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Occurrence of an acyl‐CoA:1‐acylglycerophosphorylcholine acyltransferase in plant mitochondria
Author(s) -
Testet Eric,
Bessoule Jean-Jacques,
Mongrand Sébastien,
Guillot-Salomon Thérèse,
Cantrel Catherine,
Cassagne Claude
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01293-8
Subject(s) - lysophosphatidylcholine , acyltransferase , mitochondrion , endoplasmic reticulum , biochemistry , phosphatidylcholine , acyl coa , chemistry , acyltransferases , moiety , enzyme , organelle , phospholipid , membrane , biology , biosynthesis , stereochemistry
In the presence of oleoyl‐CoA, purified and intact mitochondria from potato tuber formed phosphatidylcholine from labeled lysophosphatidylcholine. The labeled oleoyl moiety of the acyl‐CoA was also incorporated in the absence of exogenous lysolipids, such incorporation being largely increased by the addition of exogenous lysophosphatidylcholine. In the presence of various other lysophospholipids, no synthesis of the corresponding phospholipids was observed, suggesting a high specificity of the acyltransferase towards the acyl acceptor. This enzyme was chiefly located in the outer membrane of mitochondria. These results indicate that any acylglycerophosphorylcholine transferred from the endoplasmic reticulum to mitochondria may be acylated to phosphatidylcholine.