Publication | Open Access
Isolation and characterization of a hydroxyacid-oxoacid transhydrogenase from rat kidney mitochondria.
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Citations
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References
1988
Year
Aldo-keto ReductaseHydroxyacid-oxoacid TranshydrogenaseMitochondrial BiologyRedox BiologyOxoacid-dependent OxidationOxidative StressBiosynthesisMitochondrial StructureMitochondrial FractionAlcohol DehydrogenasesRat Kidney MitochondriaAldehyde DehydrogenaseBiochemistryMetabolomicsPharmacologyRat KidneyMitochondrial FunctionPhysiologyCatabolismMetabolismMedicineCarbonyl Metabolism
A transhydrogenase that catalyzes the oxoacid-dependent oxidation of specific hydroxyacids has been found in rat kidney, liver, and brain. The hydroxyacids that have been found to be substrates for this enzyme are gamma-hydroxybutyrate, D-alpha-hydroxyglutarate, and L-beta-hydroxybutyrate. The oxoacids that are the best substrates for this enzyme are alpha-ketoglutarate and succinic semialdehyde; alpha-ketoadipate and oxalacetate are also substrates. This enzyme is located in the mitochondrial fraction of the cell and is not dependent on added NAD+ or NADP+.
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