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Applied and Environmental Microbiology, October 2006, p. 6825-6828, Vol. 72, No. 10
0099-2240/06/$08.00+0 doi:10.1128/AEM.00829-06
Copyright © 2006, American Society for Microbiology. All Rights Reserved.
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Department of Biochemistry and Molecular Genetics, University of Alabama at Birmingham, Birmingham, Alabama
Received 7 April 2006/ Accepted 16 July 2006
Synthetic peptides corresponding to portions of group B streptococcal peptidoglycan were used to show that the endopeptidase activity of bacteriophage B30 lysin cleaves between D-Ala in the stem peptide and L-Ala in the cross bridge and that the minimal peptide sequence cleaved is DL-
-Glu-Lys-D-Ala-Ala-Ala. The only glycosidase activity present is that of N-acetyl-ß-D-muramidase.
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