Enzymatic acylation of ether and ester lysophospholipids in rat liver microsomes | Zendy

Neumüller W. | Zendy; Fleer E. A. M. | Zendy; Unger C. | Zendy; Eibl H. | Zendy

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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.

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