Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli.

@article{Lommatzsch1997OuterML,
  title={Outer membrane localization of murein hydrolases: MltA, a third lipoprotein lytic transglycosylase in Escherichia coli.},
  author={J{\"u}rgen Lommatzsch and Markus F. Templin and Anke R M Kraft and Waldemar Vollmer and J. - V. H{\"o}ltje},
  journal={Journal of bacteriology},
  year={1997},
  volume={179 17},
  pages={5465-70}
}
Lytic transglycosylases are a unique lysozyme-like class of murein hydrolases believed to be important for growth of Escherichia coli. A membrane-bound lytic transglycosylase with an apparent molecular mass of 38 kDa, which was designated Mlt38, has previously been purified and characterized (A. Ursinus and J.-V. Höltje, J. Bacteriol. 176:338-343, 1994). On the basis of four tryptic peptides, the gene mltA was mapped at 63 min on the chromosomal map of E. coli K-12 and cloned by reverse… CONTINUE READING

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Microbial peptidoglycan (murein) hydrolases, p. 131–166

  • G. D. Shockman, J.-V. Höltje
  • 1994

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