Abstract
The penicilloyl serine transferases are proteins or protein domains that catalyse rupture of the β-lactam amide bond of penicillin and transfer of the penicilloyl moiety to an essential serine. The serine-ester-linked penicilloyl derivatives formed by reaction with the β-lactamases are hydrolytically labile. Those formed by reaction with the penicillin-binding proteins (PBPs) are hydrolytically inert. Penicilloylation of the essential serine of some PBPs produces a signal that is transmitted to the cytosol. Penicilloylation of other PBPs causes loss of a catalytic function related to wall peptidoglycan synthesis. For a recent review and list of references, see Ghuysen (1991).
This is a preview of subscription content, log in via an institution to check access.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Adam, M., Damblon, C, Jamin, M., Zorzi, W., Dusart, V., Galleni, M., El Kharroubi, A., Piras, G., Spratt, B.G., Keck, W., Coyette, J., Ghuysen, J.M., Nguyen-Distèche, M. and Frère, J.M. (1991) Acyltransferase activities of the high-molecular-mass essential penicillin-binding proteins. Biochem. J. 279, 601–604.
Adachi, H., Ishiguro, M., Imajoh, S., Ohta, T. and Matsuzawa, H. (1992) Active-site residues of the transpeptidase domain of penicillinbinding protein 2 from Escherichia coli: similarity in the catalytic mechanism to class A β-lactamases. Biochemistry 31, 430–437.
Asoh, S., Matsuzawa, H., Ishino, F., Strominger, J.L., Matsuhashi, M. and Ohta, T. (1986) Nucleotide sequence of the pbpA gene and characteristics of the deduced amino acid sequence of penicillinbinding protein 2 of Escherichia coli K12. Eur. J. Biochem. 160, 231–238.
Broome-Smith, J.K., Edelman, A., Yousif, S. and Spratt, B.G. (1985) The nucleotide sequence of the ponA and ponB genes encoding penicillin-binding proteins 1A and IB of Escherichia coli K12. Eur. J. Biochem. 147, 437–446.
Dowson, C.G., Hutchinson, A. and Spratt, B.G. (1989) Nucleotide sequence of the penicillin-binding protein 2B gene of Streptococcus pneumoniae strain R6. Nucl. Ac. Res. 17, 7518.
El Kharroubi, A., Jacques, P., Piras, G., Coyette, J., Van Beeumen, J. and Ghuysen, J.M. (1991) The Enterococcus hirae R40 penicillin-binding protein 5 and the methicillin-resistant Staphylococcus aureus penicillin-binding protein 2′ are similar. Biochem. J. 280, 463–469.
Gaboriaud, C, Bissery, V., Benchetrit, T. and Mornon, J.P. (1987) Hydrophobie cluster analyses: an efficient new way to compare and analyse amino acid sequences. FEBS Lett. 1, 149–155.
Ghuysen, J.M. (1991) Serine β-lactamases and penicillin-binding proteins. Annu. Rev. Microbiol. 45, 37–67.
Granier, B., Duez, C, Lepage, S., Englebert, S., Dusart, J., Dideberg, O., Van Beeumen, J., Frère, J.M. and Ghuysen, J.M. (1992) Primary and predicted secondary structures of the Actinomadura R39 extracellular DD-peptidase, a penicillin-binding protein (PBP) related to the Escherichia coli PBP4. Biochem. J. 228, 781–788.
Joris, B., Ledent, P., Dideberg, O., Fonzé, E., Lamotte-Brasseur, J., Kelly, J.A., Ghuysen, J.M. and Frère, J.M. (1991) Comparison of the sequences of class A β-lactamases and of the secondary structure elements of penicillin-recognizing proteins. Antimicrob. Ag. Chemother. 35, 2294–2301.
Laible, G., Hakenbeck, R., Sicard, M. A., Joris, B. and Ghuysen, J.M. (1989) Nucleotide sequence of the pbpX genes encoding the penicillin-binding proteins 2X from Streptococcus pneumoniae R6 and a cefotaxime-resistant mutant, C506. Mol. Microb. 3, 1337–1348.
Lamotte-Brasseur, J., Dive, G., Dideberg, O., Charlier, P., Frère, J.M. and Ghuysen, J.M. (1991) Mechanism of acyl transfer by the class A serine β-lactamase of Streptomyces albus G. Biochem. J. 279, 213–221.
Martin, C, Briese, T. and Hakenbeck, R. (1992) Nucleotide sequence of genes encoding penicillin-binding proteins from Streptococcus pneumoniae and Streptococcus oralis with high homology to Escherichia coli penicillin-binding proteins 1A and IB. J. Bacteriol., in press.
Nakamura, M., Maruyama, I.N., Soma, M., Kato, J.I., Suzuki, H. and Horota, Y. (1983) On the process of cellular division in Escherichia coli: nucleotide sequence of the gene for penicillin-binding protein 3. Mol. Gen. Genet. 191, 1–9.
Palomeque-Messia, P., Englebert, S., Leyh-Bouille, M., Nguyen-Distèche, M., Duez, C, Houba, S., Dideberg, O., Van Beeumen, J. and Ghuysen, J.M. (1991) Biochem. J. 279, 223–230.
Piras, G., El Kharroubi, A., Van Beeumen, J., Coeme, E., Coyette, J. and Ghuysen, J.M. (1990) Characterization of an Enterococcus hirae penicillin-binding protein 3 with low penicillin affinity. J. Bacteriol. 172, 6856–6862.
Song, M.D., Wachi, M., Doi, M., Ishino, F. and Matsuhashi, M. (1987) Evolution of an inducible penicillin-target protein in methicillinresistant Staphylococcus aureus by gene fusion. FEBS Lett. 221, 167–171.
Spratt, B.G. (1988) Hybrid penicillin-binding proteins in penicillin-resistant strains of Neisseria gonorrhoeae. Nature 332, 173–176.
Zhang, Q.Y. and Spratt, B.G. (1989) Nucleotide sequence of the penicillin-binding protein 2 gene of Neisseria meningitidis. Nucl. Ac. Res. 17, 5383.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 1993 Springer Science+Business Media New York
About this chapter
Cite this chapter
Englebert, S. et al. (1993). Modular Design of the Bi(Multi?)Functional Penicillin-Binding Proteins. In: de Pedro, M.A., Höltje, JV., Löffelhardt, W. (eds) Bacterial Growth and Lysis. Federation of European Microbiological Societies Symposium Series, vol 65. Springer, Boston, MA. https://doi.org/10.1007/978-1-4757-9359-8_38
Download citation
DOI: https://doi.org/10.1007/978-1-4757-9359-8_38
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4757-9361-1
Online ISBN: 978-1-4757-9359-8
eBook Packages: Springer Book Archive