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Journal of Bacteriology, March 2001, p. 1595-1599, Vol. 183, No. 5
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.5.1595-1599.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

Purification and Characterization of PBP4a, a New Low-Molecular-Weight Penicillin-Binding Protein from Bacillus subtilis

Colette Duez,1 Marc Vanhove,1 Xavier Gallet,2 Fabrice Bouillenne,1 Jean-Denis Docquier,1 Alain Brans,1 and Jean-Marie Frère1,*

Centre d'Ingénierie des Protéines and Laboratoire d'Enzymologie, Institut de Chimie, Université de Liège, B-4000 Liège,1 and Laboratoire de Biophysique Moléculaire Numérique, Faculté Universitaire des Sciences Agronomiques, B-5030 Gembloux,2 Belgium

Received 22 June 2000/Accepted 4 December 2000

Penicillin-binding protein 4a (PBP4a) from Bacillus subtilis was overproduced and purified to homogeneity. It clearly exhibits DD-carboxypeptidase and thiolesterase activities in vitro. Although highly isologous to the Actinomadura sp. strain R39 DD-peptidase (B. Granier, C. Duez, S. Lepage, S. Englebert, J. Dusart, O. Dideberg, J. van Beeumen, J. M. Frère, and J. M. Ghuysen, Biochem. J. 282:781-788, 1992), which is rapidly inactivated by many beta -lactams, PBP4a is only moderately sensitive to these compounds. The second-order rate constant (k2/K) for the acylation of the essential serine by benzylpenicillin is 300,000 M-1 s-1 for the Actinomadura sp. strain R39 peptidase, 1,400 M-1 s-1 for B. subtilis PBP4a, and 7,000 M-1 s-1 for Escherichia coli PBP4, the third member of this class of PBPs. Cephaloridine, however, efficiently inactivates PBP4a (k2/K = 46,000 M-1 s-1). PBP4a is also much more thermostable than the R39 enzyme.

* Corresponding author. Mailing address: Centre d'Ingénierie des Protéines and Laboratoire d'Enzymologie, Université de Liège, Institut de Chimie, B6, Sart Tilman, B-4000 Liège, Belgium. Phone: 32-4-366.33.98. Fax: 32-4-366.33.64. E-mail: jmfrere{at}ulg.ac.be.

Journal of Bacteriology, March 2001, p. 1595-1599, Vol. 183, No. 5
0021-9193/01/$04.00+0   DOI: 10.1128/JB.183.5.1595-1599.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.


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Copyright © 2001 by the American Society for Microbiology. All rights reserved.