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Uptake and acylation of 2-acyl-lysophospholipids by Escherichia coli
Author(s) -
Li-Chung Hsu,
Suzanne Jackowski,
Charles O. Rock
Publication year - 1989
Publication title -
journal of bacteriology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.652
H-Index - 246
eISSN - 1067-8832
pISSN - 0021-9193
DOI - 10.1128/jb.171.2.1203-1205.1989
Subject(s) - acylation , escherichia coli , acyltransferase , acyl carrier protein , biology , biochemistry , phospholipid , acyl group , extracellular , acyltransferases , acyl coa , membrane , enzyme , biosynthesis , chemistry , organic chemistry , gene , alkyl , catalysis
The efficiency of extracellular 2-acyl-lysophospholipid incorporation into Escherichia coli membranes and the acyl donor utilized to acylate the 2-acyl-lysophospholipid was determined. Exogenous 2-acyl-lysophospholipids were acylated via the acyl-acyl carrier protein synthetase/2-acylglycerophosphoethanolamine acyltransferase pathway. The maximum extent of 2-acyl-lysophospholipid incorporation into the membrane was approximately 2.5% of the normal phospholipid biosynthetic rate.

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