RGD Reference Report - Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein. - Rat Genome Database

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Novel fatty acid beta-oxidation enzymes in rat liver mitochondria. II. Purification and properties of enoyl-coenzyme A (CoA) hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein.

Authors: Uchida, Y  Izai, K  Orii, T  Hashimoto, T 
Citation: Uchida Y, etal., J Biol Chem. 1992 Jan 15;267(2):1034-41.
RGD ID: 1600572
Pubmed: PMID:1730633   (View Abstract at PubMed)

Long-chain 3-hydroxyacyl-CoA dehydrogenase was extracted from the washed membrane fraction of frozen rat liver mitochondria with buffer containing detergent and then was purified. This enzyme is an oligomer with a molecular mass of 460 kDa and consisted of 4 mol of large polypeptide (79 kDa) and 4 mol of small polypeptides (51 and 49 kDa). The purified enzyme preparation was concluded to be free from the following enzymes based on marked differences in behavior of the enzyme during purification, molecular masses of the native enzyme and subunits, and immunochemical properties: enoyl-CoA hydratase, short-chain 3-hydroxyacyl-CoA dehydrogenase, peroxisomal enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase bifunctional protein, and mitochondrial and peroxisomal 3-ketoacyl-CoA thiolases. The purified enzyme exhibited activities toward enoyl-CoA hydratase and 3-ketoacyl-CoA thiolase together with the long-chain 3-hydroxyacyl-CoA dehydrogenase activity. The carbon chain length specificities of these three activities of this enzyme differed from those of the other enzymes. Therefore, it is concluded that this enzyme is not long-chain 3-hydroxyacyl-CoA dehydrogenase; rather, it is enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase/3-ketoacyl-CoA thiolase trifunctional protein.



Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
HadhaRatfatty acid beta-oxidation  IDA  RGD 
HadhbRatfatty acid beta-oxidation  IDA  RGD 

Cellular Component

  
Object SymbolSpeciesTermQualifierEvidenceWithNotesSourceOriginal Reference(s)
HadhaRatmitochondrial fatty acid beta-oxidation multienzyme complex  IDA  RGD 
HadhbRatmitochondrial fatty acid beta-oxidation multienzyme complex  IDA  RGD 

Molecular Function

  

Molecular Pathway Annotations    Click to see Annotation Detail View

RGD Manual Annotations


  
Objects Annotated

Genes (Rattus norvegicus)
Hadha  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha)
Hadhb  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit beta)

Genes (Mus musculus)
Hadha  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha)
Hadhb  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit beta)

Genes (Homo sapiens)
HADHA  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit alpha)
HADHB  (hydroxyacyl-CoA dehydrogenase trifunctional multienzyme complex subunit beta)


Additional Information