Enzymatic acylation of ether and ester lysophospholipids in rat liver microsomes.
The acylation of lysophospholipids by rat liver acyltransferases was studied. A comparison between ester and ether lysophospholipids as substrates revealed large differences in substrate properties. For instance, oleic acid from oleoyl-CoA and arachidonic acid from arachidonoyl-CoA were not incorporated into 1-O-octadecyl-sn-glycero-3-phosphocholine under experimental conditions that allowed an optimal transfer of oleic acid and arachidonic acid to 1-O-palmitoyl-sn-glycero-3-phosphocholine. However, we observed an acyl-CoA-independent transfer of arachidonic acid from 1-O-stearoyl-2-O-arachidonoyl-sn-glycero-3-phosphoinositol to 1-O-octadecyl-sn-glycero-3-phosphocholine.
Neumüller
W
W
Max-Planck-Institut für biophysikalische Chemie, Göttingen, Federal Republic of Germany.
Fleer
E A
EA
Unger
C
C
Eibl
H
H
D000215:Acylation; D000818:Animals; D000970:Antineoplastic Agents / Q000378:metabolism; D008099:Liver / Q000201:enzymology*; D008244:Lysophosphatidylcholines / Q000378:metabolism; D008246:Lysophospholipids / Q000378:metabolism*; D008861:Microsomes / Q000378:metabolism; D010742:Phospholipid Ethers / Q000378:metabolism*; D051381:Rats; D013379:Substrate Specificity
D000970:Antineoplastic Agents; D008244:Lysophosphatidylcholines; D008246:Lysophospholipids; D010742:Phospholipid Ethers; C006065:We 201