE142, having a Michael acceptor functionality for covalent bond formation with the enzyme, a biotin tag to enable enrichment of probe-bound peptide(s), and a chemically cleavable linker to facilitate release of probe-bound peptides from avidin beads. LC-MS analysis indicated that RE142 binds to one of the residues Cys384-Tyr386 of CDC25A, within a pocket adjacent to the catalytic site.

Original languageEnglish
Pages (from-to)1026-1034
Number of pages9
JournalMolecular BioSystems
Issue number5
Publication statusPublished - May 2013
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Molecular Biology


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