Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase

被引:11
作者
De Nys, K [1 ]
Meyhi, E [1 ]
Mannaerts, GP [1 ]
Fransen, M [1 ]
Van Veldhoven, PP [1 ]
机构
[1] Katholieke Univ Leuven, Afdeling Farmacol, B-3000 Louvain, Belgium
来源
BIOCHIMICA ET BIOPHYSICA ACTA-MOLECULAR AND CELL BIOLOGY OF LIPIDS | 2001年 / 1533卷 / 01期
关键词
beta-oxidation; docosahexaenoic acid; peroxisome; PTS1; polyunsaturated fatty acid;
D O I
10.1016/S1388-1981(01)00141-X
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 30 778 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. (C) 2001 Elsevier Science B.V. Al rights reserved.
引用
收藏
页码:66 / 72
页数:7
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