Lysophosphatidic acid acyltransferase (LPAAT) participates in the second step of oil biosynthesis and is expected to play a key role in altering the quantity of long-chain polyunsaturated fatty acids produced in oils of oleaginous organisms. The present application provides a nucleic acid fragment (identified as "LPAAT2") isolated from Mortierella alpina encoding a LPAAT homolog that is suitable for use in the manufacture of oils enriched in omega fatty acids in oleaginous organisms. Most desirably, the substrate specificity of the instant LPAAT2 will be particularly useful to enable accumulation of long-chain PUFAs having chain lengths equal to or greater than C.sub.20 in oleaginous yeast, such as Yarrowia lipolytica.

 
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< Mortierella alpina diacylglycerol acyltransferase for alteration of polyunsaturated fatty acids and oil content in oleaginous organisms

< Acyltransferase regulation to increase the percent of polyunsaturated fatty acids in total lipids and oils of oleaginous organisms

> Mortierella alpina glycerol-3-phosphate o-acyltransferase for alteration of polyunsaturated fatty acids and oil content in oleaginous organisms

> Mk2 interacting proteins

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