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Journal of Molecular Evolution

, Volume 52, Issue 1, pp 78–84 | Cite as

Identification of Four Families of Peptidoglycan Lytic Transglycosylases

  • Neil T. Blackburn
  • Anthony J. Clarke
Article

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.

Key words: Sequence comparison — Autolysin — Lytic transglycosylase — Lysozyme 

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Copyright information

© Springer-Verlag New York Inc. 2001

Authors and Affiliations

  • Neil T. Blackburn
    • 1
  • Anthony J. Clarke
    • 1
  1. 1.Department of Microbiology, University of Guelph, Guelph, Ontario N1G 2W1Canada

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