TY - JOUR
T1 - In vitro characterization of the Bacillus subtilis protein tyrosine phosphatase YwqE
AU - Mijakovic, Ivan
AU - Musumeci, Lucia
AU - Tautz, Lutz
AU - Petranovic, Dina
AU - Edwards, Robert A.
AU - Jensen, Peter Ruhdal
AU - Mustelin, Tomas
AU - Deutscher, Josef
AU - Bottini, Nunzio
PY - 2005/5
Y1 - 2005/5
N2 - 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, YwIE and YfkJ. The substrates for both YwIE 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, YwIE, and YfkJ), and demonstrate that the two B. subtilis class II PTPs do not dephosphorylate the physiological substrates of YwqE.
AB - 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, YwIE and YfkJ. The substrates for both YwIE 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, YwIE, and YfkJ), and demonstrate that the two B. subtilis class II PTPs do not dephosphorylate the physiological substrates of YwqE.
UR - http://www.scopus.com/inward/record.url?scp=18244375248&partnerID=8YFLogxK
U2 - 10.1128/JB.187.10.3384-3390.2005
DO - 10.1128/JB.187.10.3384-3390.2005
M3 - Article
C2 - 15866923
AN - SCOPUS:18244375248
SN - 0021-9193
VL - 187
SP - 3384
EP - 3390
JO - Journal of Bacteriology
JF - Journal of Bacteriology
IS - 10
ER -