RGD Reference Report - Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver. - Rat Genome Database

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Functional characterization of Delta3,Delta2-enoyl-CoA isomerases from rat liver.

Authors: Zhang, D  Yu, W  Geisbrecht, BV  Gould, SJ  Sprecher, H  Schulz, H 
Citation: Zhang D, etal., J Biol Chem. 2002 Mar 15;277(11):9127-32. Epub 2002 Jan 7.
RGD ID: 2306199
Pubmed: PMID:11781327   (View Abstract at PubMed)
DOI: DOI:10.1074/jbc.M112228200   (Journal Full-text)

The degradation of unsaturated fatty acids by beta-oxidation involves Delta(3),Delta(2)-enoyl-CoA isomerases (enoyl-CoA isomerases) that catalyze 3-cis --> 2-trans and 3-trans --> 2-trans isomerizations of enoyl-CoAs and the 2,5 --> 3,5 isomerization of dienoyl-CoAs. An analysis of rat liver enoyl-CoA isomerases revealed the presence of a monofunctional enoyl-CoA isomerase (ECI) in addition to mitochondrial enoyl-CoA isomerase (MECI) in mitochondria, whereas peroxisomes contain ECI and multifunctional enzyme 1 (MFE1). Thus ECI, which previously had been described as peroxisomal enoyl-CoA isomerase, was found to be present in both peroxisomes and mitochondria. This enzyme seems to be identical with mitochondrial long-chain enoyl-CoA isomerase (Kilponen, J.M., Palosaari, P.M., and Hiltunen, J.K. 1990. Biochem. J. 269, 223-226). All three hepatic enoyl-CoA isomerases have broad chain length specificities but are distinguishable by their preferences for one of the three isomerization reactions. MECI is most active in catalyzing the 3-cis --> 2-trans isomerization; ECI has a preference for the 3-trans --> 2-trans isomerization, and MFE1 is the optimal isomerase for the 2,5 --> 3,5 isomerization. A functional characterization based on substrate specificities and total enoyl-CoA isomerase activities in rat liver leads to the conclusion that the 3-cis --> 2-trans and 2,5 --> 3,5 isomerizations in mitochondria are catalyzed overwhelmingly by MECI, whereas ECI contributes significantly to the 3-trans --> 2-trans isomerization. In peroxisomes, ECI is predicted to be the dominant enzyme for the 3-cis --> 2-trans and 3-trans --> 2-trans isomerizations of long-chain intermediates, whereas MFE1 is the key enzyme in the 2,5 --> 3,5 isomerization.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Eci1Ratfatty acid beta-oxidation involved_inIDA PMID:11781327UniProt 
Eci2Ratfatty acid beta-oxidation  IDA  RGD 
EhhadhRatfatty acid beta-oxidation involved_inIDA PMID:11781327UniProt 

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
Eci1Ratmitochondrion located_inIDA PMID:11781327UniProt 
Eci2Ratperoxisome  IDA  RGD 
EhhadhRatperoxisome located_inIDA PMID:11781327UniProt 

Molecular Function

  

Objects Annotated

Genes (Rattus norvegicus)
Eci1  (enoyl-CoA delta isomerase 1)
Eci2  (enoyl-CoA delta isomerase 2)
Ehhadh  (enoyl-CoA hydratase and 3-hydroxyacyl CoA dehydrogenase)

Objects referenced in this article
Gene SPN sialophorin Homo sapiens
Gene Spn sialophorin Rattus norvegicus

Additional Information