The structure of β-lactamases

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  • R. P. Ambler
    Department of Molecular Biology, University of Edinburgh, King's Buildings, Mayfield Road, Edinburgh EH9 3JR, U. K.

書誌事項

公開日
1980-05-16
権利情報
  • https://royalsociety.org/journals/ethics-policies/data-sharing-mining/
DOI
  • 10.1098/rstb.1980.0049
公開者
The Royal Society

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説明

<jats:title>Abstract</jats:title> <jats:p>The β-lactamases are widely distributed in both Gram-positive and Gram-negative bacteria. They all inactivate penicillins and cephalosporins by opening the β-lactam ring. Many varieties of the enzyme can be distinguished on the basis of their catalytic and molecular properties, but only amino acid sequence determination gives information upon which a molecular phylogeny can be based. The present evidence suggests that the β-lactamases have a polyphyletic origin. All the β-lactamases of currently known amino acid sequence belong to one homology group, here called class A enzymes. Class B consists of the mechanistically distinct Bacillus cereus β-lactamase II, which preliminary partial sequence analysis suggests to be structurally unrelated to the class A enzymes. It is predicted that sequence analysis will show that further classes will need to be created to account for particular β-lactamases of distinctive molecular and mechanistic properties.</jats:p>

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