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.
D000215:Acylation; D000217:Acyltransferases / Q000378:metabolism*; D001426:Bacterial Proteins; D002250:Carbon Radioisotopes; D002352:Carrier Proteins; D004151:Dipeptides / Q000378:metabolism*; D004926:Escherichia coli / Q000378:metabolism*; D006602:Hexosyltransferases / Q000378:metabolism*; D007773:Lactates / Q000378:metabolism*; D009097:Multienzyme Complexes / Q000378:metabolism*; D002267:Muramoylpentapeptide Carboxypeptidase; D046915:Penicillin-Binding Proteins; D010458:Peptidyl Transferases / Q000378:metabolism*; D011485:Protein Binding
D001426:Bacterial Proteins; D002250:Carbon Radioisotopes; D002352:Carrier Proteins; D004151:Dipeptides; D007773:Lactates; D009097:Multienzyme Complexes; D046915:Penicillin-Binding Proteins; C043631:diacetyllysylalanine lactate; D000217:Acyltransferases; D010458:Peptidyl Transferases; D006602:Hexosyltransferases; D002267:Muramoylpentapeptide Carboxypeptidase