[36] N-terminal glyceride-cysteine modification of membrane penicillinases in gram-positive bacteria
- 1 January 1984
- book chapter
- Published by Elsevier
- Vol. 106, 365-368
- https://doi.org/10.1016/0076-6879(84)06038-9
Abstract
No abstract availableThis publication has 12 references indexed in Scilit:
- .beta.-Lactamase III of Bacillus cereus 569: membrane lipoprotein and secreted proteinBiochemistry, 1983
- Characterization of the membrane .beta.-lactamase in Bacillus cereus 569/H/9Biochemistry, 1983
- Construction of penP delta 1, Bacillus licheniformis 749/C beta-lactamase lacking site for lipoprotein modification. Expression in Escherichia coli and Bacillus subtilis.Journal of Biological Chemistry, 1983
- Accumulation of glyceride‐modified pre‐penicillinase of Bacillus licheniformis in Escherichia coli treated with globomycinFEBS Letters, 1983
- Prolipoprotein signal peptidase in Escherichia coli is distinct from the M13 procoat protein signal peptidase.Journal of Biological Chemistry, 1982
- Mechanism of signal peptide cleavage in the biosynthesis of the major lipoprotein of the Escherichia coli outer membrane.Journal of Biological Chemistry, 1982
- ProteolipidsAnnual Review of Biochemistry, 1981
- The hydrophobic membrane penicillinase of Bacillus licheniformis 749/C. Characterization of the hydrophilic enzyme and phospholipopeptide produced by trypsin cleavage.Journal of Biological Chemistry, 1976
- Covalent Binding of Lipid to ProteinEuropean Journal of Biochemistry, 1973
- Affinity chromatography purification of penicillinase of Bacillus licheniformis 749/C and its use to measure turnover of the cell bound enzymeBiochemical and Biophysical Research Communications, 1973