Escherichia coli murein-DD-endopeptidase insensitive to beta-lactam antibiotics.
A novel endopeptidase degrading the peptide cross-links in sacculi has been isolated from Escherichia coli and purified to homogeneity. The enzyme has a molecular weight of 30,000 and, in contrast to already known enzymes of similar specificity, remains fully active in the presence of beta-lactam antibiotics. In addition, it is exceptional in being inhibited by single-stranded deoxyribonucleic acid and by some polynucleotides. The possible role of the enzyme in cell division is discussed.
D010450:Endopeptidases / Q000302:isolation & purification / Q000378:metabolism*; D004926:Escherichia coli / Q000201:enzymology*; D007700:Kinetics; D010400:Penicillin G / Q000494:pharmacology*; D010457:Peptidoglycan; D011131:Polyribonucleotides / Q000494:pharmacology
D010457:Peptidoglycan; D011131:Polyribonucleotides; D010450:Endopeptidases; D010400:Penicillin G