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Substrate specificity of mouse and human delta9‐desaturases
Author(s) -
Miyazaki Makoto,
Ntambi James M
Publication year - 2006
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.20.5.a1345-a
Subject(s) - substrate (aquarium) , substrate specificity , chemistry , biophysics , biology , biochemistry , enzyme , ecology
Delta9‐desaturase catalyzes the desaturation of saturated fatty acids to monounsaturated fatty acids in mammalian cells. Currently, there are four known enzymatic isoforms in mice (mSCD1‐4) and two in humans (hSCD1, hSCD5). The physiological role for multiple SCD isoforms and their substrate specificities are currently unknown. We report here distinct substrate specificities for the human and mouse SCD isoforms. Each SCD isoform was able to complement the OLE‐1 mutation in S. cerevisiae through heterologous expression of transgenic SCD. Fatty acid analysis showed that the desaturases have distinct preferences for saturated fatty acyl‐CoA substrates in yeast and mammalian cells. Mouse SCD1, SCD2 and SCD4 desaturate both C18 and C16, although with greater preference for C18:0 than C16:0. Mouse SCD3 selectively uses C16:0 as a substrate. Human SCD1 like mouse SCD1 and 2 utilize both C18:0 and C16:0 as substrates. Human SCD5 prefers C18:0 as substrate. This substrate preference helps to explain distinct physiological roles for each SCD isoform. Supported by NIH (RO1‐DK62388)