6533b839fe1ef96bd12a5d10

RESEARCH PRODUCT

Characterization of two d-β-hydroxybutyrate dehydrogenase populations in heavy and light mitochondria from jerboa (Jaculus orientalis) liver

M'hammed Saïd El KebbajMostafa KabineDriss MountassifNorbert Latruffe

subject

Gene isoformHEPESchemistry.chemical_classificationbiologyPhysiologyMitochondria LiverRodentiaDehydrogenaseMitochondrionbiology.organism_classificationBiochemistryMolecular biologyHydroxybutyrate DehydrogenaseKineticschemistry.chemical_compoundEnzymeBiochemistrychemistryKetone bodiesAnimalsInner mitochondrial membraneMolecular BiologyJaculus orientalis

description

Mitochondrial membrane-bound and phospholipid-dependent D-beta-hydroxybutyrate dehydrogenase (BDH) (EC 1.1.1.30), a ketone body converting enzyme in mitochondria, has been studied in two populations of mitochondria (heavy and light) of jerboa (Jaculus orientalis) liver. The results reveal significant differences between the BDH of the two mitochondrial populations in terms of protein expression, kinetic parameters and physico-chemical properties. These results suggest that the beta-hydroxybutyrate dehydrogenases from heavy and light mitochondria are isoform variants. These differences in BDH distribution could be the consequence of cell changes in the lipid composition of the inner mitochondrial membrane of heavy and light mitochondria. These changes could modify both BDH insertion and BDH lipid-dependent catalytic properties.

yearjournalcountryeditionlanguage
2005-04-07Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology
https://doi.org/10.1016/j.cbpb.2005.11.019