Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase from rat liver - Molecular characterization
(1998) In Journal of Biological Chemistry 273(1). p.349-355- 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 Delta(3)-Delta(5) to the Delta(2)-Delta(4) 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... (More)
- 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 Delta(3)-Delta(5) to the Delta(2)-Delta(4) 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 Delta(3,5)-Delta(2,4)-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. (Less)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/3852665
- author
- Filppula, SA ; Yagi, AI ; Kilpelainen, SH ; Novikov, D ; FitzPatrick, DR ; Vihinen, Mauno LU ; Valle, D and Hiltunen, JK
- publishing date
- 1998
- type
- Contribution to journal
- publication status
- published
- subject
- in
- Journal of Biological Chemistry
- volume
- 273
- issue
- 1
- pages
- 349 - 355
- publisher
- American Society for Biochemistry and Molecular Biology
- external identifiers
-
- wos:000071295600053
- scopus:0031594712
- ISSN
- 1083-351X
- DOI
- 10.1074/jbc.273.1.349
- language
- English
- LU publication?
- no
- id
- 59bf7e13-612d-4ef8-ab99-f319c69543bc (old id 3852665)
- date added to LUP
- 2016-04-01 11:39:36
- date last changed
- 2022-01-26 08:16:55
@article{59bf7e13-612d-4ef8-ab99-f319c69543bc, 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 Delta(3)-Delta(5) to the Delta(2)-Delta(4) 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 Delta(3,5)-Delta(2,4)-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.}}, author = {{Filppula, SA and Yagi, AI and Kilpelainen, SH and Novikov, D and FitzPatrick, DR and Vihinen, Mauno and Valle, D and Hiltunen, JK}}, issn = {{1083-351X}}, language = {{eng}}, number = {{1}}, pages = {{349--355}}, publisher = {{American Society for Biochemistry and Molecular Biology}}, series = {{Journal of Biological Chemistry}}, title = {{Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase from rat liver - Molecular characterization}}, url = {{http://dx.doi.org/10.1074/jbc.273.1.349}}, doi = {{10.1074/jbc.273.1.349}}, volume = {{273}}, year = {{1998}}, }