D-beta-hydroxybutyrate dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the BDH1gene.[1][2][3]
This gene encodes a member of the short-chain dehydrogenase/reductase gene family. The encoded protein forms a homotetrameric lipid-requiring enzyme of the mitochondrial membrane and has a specific requirement for phosphatidylcholine for optimal enzymatic activity. The encoded protein catalyzes the interconversion of acetoacetate and (R)-3-hydroxybutyrate, the two major ketone bodies produced during fatty acid catabolism. Alternatively spliced transcript variants encoding the same protein have been described.[3]
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Green D, Marks AR, Fleischer S, McIntyre JO (1996). "Wild type and mutant human heart (R)-3-hydroxybutyrate dehydrogenase expressed in insect cells". Biochemistry. 35 (25): 8158–65. doi:10.1021/bi952807n. PMID8679568.
Hillier LD, Lennon G, Becker M, et al. (1997). "Generation and analysis of 280,000 human expressed sequence tags". Genome Res. 6 (9): 807–28. doi:10.1101/gr.6.9.807. PMID8889549.
Chelius D, Loeb-Hennard C, Fleischer S, et al. (2000). "Phosphatidylcholine activation of human heart (R)-3-hydroxybutyrate dehydrogenase mutants lacking active center sulfhydryls: site-directed mutagenesis of a new recombinant fusion protein". Biochemistry. 39 (32): 9687–97. doi:10.1021/bi000274z. PMID10933785.
Loeb-Hennard C, McIntyre JO (2000). "(R)-3-hydroxybutyrate dehydrogenase: selective phosphatidylcholine binding by the C-terminal domain". Biochemistry. 39 (39): 11928–38. doi:10.1021/bi000425y. PMID11009606.
