Issue 5, 2013

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

Abstract

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.

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

Supplementary files

Article information

Article type
Paper
Submitted
01 Jan 2013
Accepted
10 Feb 2013
First published
11 Feb 2013

Mol. BioSyst., 2013,9, 1026-1034

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

A. Tsuchiya, M. Asanuma, G. Hirai, K. Oonuma, M. Muddassar, E. Nishizawa, Y. Koyama, Y. Otani, K. Y. J. Zhang and M. Sodeoka, Mol. BioSyst., 2013, 9, 1026 DOI: 10.1039/C3MB00003F

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