Using a combination of database-mining and functional characterization, we have identified a component of the polyunsaturated fatty acid (PUFA) elongase. Co-expression of this elongating activitiy with fatty acid desaturases has allowed us to heterologously reconstitute the PUFA biosynthetic pathway. Both these enzymes (desaturases and elongase components) have undergone gene-duplication events which provide a paradigm for the diverged nature of PUFA biosynthetic activities.

Keywords:
arachidonic acid, desaturase, fatty acid elongation, PUFA, polyunsaturated fatty acid, ORF, open reading frame
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© 2000 Biochemical Society
2000
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