Modular Design of the Bi(Multi?)Functional Penicillin-Binding Proteins
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Publisher
Springer US
Link
http://link.springer.com/content/pdf/10.1007/978-1-4757-9359-8_38
Reference19 articles.
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2. 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.
3. 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.
4. 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.
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1. Sequence of the ponA gene and characterization of the penicillin-binding protein 1A of Pseudomonas aeruginosa PAO1;Gene;1997-10
2. The bimodular G57-V577 polypeptide chain of the class B penicillin-binding protein 3 of Escherichia coli catalyzes peptide bond formation from thiolesters and does not catalyze glycan chain polymerization from the lipid II intermediate;Journal of Bacteriology;1997-10
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4. Molecular analysis of a beta-lactam resistance gene encoded within the cephamycin gene cluster of Streptomyces clavuligerus;Journal of Bacteriology;1996-11
5. The non-penicillin-binding module of the tripartite penicillin-binding protein 3 of Escherichia coli is required for folding and/or stability of the penicillin-binding module and the membrane-anchoring module confers cell septation activity on the folded structure;Journal of Bacteriology;1996-09
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