Human Δ3,Δ2-enoyl-CoA isomerase, type 2: a structural enzymology study on the catalytic role of its ACBP domain and helix-10
Author:
Affiliation:
1. Biocenter Oulu and Faculty of Biochemistry and Molecular Medicine; University of Oulu; Finland
2. Department of Biomedicine; University of Bergen; Norway
3. Theodor Boveri Institute of Biosciences (Biocenter); University of Würzburg; Germany
Funder
European Community's Seventh Framework Programme
BioStruct-X
Academy of Finland
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/febs.13179/fullpdf
Reference55 articles.
1. Functional redundancy of mitochondrial enoyl-CoA isomerases in the oxidation of unsaturated fatty acids;Weeghel;FASEB J,2012
2. β-oxidation strategies for the metabolism of a wide variety of acyl-CoA esters;Hiltunen;Biochim Biophys Acta,2000
3. Mitochondrial 2,4-dienoyl-CoA reductase deficiency in mice results in severe hypoglycemia with stress intolerance and unimpaired ketogenesis;Miinalainen;PLoS Genet,2009
4. Disruption of mitochondrial β-oxidation of unsaturated fatty acids in the 3,2-trans-enoyl-CoA isomerase-deficient mouse;Janssen;J Biol Chem,2002
5. Peroxisomal Δ3-cis-Δ2-trans-enoyl-CoA isomerase encoded by ECI1 is required for growth of the yeast Saccharomyces cerevisiae on unsaturated fatty acids;Gurvitz;J Biol Chem,1998
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