-transparent.png){kind=logo}
The concentration of gamma-hydroxybutyrate (GHB) in brain, kidney, and muscle as well as the clearance of [1-14C]GHB in plasma have been found to be altered by the administration of a number of metabolic intermediates and drugs that inhibit the NADP+-dependent oxidoreductase, "GHB dehydrogenase," an enzyme that catalyzes the oxidation of GHB to succinic semialdehyde. Administration of valproate, salicylate, and phenylacetate, all inhibitors of GHB dehydrogenase, significantly increased the concentration of GHB in brain; salicylate increased GHB concentration in kidney, and alpha-ketoisocaproate increased GHB levels in kidney and muscle. The half-life of [1-14C]GHB in plasma was decreased by D-glucuronate, a compound that stimulates the oxidation of GHB by this enzyme and was increased by a competitive substrate of the enzyme, L-gulonate. The results of these experiments suggest a role for GHB dehydrogenase in the regulation of tissue levels of endogenous GHB.
E E Kaufman, and
T Nelson
March 1997,
Biochimica et biophysica acta,
E E Kaufman, and
T Nelson
January 1969,
Journal de physiologie,
E E Kaufman, and
T Nelson
May 1990,
Biochimica et biophysica acta,
E E Kaufman, and
T Nelson
July 1984,
The Journal of biological chemistry,
E E Kaufman, and
T Nelson
April 2009,
Free radical research,
E E Kaufman, and
T Nelson
May 1966,
Nature,
E E Kaufman, and
T Nelson
February 2002,
Protein science : a publication of the Protein Society,
E E Kaufman, and
T Nelson
June 1984,
Clinical nephrology,
E E Kaufman, and
T Nelson
August 1985,
European journal of biochemistry,
E E Kaufman, and
T Nelson
November 1969,
FEBS letters,
