Influence of cationic peptides on the activity of the autolytic endo-beta-N-acetylglucosaminidase of Staphylococcus simulans 22

FEMS Microbiology Letters
G Bierbaum, H G Sahl

Abstract

The peptidoglycan hydrolyzing endo-beta-N-acetylglucosaminidase of Staphylococcus simulans 22 is not able to attack intact cell walls of S. simulans 22, but hydrolyzes cell walls of Micrococcus luteus and soluble peptidoglycan chains of S. simulans 22. Hydrolysis of cell walls of M. luteus is activated in presence of organic cations such as poly-L-lysine (n = 17) and the peptide antibiotics Pep 5 and nisin, whereas hydrolysis of soluble peptidoglycan chains is not influenced. High concentrations of inorganic cations inhibit enzyme activity. These effects are discussed with respect to the cationic nature of the enzyme (pI greater than 9.5) and the regulation of the concerted action of the N-acetylmuramoyl-L-alanine amidase and the glucosaminidase during S. simulans 22 autolysis in vivo.

References

Jan 1, 1985·Annales De L'Institut Pasteur. Microbiology·G D ShockmanD L Dolinger
Nov 10, 1972·Biochimica Et Biophysica Acta·J M OrtizR C Berkeley
Sep 8, 1971·Journal of the American Chemical Society·E Gross, J L Morell
Jan 1, 1983·Annual Review of Microbiology·G D Shockman, J F Barrett

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Citations

Jan 22, 2014·International Journal of Medical Microbiology : IJMM·Friedrich GötzThilo Stehle
Jan 15, 1994·European Journal of Biochemistry·R JackH G Sahl
Jun 15, 1995·European Journal of Biochemistry·H G SahlG Bierbaum
Apr 24, 2007·The Journal of Antimicrobial Chemotherapy·Emiliano SalvucciFernando Sesma

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