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- Name help_outline (3E,5Z,8Z,11Z,14Z)-eicosapentaenoyl-CoA Identifier CHEBI:85090 Charge -4 Formula C41H60N7O17P3S InChIKeyhelp_outline PHIGJHMEMQBUMA-MHBLKGGESA-J SMILEShelp_outline CCCCC\C=C/C\C=C/C\C=C/C\C=C/C=C/CC(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
- Name help_outline (2E,4E,8Z,11Z,14Z)-eicosapentaenoyl-CoA Identifier CHEBI:85091 Charge -4 Formula C41H60N7O17P3S InChIKeyhelp_outline VEOYVBZJFWTPAJ-AKGIYQAYSA-J SMILEShelp_outline CCCCC\C=C/C\C=C/C\C=C/CC\C=C\C=C\C(=O)SCCNC(=O)CCNC(=O)[C@H](O)C(C)(C)COP([O-])(=O)OP([O-])(=O)OC[C@H]1O[C@H]([C@H](O)[C@@H]1OP([O-])([O-])=O)n1cnc2c(N)ncnc12 2D coordinates Mol file for the small molecule Search links Involved in 1 reaction(s) Find molecules that contain or resemble this structure Find proteins in UniProtKB for this molecule
Cross-references
RHEA:45224 | RHEA:45225 | RHEA:45226 | RHEA:45227 | |
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Reaction direction help_outline | undefined | left-to-right | right-to-left | bidirectional |
UniProtKB help_outline |
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Related reactions help_outline
More general form(s) of this reaction
Publications
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Delta3,5-delta2,4-dienoyl-CoA isomerase from rat liver. Molecular characterization.
Filppula S.A., Yagi A.I., Kilpeleainen S.H., Novikov D., Fitzpatrick D.R., Vihinen M., Valle D., Hiltunen J.K.
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 th ... >> 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 Delta3-Delta5 to the Delta2-Delta4 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 Delta3,5-Delta2,4-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
J. Biol. Chem. 273:349-355(1998) [PubMed] [EuropePMC]
This publication is cited by 2 other entries.