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Delta(3,5)-Delta(2,4)-dienoyl-CoA isomerase from rat liver - Molecular characterization

Filppula, SA; Yagi, AI; Kilpelainen, SH; Novikov, D; FitzPatrick, DR; Vihinen, Mauno LU ; Valle, D and Hiltunen, JK (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)
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author
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
273
issue
1
pages
349 - 355
publisher
ASBMB
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
2013-06-28 14:30:15
date last changed
2017-01-01 04:24:59
@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    = {ASBMB},
  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},
  volume       = {273},
  year         = {1998},
}