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Journal of Lipid Research, Vol 25, 185-188, Copyright © 1984 by Lipid Research, Inc.

ARTICLES

Utilization of different fatty acyl-CoA thioesters by serine palmitoyltransferase from rat brain

AH Merrill Jr and RD Williams

Serine palmitoyltransferase (EC 2.3.1.50) catalyzes the first unique reaction of sphingolipid biosynthesis. Activities were determined with different fatty acyl-CoA substrates to describe the range of long-chain bases that could be made by rat brain microsomes. The activities were greatest with palmitoyl-CoA and palmitelaidoyl-CoA, followed by fully saturated homologs differing from these by only one carbon atom, and diminished considerably as the alkyl-chain length increased or decreased, or with the presence of a cis-double bond. These characteristics explain the predominance of long-chain bases with 18 carbon atoms in brain sphingolipids, and account for the minor variants such as the C17- and C20-long chain bases.
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