9 research outputs found

    Acyltransferase activities of the high-molecular-mass essential penicillin-binding proteins

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    The high-molecular-mass penicillin-binding proteins (HMM-PBPs), present in the cytoplasmic membranes of all eubacteria, are involved in important physiological events such as cell elongation, septation or shape determination. Up to now it has, however, been very difficult or impossible to study the catalytic properties of the HMM-PBPs in vitro. With simple substrates, we could demonstrate that several of these proteins could catalyse the hydrolysis of some thioesters or the transfer of their acyl moiety on the amino group of a suitable acceptor nucleophile. Many of the acyl-donor substrates were hippuric acid or benzoyl-D-alanine derivatives, and their spectroscopic properties enabled a direct monitoring of the enzymic reaction. In their presence, the binding of radioactive penicillin to the PBPs was also inhibited

    Mode of Membrane Insertion and Sequence of a 32-Amino Acid Peptide Stretch of the Penicillin-Binding Protein 4 of Enterococcus Hirae

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    Analysis of water-soluble derivatives of the Enterococcus hirae 75-kDa membrane-bound penicillin-binding protein 4 (PBP4) has yielded the amino acid sequence of a 32-amino acid polypeptide stretch. This peptide is similar to peptide segments known to occur in the N-terminal domain of high-Mr PBPs of class B. The E. hirae PBP4 probably belongs to the same class. It is anchored in the membrane at the N-terminus of the polypeptide chain

    Modular Design of the Bi(multi?) functional penicillin-binding proteins

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    peer reviewedProceedings of a symposium held in Mallorca, Spain in April 1992. The goal of the meeting was to assess the present state of knowledge on the structure and physiology of the bacterium murien sacculus, and develop new hypotheses and strategies to promote further development of the field. The contributions reflect broadly different approaches. Papers discuss structure and chemistry, biosynthesis and maturation, regulation and control of cell wall hydrolases, penicillin interactive proteins, morphogenesis and septum formation, and cell growth. Annotation c. Book News, Inc., Portland, OR (booknews.com
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