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Murine 12( R )‐lipoxygenase: functional expression, genomic structure and chromosomal localization 1
Author(s) -
Krieg Peter,
Siebert Malte,
Kinzig Andreas,
Bettenhausen Rainer,
Marks Friedrich,
Fürstenberger Gerhard
Publication year - 1999
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/s0014-5793(99)00196-9
Subject(s) - recombinant dna , lipoxygenase , linoleic acid , microbiology and biotechnology , exon , complementary dna , intron , gene , biology , arachidonic acid , chemistry , biochemistry , enzyme , fatty acid
A cDNA, recently cloned (by Krieg et al. (1998)) from mouse skin, was shown to encode a 12( R )‐lipoxygenase. When expressed in HEK cells, the recombinant protein converted methyl arachidonate into the corresponding 12‐HETE ester which was shown to be the R ‐enantiomer by chiral phase chromatography. Neither arachidonic acid nor linoleic acid were substrates for the recombinant protein. The structure of the 12( R )‐lipoxygenase gene is unique among all animal lipoxygenases in that it is divided into 15 exons and 14 introns spanning approximately 12.5 kb. By interspecific backcross analysis, the 12( R )‐lipoxygenase gene was localized to the central region of mouse chromosome 11.