Correction: Primary and predicted secondary structure of the actinomadura R39 extracellular DD-peptidase, a penicillin-binding protein (PBP) related to the escherichia coli PBP4 (Biochemical Journal(1992)282(786))

peer reviewe

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

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

Modular Design of the Enterococcus Hirae Muramidase-2 and Streptococcus Faecalis Autolysin

The mature forms of the extracellular muramidase-2 of Enterococcus hirae and Streptococcus faecalis autolysin have very similar primary structures. Each consists of an active-site-containing N-terminal domain fused to a multiple-repeat C-terminal domain. Polypeptide segments occurring at equivalent places in these two bacterial wall lytic enzymes have homologues in two phage lysozymes and in three functionally unrelated proteins, illustrating the principle that protein molecules frequently are constructed from modules that are linked in a single polypeptide chain