Characterization of four mammalian 3-hydroxyacyl-CoA dehydratases involved in very long-chain fatty acid synthesis

Very long-chain fatty acids are produced through a four-step cycle. However, the 3-hydroxyacyl-CoA dehydratase catalyzing the third step in mammals has remained unidentified. Mammals have four candidates, HACD1–4, based on sequence similarities to the recently identified yeast Phs1, although HACD3 a...

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Bibliographic Details
Published in:FEBS letters 2008-07, Vol.582 (16), p.2435-2440
Main Authors: Ikeda, Mika, Kanao, Yuki, Yamanaka, Masao, Sakuraba, Hiroko, Mizutani, Yukiko, Igarashi, Yasuyuki, Kihara, Akio
Format: Article
Language:English
Subjects:
3-Hydroxyacyl-CoA dehydratase
Acetyltransferases - metabolism
Cell Line
EGFP
ELOVL
Endoplasmic Reticulum - enzymology
enhanced green fluorescent protein
fatty acid
Fatty Acids - biosynthesis
Fatty Acids - chemistry
HACD
HeLa Cells
Humans
Hydro-Lyases - metabolism
Lipid
RNA, Messenger - metabolism
Saccharomyces cerevisiae Proteins - metabolism
synthetic complete
Tissue Distribution
Very long-chain fatty acid
VLCFA
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Summary:Very long-chain fatty acids are produced through a four-step cycle. However, the 3-hydroxyacyl-CoA dehydratase catalyzing the third step in mammals has remained unidentified. Mammals have four candidates, HACD1–4, based on sequence similarities to the recently identified yeast Phs1, although HACD3 and HACD4 share relatively weak similarity. We demonstrate that all four of these human proteins are indeed 3-hydroxyacyl-CoA dehydratases, in growth suppression experiments using a PHS1-shut off yeast strain and/or in vitro 3-hydroxypalmitoyl-CoA dehydratase assays. HACD proteins exhibit distinct tissue-expression patterns. We also establish that HACD proteins interact with the condensation enzymes ELOVL1–7, with some preferences.
ISSN:0014-5793
1873-3468
DOI:10.1016/j.febslet.2008.06.007