Identification of Four Families of Peptidoglycan Lytic Transglycosylases (original) (raw)

Abstract

The lytic transglycosylases are a class of autolysins which cleave the bacterial cell wall heteropolymer peptidoglycan (murein) to facilitate its biosynthesis and turnover. A search of the National Center for Biotechnology Information (NCBI) databases using the primary sequences of the six characterized lytic transglycosylases of Escherichia coli, a membrane-bound form of the enzyme from Pseudomonas aeruginosa, and the endolysins of λ bacteriophage permitted the identification of a total of 127 known and hypothetical enzymes from a wide variety of bacteria and bacteriophage. These amino acid sequences have been arranged into four families based on alignments, and consensus motifs have been identified. Family 1 represents a superfamily comprising 86 sequences which are subdivided into five (1A–1E) subfamilies.

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Authors and Affiliations

  1. Department of Microbiology, University of Guelph, Guelph, Ontario N1G 2W1, Canada
    Neil T. Blackburn & Anthony J. Clarke

Authors

  1. Neil T. Blackburn
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  2. Anthony J. Clarke
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Received: 27 March 2000 / Accepted: 6 July 2000

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Blackburn, N.T., Clarke, A. Identification of Four Families of Peptidoglycan Lytic Transglycosylases.J Mol Evol 52, 78–84 (2001). https://doi.org/10.1007/s002390010136

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