Abstract
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 activity 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.
Publication types
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Research Support, Non-U.S. Gov't
MeSH terms
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Acetyltransferases / chemistry
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Acetyltransferases / genetics
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Acetyltransferases / metabolism*
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Amino Acid Sequence
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Animals
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Caenorhabditis elegans / enzymology*
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Caenorhabditis elegans / genetics
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Fatty Acid Desaturases / metabolism*
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Fatty Acid Elongases
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Fatty Acids, Unsaturated / biosynthesis*
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Genetic Engineering
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Genome
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Molecular Sequence Data
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Open Reading Frames
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Sequence Alignment
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Sequence Homology, Amino Acid
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Substrate Specificity
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gamma-Linolenic Acid / metabolism
Substances
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Fatty Acids, Unsaturated
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gamma-Linolenic Acid
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Fatty Acid Desaturases
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Acetyltransferases
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Fatty Acid Elongases