| First Author | De Nys K | Year | 2001 |
| Journal | Biochim Biophys Acta | Volume | 1533 |
| Issue | 1 | Pages | 66-72 |
| PubMed ID | 11514237 | Mgi Jnum | J:182412 |
| Mgi Id | MGI:5315368 | Doi | 10.1016/s1388-1981(01)00141-x |
| Citation | De Nys K, et al. (2001) Characterisation of human peroxisomal 2,4-dienoyl-CoA reductase. Biochim Biophys Acta 1533(1):66-72 |
| abstractText | 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. |
