The activity of a bacterial enzyme "able to degrade penicillin" had
first been described in 1940, even before the exact structure of
penicillin was elucidated and, by 1970, several enzymes had been
purified to homogeneity, the amino acid sequence of a
staphylococcal penicillinase was also known and that of its
Bacillus licheniformis counterpart was well under way. By contrast,
their catalytic mechanism remained quite mysterious. A Zn++
metallo-beta-lactamase (ss-lactamase II, BcII or ssII) had also
been described as soon as 1967 and later purified. It was thus
surprising that the first mechanistic information demonstrating the
presence of a penicillin-binding serine residue was obtained with a
penicillin-sensitive DD-peptidase rather than a ss-lactamase. This
seemed to open the floodgates and several class A ss-lactamases
were then rapidly shown to be active-site serine enzymes. This book
presents current research in the study of beta-lactamases.
General
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