Download e-book for iPad: Antibiotics: Containing the Beta-Lactam Structure, Part II by N. H. Georgopapadakou, R. B. Sykes (auth.), Professor Dr.

By N. H. Georgopapadakou, R. B. Sykes (auth.), Professor Dr. Arnold L. Demain, Ms. Nadine A. Solomon (eds.)

ISBN-10: 3642689019

ISBN-13: 9783642689017

ISBN-10: 3642689035

ISBN-13: 9783642689031

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Additional info for Antibiotics: Containing the Beta-Lactam Structure, Part II

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DFP (10 mM) inhibits binding of penicillin indicating that this enzyme too might be a Bacterial Enzymes Interacting with p-Lactam Antibiotics 31 serine peptidase (GEORGOPAPAOAKOU and Lm, unpublished work). Contrary to carboxypeptidase I A, carboxypeptidase I B is activated by EDTA and divalent cations (TAMURA et al. 1976). In S. typhimurium two oo-carboxypeptidases have been found (PBPs 4 and 5) which appear to be homologous to those of E. coli (SHEPHERO et al. 1977). Both PBPs 5 and 4 release bound penicillin, with half-lives of 5 and 90 min at 37°C, respectively.

9. A remarkable feature of its amino acid sequence is the extensive homology (approximately 40%) to the fJlactamases of B. licheniformis and B. cereus (AMBLER 1975; THATCHER 1975). The enzyme is inactivated by iodine (RICHMOND 1963) and tetranitromethane (AMBLER 1975), the latter reacting preferentially with tyrosine-82. However, as in other proteins, tetranitromethane promotes intermolecular cross-linking resulting in a high-molecular-weight inactive species, which accounts for the observed inactivation, while the monomeric species has normal activity (BRISTOW and VIRDEN 1978).

1979). It is possible that the 98,000- and 118,000-dalton proteins in P. aeruginosa correspond to PBPs 1 band 1 a of E. coli and that the 86,000-dalton protein has no E. coli counterpart. Curiously, mecillinam appears to inhibit penicillin binding to the 86,000-dalton protein at concentrations less than 10 Ilg(ml (GEORGOPAPADAKOU and Lru, unpublished work). Binding of fJ-lactam antibiotics to P. aeruginosa PBPs results in morphological changes similar to those observed in E. coli, although the concentration range over which these occur may differ as a result of differences in permeability (NIKAIDO and NAKAE 1979), fJ-lactamases (OHMORI et al.

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Antibiotics: Containing the Beta-Lactam Structure, Part II by N. H. Georgopapadakou, R. B. Sykes (auth.), Professor Dr. Arnold L. Demain, Ms. Nadine A. Solomon (eds.)

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