Accumulation of the prolipoprotein of the Escherichia coli outer membrane caused by benzyloxycarbonylalanine chloromethyl ketone.
Benzyloxycarbonylalanine chloromethyl ketone (Z-Ala-CH2Cl) was found to inhibit the processing of the prolipoprotein, a secretory precursor of the lipoprotein of the Escherichia coli outer membrane. The accumulation of the prolipoprotein in the presence of Z-Ala-CH2Cl was observed both in vivo and in vitro. Z-Ala-CH2Cl did not inhibit the processing of precursors of the other major outer membrane proteins. A preliminary experiment to identify the processing enzyme(s) of the prolipoprotein was carried out with use of Z-[3H]Ala-CH2Cl and revealed that two cytoplasmic membrane proteins with Mr = 78,000 and 46,000 were predominantly labeled.
D000590:Amino Acid Chloromethyl Ketones / Q000494:pharmacology*; D001425:Bacterial Outer Membrane Proteins; D002462:Cell Membrane / Q000187:drug effects / Q000378:metabolism; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D029968:Escherichia coli Proteins; D007700:Kinetics; D008074:Lipoproteins / Q000378:metabolism*; D008565:Membrane Proteins / Q000096:biosynthesis; D011498:Protein Precursors / Q000378:metabolism*
D000590:Amino Acid Chloromethyl Ketones; D001425:Bacterial Outer Membrane Proteins; D029968:Escherichia coli Proteins; D008074:Lipoproteins; C099932:Lpp protein, E coli; D008565:Membrane Proteins; D011498:Protein Precursors; C029959:benzyloxycarbonylalanine chloromethyl ketone