Identification of four families of peptidoglycan lytic transglycosylases

J Mol Evol. 2001 Jan;52(1):78-84. doi: 10.1007/s002390010136.

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 lambda 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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Motifs
  • Amino Acid Sequence
  • Bacterial Proteins / chemistry
  • Bacterial Proteins / genetics
  • Bacteriophage lambda / enzymology
  • Bacteriophage lambda / genetics
  • Databases, Factual
  • Endopeptidases / chemistry
  • Endopeptidases / genetics
  • Escherichia coli / enzymology
  • Escherichia coli / genetics*
  • Evolution, Molecular
  • Glycosyltransferases / chemistry*
  • Glycosyltransferases / classification
  • Glycosyltransferases / genetics*
  • Hexosyltransferases / chemistry*
  • Hexosyltransferases / classification
  • Hexosyltransferases / genetics*
  • Molecular Sequence Data
  • Molecular Structure
  • Multigene Family*
  • Phylogeny
  • Pseudomonas aeruginosa / enzymology
  • Pseudomonas aeruginosa / genetics*

Substances

  • Bacterial Proteins
  • Glycosyltransferases
  • Hexosyltransferases
  • murein transglycosylase
  • Endopeptidases
  • endolysin