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
1977) with identical enzymatic and physiological functions but different heat stabilities and affinities toward p-lactam antibiotics (NAKAGAWA et al. 1979) (Table 1). PBP 1 a is heat labile and highly sensitive to p-lactam antibiotics. PBP 1 b, which is composed of at least three genetically indistinguishable proteins, is relatively heat stable and only moderately sensitive to p-lactam antibiotics. E. coli mutants lacking PBP 1 a have no phenotypic defect (SPRATT et al. 1977) while mutants lacking PBP 1 b are hypersensitive to p-lactam antibiotics (SUZUKI et al.
The enzyme is also present in a membrane-bound form acting exclusively as a transpeptidase. This fact and the fact that the membrane-bound form releases bound penicillin exclusively as penicilloic acid suggest different conformations of the two enzyme forms. The discussion which follows is limited to the exocellular form of the enzyme. a) Streptomyces R61 Streptomyces R 61 DD-carboxypeptidase has been purified to homogeneity by conventional methods, and, on SDS-polyacrylamide gel electrophoresis, has a molecular weight of 38,000 (FRERE et al.
DD-Carboxypeptidases (molecular weight: 25,000-50,000) from a variety of species have been isolated and studied extensively. In contrast, peptidoglycan transpeptidases (molecular weight: 90,000-100,000) have only recently been isolated and their properties are largely unknown. , B. subtilis DD-carboxypeptidase) in vitro transpeptidase activity. I. DD-Carboxypeptidases With a notable exception (FRERE et al. 1978), all DD-carboxypeptidases studied thus far are readily inhibited by penicillin, 7cx-methoxy cephalosporins and, to a lesser degreee, by nonmethoxylated cephalosporins.
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