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Characterization of four mammalian 3‐hydroxyacyl‐CoA dehydratases involved in very long‐chain fatty acid synthesis
Author(s) -
Ikeda Mika,
Kanao Yuki,
Yamanaka Masao,
Sakuraba Hiroko,
Mizutani Yukiko,
Igarashi Yasuyuki,
Kihara Akio
Publication year - 2008
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2008.06.007
Subject(s) - dehydratase , biochemistry , yeast , enzyme , biology , chemistry
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.