Open AccessThe Specificity Requirements of Bacteriophage T4 Lysozyme
Author(s) -
KLEPPE Gunnar,
VASSTRAND Endre,
JENSEN Harald B.
Publication year - 1981
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1981.tb05648.x
Subject(s) - peptidoglycan , lysozyme , bacillus cereus , bacteriophage , muramidase , chemistry , acetylation , biochemistry , acetic anhydride , bacillus megaterium , peptide , enzyme , biology , bacteria , catalysis , escherichia coli , gene , genetics
Bacillus cereus peptidoglycan with N‐unsubstituted glucosamine residues was insensitive to treatment with bacteriophage T4 lysozyme. After N ‐acetylation with acetic anhydride, T4 lysozyme cleared solutions of the peptidoglycan and reducting sugars were liberated. The digestion products were mainly of high molecular weight, since the peptidoglycan is peptide cross‐linked to a great extent. N ‐Propylation did not convert the partially N‐unsubstituted peptidoglycan to a sensitive form. It is concluded that the acetamido groups are required for binding and/or catalysis by T4 lysozyme.