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.)

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

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PBP 3 (molecular weight: 56,000-62,000) is sensitive to both penicillins and cephalosporins. PBP 4 (molecular weight: 45,000-49,000) sometimes solubilized during membrane isolation as in Klebsiella pneumoniae, is generally sensitive to fJ-lactam antibiotics and, in the case of S. typhimurium, has been shown to possess DD-carboxypeptidase and natural model transpeptidase activities (SHEPHERD et al. 1977). PBP 5(6 (molecular weight: 36,000-40,000), the major PBP, is moderately sensitive to fJ-lactam antibiotics and possesses DD-carboxypeptidase and weak penicillinase activity (MARTIN et al.

II. Penicillin-Binding Proteins in Gram-Negative Bacteria Although PBP patterns in gram-negative bacteria are diverse, those of enterobacteria are remarkably similar. Unfortunately, as most studies have involved enterobacteria, a false impression has been created of the universality of the enterobacterial PBP pattern (CURTIS et al. 1979 a). Perhaps the only universal feature ofPBPs is a 35,000- to 40,000-dalton protein, present in varying amounts, which is moderately sensitive to p-Iactam antibiotics and has weak but measurable p-1actamase activity.

The properties of the two enzymes are very similar although the optimal temperatures for activity differ by over 20°C. In addition to carboxypeptidase activity, the enzyme shows some transpeptidase activity, the amino donor being glycine or o-alanine but not meso-diaminopimelic acid (NISIflNO et al. 1977). B. megaterium oo-carboxypeptidase (PBP 5) has a molecular weight of 45,000 and has been solubilized by nonionic detergents and purified by affinity chromatography on ampicillin-Affinose (CHASE et al.

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