6533b7dafe1ef96bd126f5e9
RESEARCH PRODUCT
Cloning and tissue expression of two cDNAs encoding the peroxisomal 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase in the guinea pig liver
Mustapha Cherkaoui-malkiNorbert LatruffeGerald HoeflerFrançoise Cairasubject
DNA ComplementaryGuinea PigsMolecular Sequence DataBiophysicsGene ExpressionDehydrogenasePeroxisomeBiologyKidneyMicrobodiesBiochemistryStructural BiologyComplementary DNAGeneticsAnimalsPhosphofructokinase 2Amino Acid SequenceRNA MessengerNorthern blotCloning Molecular2-Enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenaseBifunctional enzymeEnoyl-CoA HydrataseMolecular BiologyCloningBase Sequence3-Hydroxyacyl CoA DehydrogenasesSequence Analysis DNACell BiologyPeroxisomeEnoyl-CoA hydrataseBlotting NorthernGuinea pigMolecular biology3-Hydroxyacyl-CoA DehydrogenaseLiverBiochemistrycDNAdescription
Abstract The 2-enoyl-CoA hydratase/3-hydroxyacyl-CoA dehydrogenase (HD) is the second enzyme of the peroxisomal β-oxidation pathway. In human and rat, only one HD mRNA has been so far detected in the liver. This paper reports for the first time in a mammal species, the guinea pig, the cloning and sequencing of two cDNAs encoding an HD. The 3,274 nucleotide-cDNA is a strictly identical but longer copy of the 2,494 nucleotide-form. A 2,178 by-open reading frame encodes a protein of 726 amino acids ( M r 79.3 kDa) with the peroxisomal-targeting signal (tripeptide SKL) at the carboxyterminus. Northern blot analysis of HD mRNA identified three mRNAs of respective sizes 3.5, 2.6 and 1.6 kb in the guinea pig liver and kidneys.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 1996-01-02 | FEBS Letters |