Formation of hyper-crosslinked peptidoglycan with multiple crosslinkages by a penicillin-binding protein, 1A, of Escherichia coli
- 1 June 1982
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 106 (4), 1175-1182
- https://doi.org/10.1016/0006-291x(82)91236-0
Abstract
No abstract availableThis publication has 10 references indexed in Scilit:
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- Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1ABiochemical and Biophysical Research Communications, 1980
- Identification of peptide-cross-linked trisdisaccharide peptide trimers in murein of Escherichia coliJournal of Bacteriology, 1980
- Purified penicillin binding proteins 1Bs from Escherichia coli membrane showing activities of both peptidoglycan polymerase and peptidoglycan crosslinking enzyme.Agricultural and Biological Chemistry, 1979
- Purification of penicillin-insensitive DD-endopeptidase, a new cell wall peptidoglycan-hydrolyzing enzyme in Escherichia coli, and its inhibition by deoxyribonucleic acidsBiochemical and Biophysical Research Communications, 1978
- On the process of cellular division in Escherichia coli: a series of mutants of E. coli altered in the penicillin-binding proteins.Proceedings of the National Academy of Sciences, 1978
- Thermosensitive mutation in Escherichia coli simultaneously causing defects in penicillin-binding protein-1Bs and in enzyme activity for peptidoglycan synthesis in vitro.Proceedings of the National Academy of Sciences, 1977