Δ3,5-Δ2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization

S. A. Filppula, A. I. Yagi, S. H. Kilpeläinen, D. Novikov, D. R. FitzPatrick, M. Vihinen, David Valle, J. K. Hiltunen

Research output: Contribution to journalArticle

Abstract

rECH1, a recently identified rat cDNA (FitzPatrick, D. R., Germain-Lee, E., and Valle, D. (1995) Genomics 27, 457-466) encodes a polypeptide belonging to the hydratase/isomerase superfamily. We modeled the structure of rECH1 based on rat mitochondrial 2-enoyl-CoA hydratase 1. The model predicts that rECH1p has the hydratase fold in the core domain and two domains for interaction with other subunits. When we incubated 3,5,8,11,14- eicosapentaenoyl-CoA with purified rECH1p, the spectral data suggested a switching of the double bonds from the Δ35 to the Δ24 positions. This was confirmed by demonstrating that the product was a valid substrate for 2,4-dienoyl-CoA reductase. These results indicate that rECH1p is Δ3,52,4-dienoyl-CoA isomerase. Subcellular fractionation and immunoelectron microscopy using antibodies to a synthetic polypeptide derived from the C terminus of rECH1p showed that rECH1p is located in the matrix of both mitochondria and peroxisomes in rat liver. Consistent with these observations, the 36,000-Da rECH1p has a potential N-terminal mitochondrial targeting signal as well as a C-terminal peroxisomal targeting signal type 1. Transport of the protein into the mitochondria with cleavage of the targeting signal results in a mature mitochondrial form with a molecular mass of 32,000 Da; transport to peroxisomes yields a protein of 36,000 Da.

Original languageEnglish (US)
Pages (from-to)349-355
Number of pages7
JournalJournal of Biological Chemistry
Volume273
Issue number1
DOIs
StatePublished - Jan 2 1998

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Isomerases
Coenzyme A
Liver
Hydro-Lyases
Rats
Mitochondria
Peroxisomes
2,4-dienoyl-CoA reductase
Enoyl-CoA Hydratase 2
Peptides
Immunoelectron Microscopy
Molecular mass
Fractionation
Genomics
Carrier Proteins
Microscopic examination
Complementary DNA
Antibodies
Substrates
Proteins

ASJC Scopus subject areas

  • Biochemistry

Cite this

Filppula, S. A., Yagi, A. I., Kilpeläinen, S. H., Novikov, D., FitzPatrick, D. R., Vihinen, M., ... Hiltunen, J. K. (1998). Δ3,5-Δ2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization. Journal of Biological Chemistry, 273(1), 349-355. https://doi.org/10.1074/jbc.273.1.349

Δ3,5-Δ2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization. / Filppula, S. A.; Yagi, A. I.; Kilpeläinen, S. H.; Novikov, D.; FitzPatrick, D. R.; Vihinen, M.; Valle, David; Hiltunen, J. K.

In: Journal of Biological Chemistry, Vol. 273, No. 1, 02.01.1998, p. 349-355.

Research output: Contribution to journalArticle

Filppula, SA, Yagi, AI, Kilpeläinen, SH, Novikov, D, FitzPatrick, DR, Vihinen, M, Valle, D & Hiltunen, JK 1998, 'Δ3,5-Δ2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization', Journal of Biological Chemistry, vol. 273, no. 1, pp. 349-355. https://doi.org/10.1074/jbc.273.1.349
Filppula SA, Yagi AI, Kilpeläinen SH, Novikov D, FitzPatrick DR, Vihinen M et al. Δ3,5-Δ2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization. Journal of Biological Chemistry. 1998 Jan 2;273(1):349-355. https://doi.org/10.1074/jbc.273.1.349
Filppula, S. A. ; Yagi, A. I. ; Kilpeläinen, S. H. ; Novikov, D. ; FitzPatrick, D. R. ; Vihinen, M. ; Valle, David ; Hiltunen, J. K. / Δ3,5-Δ2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization. In: Journal of Biological Chemistry. 1998 ; Vol. 273, No. 1. pp. 349-355.
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AU - Yagi, A. I.

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AU - Novikov, D.

AU - FitzPatrick, D. R.

AU - Vihinen, M.

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