%0 Journal Article
%T Characterization of the Bacillus subtilis Penicillin-Binding Protein PBP4
%A Arnaud Vanden Broeck
%A Eric Sauvage
%A Bernard Joris
%A Colette Duez
%J Advances in Microbiology
%P 164-176
%@ 2165-3410
%D 2019
%I Scientific Research Publishing
%R 10.4236/aim.2019.93013
%X <b>Purpose:</b> The PBP4* is a Penicillin Binding Protein belonging to the class C of AmpH type whose function remains poorly understood. This study aimed to evaluate the biophysical and enzymatic properties of the <i>Bacillus subtilis</i> PBP4* to gain insights into its role in the context of bacterial cell wall recycling. <b>Methods:</b> To characterize the PBP4*, the full-length PBP4* and its N-terminal penicillin-binding domain have been produced in <i>Escherichia coli</i> and purified. <b>Results:</b> A comparison of biophysical properties has shown that both recombinant proteins are monomeric in solution and retain the same thermal stability. On the other hand, the D-alanine methyl esterase activity detected with the full-length PBP4* is impeded by the cleavage of the 92 amino acid C-terminal domain. The esterase activity of the full-length PBP4* strates a clear D-stereospecificity. The PBP4* is also active on <i>B. subtilis</i> cell walls bearing teichoic acids, compounds commonly substituted with D-alanine residues. <b>Conclusions:</b> Our results are in agreement with the hypothesis that PBP4* could play a role in recycling cell wall components, as previously suggested.
%K B. subtilis PBP4*
%K Class-C PBP
%K D-Stereospecific Esterase
%U http://www.scirp.org/journal/PaperInformation.aspx?PaperID=90927