SECONDARY STRUCTURE RELATIONS BETWEEN BETA‐LACTAMASES AND PENICILLIN‐SENSITIVE D—ALANINE—CARBOXYPEPTIDASES

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Abstract
The sequence homology found by Waxman and Strominger between penicillin-sensitive D-alanine-carboxypeptidases [Bacillus stearothermophilus, B. subtilis] and penicillin-inactivating .beta.-lactamases [Staphylococcus aureus, B. licheniformis, B. cereus, Escherichia coli plasmid R-TEM] extends to the level of secondary structure as predicted by the method of Chou and Fasman or by the informational method of Garnier et al. Thermodynamic similarity of homologous segments of these proteins is demonstrated by means of a sequence-independent parameter, the hydration potential of Wolfenden et al. Although the 40- to 70-residue amino-terminal sequences examined contain a common serine reactive with penicillins and (in the case of the carboxypeptidases) an R-D-alanyl-D-alanine substrate analog, no homology in secondary structure or hydration potential could be found with a serine protease such as .alpha.-chymotrypsin.