Abstract
Lysozymes produced in host cells infected with bacteriophages T3 and T5 were found to have the same enzymatic specificity toward the peptidoglycan from Escherichia coli as T7 phage lysozyme, which has been shown to be an N-acetylmuramyl-L-alanine amidase.
MeSH Terms
Acetylglucosamine/metabolism
Amidohydrolases/metabolism
Arginine/metabolism
Bacterial Proteins/biosynthesis
Carbon Radioisotopes
Coliphages/enzymology
DNA Viruses
Diaminopimelic Acid/metabolism
Electrophoresis, Polyacrylamide Gel
Escherichia coli/metabolism
Lipoproteins/biosynthesis
Muramidase/biosynthesis,metabolism
Peptidoglycan/biosynthesis,metabolism
Tritium
Chemicals
Bacterial Proteins
Carbon Radioisotopes
Lipoproteins
Peptidoglycan
Tritium
Diaminopimelic Acid
Arginine
Muramidase
Amidohydrolases
Acetylglucosamine
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
DeMartini M
Halegoua S
Inouye M
References (3)
3 references, click to expand
-
Bacteriophage T7 lysozyme is an N-acetylmuramyl-L-alanine amidase.
J Biol Chem. 1973 Oct 25;248(20):7247-52
PMID: 4582731
-
Amino acid sequence of T2 phage lysozyme.
J Mol Biol. 1968 Oct 14;37(1):213-23
PMID: 4939037
-
First-step-transfer deoxyribonucleic acid of bacteriophage T5.
Bacteriol Rev. 1968 Sep;32(3):227-42
PMID: 4879238