On the Origin of Bacterial Resistance to Penicillin: Comparison of a β-Lactamase and a Penicillin Target
Julia Kelly(University of Connecticut), O. Dideberg(University of Liège), P. Charlier(University of Liège), Jean‐Pierre Wery(University of Liège), Marie Libert(University of Liège), Paul C. Moews(University of Connecticut), James R. Knox(University of Connecticut), Colette Duez(University of Liège), Cl. Fraipont(University of Liège), Bernard Joris(University of Liège), Jean Dusart(University of Liège), J.-M. Frère(University of Liège), Jean‐Marie Ghuysen(University of Liège)
Cited by 223Open Access
Abstract
Structural data are now available for comparing a penicillin target enzyme, the D-alanyl-D-alanine-peptidase from Streptomyces R61, with a penicillin-hydrolyzing enzyme, the beta-lactamase from Bacillus licheniformis 749/C. Although the two enzymes have distinct catalytic properties and lack relatedness in their overall amino acid sequences except near the active-site serine, the significant similarity found by x-ray crystallography in the spatial arrangement of the elements of secondary structure provides strong support for earlier hypotheses that beta-lactamases arose from penicillin-sensitive D-alanyl-D-alanine-peptidases involved in bacterial wall peptidoglycan metabolism.
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