Characterisation of the peptidoglycan hydrolases of Listeria monocytogenes EGD

A M McLaughlan; S J Foster

doi:10.1111/j.1574-6968.1997.tb10421.x

Characterisation of the peptidoglycan hydrolases of Listeria monocytogenes EGD

FEMS Microbiol Lett. 1997 Jul 1;152(1):149-54. doi: 10.1111/j.1574-6968.1997.tb10421.x.

Authors

A M McLaughlan¹, S J Foster

Affiliation

¹ Department of Molecular Biology and Biotechnology, University of Sheffield, UK.

PMID: 9228781
DOI: 10.1111/j.1574-6968.1997.tb10421.x

Abstract

The peptidoglycan hydrolase profile of Listeria monocytogenes EGD has been characterised under a variety of environmental and physiological conditions, using renaturing sodium dodecyl sulfate-polyacrylamide gel electrophoresis. The profiles show activities ranging from 29 to 186 kDa. The 186-kDa enzyme was only observable under specific medium and aeration conditions. The enzyme activities show differential substrate specificity and sensitivity to incubation conditions. The peptidoglycan hydrolase profile of several different Listeria strains was also compared.

Publication types

Research Support, Non-U.S. Gov't

MeSH terms

Listeria monocytogenes / enzymology*
Mitomycin / pharmacology
N-Acetylmuramoyl-L-alanine Amidase / metabolism*
Phenylmethylsulfonyl Fluoride / pharmacology
Substrate Specificity

Substances

Mitomycin
Phenylmethylsulfonyl Fluoride
N-Acetylmuramoyl-L-alanine Amidase