Abstract
The tetrahydropteridine-requiring enzyme in rat liver microsomes that oxidatively cleaved the O-alkyl moiety of glycerolipids does not utilize alkyl glycerolipid substrates that contain carbonyl, acyl, or phosphate groups on the glycerol portion. However, the ether linkage in rac and 1-, 2-, or 3-isomeric forms of alkylglycerols and 1-alkyl- sn-glycero-3-phosphorylethanolamine is readily cleaved by the pteridine-requiring enzyme. Therefore, it appears that hydrolytic enzymes play an essential role in conjunction with the cleavage enzyme in the regulation of cellular levels of O-alkyl moieties in glycerolipids.
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