z-logo
open-access-imgOpen Access
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.

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here
Accelerating Research

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom