By N. H. Georgopapadakou, R. B. Sykes (auth.), Professor Dr. Arnold L. Demain, Ms. Nadine A. Solomon (eds.)
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Extra info for Antibiotics: Containing the Beta-Lactam Structure, Part II
9). Both DD-carboxypeptidase and peptidoglycan transpeptidase are present in all species of bacteria examined thus far and both are PBPs. When assayed in vitro, there appears to be some spill-over of enzymatic activity between the two enzymes. That is, most DD-carboxypeptidases are capable of both hydrolysis and transpeptidation under certain conditions and have been called DD-carboxypeptidases-transpeptidases. Although this may have important mechanistic and evolutionary implications, the physiological role of each enzyme is specific.
The PBP patterns of Proteus and Serratia differ somewhat from those of the rest of enterobacteria (Table 3). Significantly, it has been suggested that both genera are taxonomically and evolutionarily distant from the rest of enterobacteria (GRIMONT and GRIMONT 1978). Proteus PBPs are almost identical from species to species (OHYA et al. 1979) and can be correlated fairly easily with those of E. coli. Serratia PBPs are generally resistant to fJ-lactam antibiotics (GEORGOPAPADAKOU and Lru, unpublished work) which might account to some extent for the resistance of these organisms to most fJ-lactam antibiotics.
It is moderately sensitive to penicillin which releases as penicilloic acid with a half-life at 30°C of less than 1 min (KOZARICH and STROMINGER 1978). It catalyzes both the release ofo-alanine from the synthetic substrate DiacL-Lys-o-Ala-o-Ala and the transfer of the Diac-L-Lys-o-Ala to water or simple amino acceptors such as glycine and hydroxylamine. It does not, however, catalyze natural model transpeptidations. Acyl-enzyme complexes have been isolated by SDS-polyacrylamide gel electrophoresis both with substrate and penicillin (KOZARICH and STROMINGER 1978).