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Duez, C., Vanhove, M., Gallet, X., Bouillenne, F., Docquier, J.-D., Brans, A. and Frère, J.-M. (2001) Purification and Characterization of PBP4a, a New Low-Mo- lecular-Weight Penicillin-Binding Protein from Bacillus subtilis. Journal of Bacteriology, 183, 1595-1599.
https://doi.org/10.1128/JB.183.5.1595-1599.2001

has been cited by the following article:

• TITLE: Characterization of the Bacillus subtilis Penicillin-Binding Protein PBP4

  AUTHORS: Arnaud Vanden Broeck, Eric Sauvage, Bernard Joris, Colette Duez

  KEYWORDS: B. subtilis PBP4*, Class-C PBP, D-Stereospecific Esterase

  JOURNAL NAME: Advances in Microbiology, Vol.9 No.3, March 5, 2019

  ABSTRACT: Purpose: 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 Bacillus subtilis PBP4* to gain insights into its role in the context of bacterial cell wall recycling. Methods: To characterize the PBP4*, the full-length PBP4* and its N-terminal penicillin-binding domain have been produced in Escherichia coli and purified. Results: 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 B. subtilis cell walls bearing teichoic acids, compounds commonly substituted with D-alanine residues. Conclusions: Our results are in agreement with the hypothesis that PBP4* could play a role in recycling cell wall components, as previously suggested.