Endopeptidase and glycosidase activities of the bacteriophage B30 lysin.
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.
Baker
John R
JR
Department of Biochemistry & Molecular Genetics, MCLM 552, University of Alabama at Birmingham, 1530 3rd Ave. S, Birmingham, AL 35294-0005, USA.
Liu
Chengbao
C
Dong
Shengli
S
Pritchard
David G
DG
D001435:Bacteriophages / Q000201:enzymology*; D010450:Endopeptidases / Q000378:metabolism*; D006026:Glycoside Hydrolases / Q000378:metabolism*; D009088:Mucoproteins / Q000378:metabolism*; D009238:N-Acetylmuramoyl-L-alanine Amidase; D010455:Peptides / Q000378:metabolism
D009088:Mucoproteins; D010455:Peptides; C010393:lysin, gastropoda; D006026:Glycoside Hydrolases; D010450:Endopeptidases; D009238:N-Acetylmuramoyl-L-alanine Amidase