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Oxidation of γ‐Hydroxybutyrate to Succinic Semialdehyde by a Mitochondrial Pyridine Nucleotide‐Independent Enzyme
Author(s) -
Kaufman Elaine E.,
Nelson Thomas,
Miller David,
Stadlan Noam
Publication year - 1988
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1988.tb03071.x
Subject(s) - nad+ kinase , biochemistry , enzyme , cytosol , oxidoreductase , mitochondrion , dehydrogenase , chemistry , kidney , biology , stereochemistry , endocrinology
An antibody that inhibits over 95% of the cytosolic NADP + ‐dependent 7‐hydroxybutyrate (GHB) dehydrogenase activity of either rat brain or kidney was found to inhibit only approximately 50% of the conversion of [1– 14 C]GHB to 14 CO 2 by rat kidney homogenate. A similar result was obtained with sodium valproate, a potent inhibitor of GHB dehydrogenase. The mitochondrial fraction from rat brain and kidney was found to catalyze the conversion of [1– 14 C]GHB to 14 CO 2 . The dialyzed mitochondrial fraction also catalyzed the oxidation of GHB to succinic semialdehyde (SSA) in a reaction that did not require added NAD + or NADP T and which was not inhibited by sodium valproate. The enzyme from the mitochondrial fraction which converts GHB to SSA appears to be distinct from the NADP + ‐depen‐dent cytosolic oxidoreductase which catalyzes this reaction.