Royal Society Publishing

The Structure of <latex>$\beta$</latex>-Lactamases

R. P. Ambler

Abstract

The <latex>$\beta$</latex>-lactamases are widely distributed in both Gram-positive and Gram-negative bacteria. They all inactivate penicillins and cephalosporins by opening the <latex>$\beta$</latex>-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 <latex>$\beta$</latex>-lactamases have a polyphyletic origin. All the <latex>$\beta$</latex>-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 <latex>$\beta$</latex>-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 <latex>$\beta$</latex>-lactamases of distinctive molecular and mechanistic properties.

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