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. 1969 Oct;100(1):254–259. doi: 10.1128/jb.100.1.254-259.1969

Specificity of a Bacteriolytic Enzyme from Pseudomonas aeruginosa1

Marvin Lache 1,2,2, Walter R Hearn 1,2, Judith W Zyskind 1,2,2, Donald J Tipper 1,2, Jack L Strominger 1,2,3
PMCID: PMC315386  PMID: 4981057

Abstract

A bacteriolytic enzyme isolated from shake-flask cultures of Pseudomonas aeruginosa and capable of lysing cells of Staphylococcus aureus was purified approximately 500-fold by passage through diethylaminoethyl cellulose and chromatography on carboxymethyl-cellulose. The purified enzyme was shown to act as an endopeptidase, cleaving the pentaglycine cross-bridges of the cell wall peptidoglycan at d-alanyl-glycine and glycyl-glycine linkages with the release of di−, tri−, and tetraglycine fragments. Release of NH2-alanine indicated weak N-acetylmuramyl-l-alanine amidase activity, but most of the residual peptide remained attached to the glycan. No hydrolysis of the glycan occurred. The lytic spectrum of the enzyme toward a variety of other cell walls of known peptidoglycan composition indicated relatively high specificity for peptidoglycans with polyglycine bridges.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

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