In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE.

Ivan Mijakovic, Lucia Musumeci, Lutz Tautz, Dina Petranovic, Robert A. Edwards, Peter Ruhdal Jensen, Tomas Mustelin, Josef Deutscher, Nunzio Bottini

    Research output: Contribution to journalJournal articlepeer-review


    Both gram-negative and gram-positive bacteria possess protein tyrosine phosphatases (PTPs) with a catalytic Cys residue. In addition, many gram-positive bacteria have acquired a new family of PTPs, whose first characterized member was CpsB from Streptococcus pneumoniae. Bacillus subtilis contains one such CpsB-like PTP, YwqE, in addition to two class II Cys-based PTPs, YwlE and YfkJ. The substrates for both YwlE and YfkJ are presently unknown, while YwqE was shown to dephosphorylate two phosphotyrosine-containing proteins implicated in UDP-glucuronate biosynthesis, YwqD and YwqF. In this study, we characterize YwqE, compare the activities of the three B. subtilis PTPs (YwqE, YwlE, and YfkJ), and demonstrate that the two B. subtilis class II PTPs do not dephosphorylate the physiological substrates of YwqE.
    Original languageEnglish
    JournalJournal of Bacteriology
    Issue number10
    Pages (from-to)3384-3390
    Publication statusPublished - 2005


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