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
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.