Characterisation of the peptidoglycan hydrolases of Listeria monocytogenes EGD.
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.
McLaughlan
A M
AM
Department of Molecular Biology and Biotechnology, University of Sheffield, UK.
Foster
S J
SJ
D008089:Listeria monocytogenes / Q000201:enzymology*; D016685:Mitomycin / Q000494:pharmacology; D009238:N-Acetylmuramoyl-L-alanine Amidase / Q000378:metabolism*; D010664:Phenylmethylsulfonyl Fluoride / Q000494:pharmacology; D013379:Substrate Specificity
D016685:Mitomycin; D010664:Phenylmethylsulfonyl Fluoride; D009238:N-Acetylmuramoyl-L-alanine Amidase