Identification and subcellular localization of apolipoprotein N-acyltransferase in Escherichia coli.
Apolipoprotein N-acyltransferase, the enzyme catalyzing the conversion of apolipoprotein to mature lipoprotein, was detected by an in vitro assay using [35S]methionine-labeled apolipoprotein as the substrate. Triton X-100 solubilized the enzyme, and was required for its activity. The enzyme showed a broad pH optimum (pH 6.5-7.5). N-Acylation of apolipoprotein with ethanol-washed membranes was dependent on exogenous phospholipids, with phosphatidylethanolamine, phosphatidylglycerol and cardiolipin all showing about 10- to 20-times enhancement of the enzyme activity in the delipidated membranes. Incubation of apolipoprotein with [3H]palmitate-labeled membranes resulted in the incorporation of [3H]palmitate into lipoprotein. The enzyme was found to be enriched in the inner membrane and in the inner membrane/outer membrane mixed fractions of the E. coli cell envelope.
Gupta
S D
SD
Department of Microbiology, Uniformed Services University of the Health Sciences, Bethesda, MD 20889-4799.
Wu
H C
HC
D000217:Acyltransferases / Q000032:analysis*; D001053:Apolipoproteins / Q000378:metabolism*; D003902:Detergents / Q000494:pharmacology; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007700:Kinetics; D010743:Phospholipids / Q000378:metabolism
D001053:Apolipoproteins; D003902:Detergents; D010743:Phospholipids; D000217:Acyltransferases; C068902:apolipoprotein N-acyltransferase