Endopeptidase and Glycosidase Activities of the Bacteriophage B30 Lysin
Author(s) -
John Baker,
Chengbao Liu,
Shengli Dong,
David G. Pritchard
Publication year - 2006
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.00829-06
Subject(s) - lysin , endopeptidase , bacteriophage , glycoside hydrolase , peptide , muramidase , peptide sequence , biochemistry , biology , peptidoglycan , chemistry , enzyme , escherichia coli , gene
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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