Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase.
Based on the primary structure of the rat peroxisomal 2,4-dienoyl-CoA reductase (M. Fransen, P.P. Van Veldhoven, S. Subramani, Biochem. J. 340 (1999) 561-568), the cDNA of the human counterpart was cloned. It contained an open reading frame of 878 bases encoding a protein of 291 amino acids (calculated molecular mass 30778 Da), being 83% identical to the rat reductase. The gene, encompassing nine exons, is located at chromosome 16p13. Bacterially expressed poly(His)-tagged reductase was active not only towards short and medium chain 2,4-dienoyl-CoAs, but also towards 2,4,7,10,13,16,19-docosaheptaenoyl-CoA. Hence, the reductase does not seem to constitute a rate limiting step in the peroxisomal degradation of docosahexaenoic acid. The reduction of docosaheptaenoyl-CoA, however, was severely decreased in the presence of albumin.
De Nys
K
K
Afdeling Farmacologie, Katholieke Universiteit Leuven, Campus Gasthuisberg, Herestraat 49, B-3000, Leuven, Belgium.
Meyhi
E
E
Mannaerts
G P
GP
Fransen
M
M
Van Veldhoven
P P
PP
D000214:Acyl Coenzyme A / Q000378:metabolism; D000595:Amino Acid Sequence; D001483:Base Sequence; D003001:Cloning, Molecular; D018076:DNA, Complementary / Q000096:biosynthesis / Q000737:chemistry; D004281:Docosahexaenoic Acids / Q000378:metabolism; D044943:Fatty Acid Desaturases / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D006801:Humans; D007700:Kinetics; D008969:Molecular Sequence Data; D044925:Oxidoreductases Acting on CH-CH Group Donors; D020675:Peroxisomes / Q000201:enzymology*
D000214:Acyl Coenzyme A; D018076:DNA, Complementary; C417225:hexadienoyl-coenzyme A; D004281:Docosahexaenoic Acids; C040351:2,4-decadienoyl-coenzyme A; D044943:Fatty Acid Desaturases; D044925:Oxidoreductases Acting on CH-CH Group Donors; C100153:2,4-dienoyl-CoA reductase