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Defining Substrate Specificities for Lipase and Phospholipase Candidates
Published on: November 23, 2016
Enzymatic acylation of ether and ester lysophospholipids in rat liver microsomes
W Neumüller1, E A Fleer, C Unger
1Max-Planck-Institut für biophysikalische Chemie, Göttingen, Federal Republic of Germany.
Abstract:
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.
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