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Science 21 March 1986:
Vol. 231. no. 4744, pp. 1429 - 1431
DOI: 10.1126/science.3082007
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Articles

Science, Vol 231, Issue 4744, 1429-1431
Copyright © 1986 by American Association for the Advancement of Science

articles

On the origin of bacterial resistance to penicillin: comparison of a beta-lactamase and a penicillin target

JA Kelly, O Dideberg, P Charlier, JP Wery, M Libert, PC Moews, Knox JR, C Duez, C Fraipont, B Joris, and al. et

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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