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Updated: Jul 19, 2026

A New Screening Method for the Directed Evolution of Thermostable Bacteriolytic Enzymes
Published on: November 7, 2012
Endopeptidase and glycosidase activities of the bacteriophage B30 lysin
John R Baker1, Chengbao Liu, Shengli Dong
1Department of Biochemistry & Molecular Genetics, MCLM 552, University of Alabama at Birmingham, 1530 3rd Ave. S, Birmingham, AL 35294-0005, USA.
Abstract:
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-gamma-Glu-Lys-D-Ala-Ala-Ala. The only glycosidase activity present is that of N-acetyl-beta-D-muramidase.
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