Premium
Enzymatic acylation of ether and ester lysophospholipids in rat liver microsomes
Author(s) -
Neumüller W.,
Fleer E. A. M.,
Unger C.,
Eibl H.
Publication year - 1987
Publication title -
lipids
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.601
H-Index - 120
eISSN - 1558-9307
pISSN - 0024-4201
DOI - 10.1007/bf02535535
Subject(s) - arachidonic acid , acylation , phosphocholine , chemistry , acyltransferases , biochemistry , oleic acid , substrate (aquarium) , ether , enzyme , stereochemistry , phospholipid , organic chemistry , biosynthesis , phosphatidylcholine , biology , catalysis , membrane , ecology
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.