Isolation and characterization of a hydroxyacid-oxoacid transhydrogenase from rat kidney mitochondria.
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+.
Kaufman
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Department of Health and Human Services, National Institute of Mental Health, Bethesda, Maryland 20892.
Nelson
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Fales
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Levin
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D020155:3-Hydroxybutyric Acid; D000818:Animals; D002854:Chromatography, Paper; D008401:Gas Chromatography-Mass Spectrometry; D005977:Glutarates / Q000378:metabolism; D006863:Hydrogen-Ion Concentration; D006885:Hydroxybutyrates / Q000378:metabolism; D007668:Kidney / Q000201:enzymology* / Q000648:ultrastructure; D007700:Kinetics; D008928:Mitochondria / Q000201:enzymology; D009243:NAD / Q000378:metabolism; D009249:NADP / Q000378:metabolism; D051381:Rats; D012978:Sodium Oxybate / Q000378:metabolism; D013997:Time Factors; D005680:gamma-Aminobutyric Acid / Q000031:analogs & derivatives / Q000378:metabolism
D005977:Glutarates; D006885:Hydroxybutyrates; D009243:NAD; C019417:alpha-hydroxyglutarate; D009249:NADP; D005680:gamma-Aminobutyric Acid; D012978:Sodium Oxybate; C009338:succinic semialdehyde; D020155:3-Hydroxybutyric Acid