Trapping of the substrate-derived acyl enzyme intermediate of purified penicillin-binding protein 1a of Escherichia coli

Purified penicillin-binding protein 1a of Escherichia coli formed an acyl enzyme intermediate with the highly reactive synthetic substrate diacetyl-L-lysyl-D-alanyl-D-lactate at acid pH, although in extremely low yields.

[1]  J. Strominger,et al.  Synthesis of peptidoglycan by high molecular weight penicillin-binding proteins of Bacillus subtilis and Bacillus stearothermophilus. , 1984, The Journal of biological chemistry.

[2]  J. Strominger,et al.  Purification and properties of penicillin-binding proteins 5 and 6 from the dacA mutant strain of Escherichia coli (JE 11191). , 1984, The Journal of biological chemistry.

[3]  F. Ishino,et al.  Formation of hyper-crosslinked peptidoglycan with multiple crosslinkages by a penicillin-binding protein, 1A, of Escherichia coli. , 1982, Biochemical and biophysical research communications.

[4]  J. Strominger,et al.  High-molecular-weight penicillin-binding proteins from membranes of bacilli , 1981, Journal of bacteriology.

[5]  U. Schwarz,et al.  Heterogeneity of newly inserted and preexisting murein in the sacculus of Escherichia coli. , 1981, Proceedings of the National Academy of Sciences of the United States of America.

[6]  J. Strominger,et al.  Purification and properties of penicillin-binding proteins 5 and 6 from Escherichia coli membranes. , 1980, The Journal of biological chemistry.

[7]  A. Wyke,et al.  A mutant of Staphylococcus aureus H lacking penicillin-binding protein 4 and transpeptidase activity in vitro , 1980 .

[8]  F. Ishino,et al.  Dual enzyme activities of cell wall peptidoglycan synthesis, peptidoglycan transglycosylase and penicillin-sensitive transpeptidase, in purified preparations of Escherichia coli penicillin-binding protein 1A. , 1980, Biochemical and biophysical research communications.