Utilization of different fatty acyl-CoA thioesters by serine palmitoyltransferase from rat brain.
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.
D000214:Acyl Coenzyme A / Q000378:metabolism*; D000217:Acyltransferases / Q000378:metabolism*; D000818:Animals; D001921:Brain / Q000201:enzymology / Q000378:metabolism*; D005260:Female; D008861:Microsomes / Q000201:enzymology / Q000378:metabolism*; D010171:Palmitoyl Coenzyme A / Q000378:metabolism; D051381:Rats; D011915:Rats, Inbred BUF; D051102:Serine C-Palmitoyltransferase; D013107:Sphingolipids / Q000096:biosynthesis
D000214:Acyl Coenzyme A; D013107:Sphingolipids; C017585:oleoyl-coenzyme A; D010171:Palmitoyl Coenzyme A; C017725:stearoyl-coenzyme A; D000217:Acyltransferases; D051102:Serine C-Palmitoyltransferase