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Gene Review

Bdh1  -  3-hydroxybutyrate dehydrogenase, type 1

Rattus norvegicus

Synonyms: 3-hydroxybutyrate dehydrogenase, BDH, Bdh, D-beta-hydroxybutyrate dehydrogenase, mitochondrial
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Disease relevance of Bdh1

  • These results suggest that the decrease in BDH content in hepatoma cells results from a decrease in functional BDH-mRNA [1].
  • The expressed activity in E. coli could be inhibited in a dose-dependent manner by BDH antiserum [2].
  • Hypothyroidism, on the other hand, affects BDH activity in neither heart nor liver [3].
  • A rat liver bacteriophage lambda expression library was probed using polyclonal antibodies raised to purified rat liver D-beta-hydroxybutyrate dehydrogenase (BDH) [2].

High impact information on Bdh1

  • BDH activity in normal rat hepatocyte mitochondria was 321 nmol/min/mg, which was greatly reduced to 10.7 nmol/min/mg and 1.7 nmol/min/mg in H4-II-EC3 and RLT-3C cell mitochondria, respectively [1].
  • Quantitation of D-beta-hydroxybutyrate dehydrogenase (BDH) in normal rat hepatocytes was compared with that in two rat hepatoma cell lines, H4-II-EC3 and RLT-3C [1].
  • These results suggest that there is a reciprocal correlation between BDH activity and cell growth and protein synthesis rates [1].
  • A computer-based comparison of the amino acid sequence of BDH with other reported sequences reveals a homology with the superfamily of short-chain alcohol dehydrogenases, which are distinct from the classical zinc-dependent alcohol dehydrogenases [4].
  • The largest clone contained 1435 base pairs and encoded the entire amino acid sequence of mature BDH and the leader peptide of precursor BDH [4].

Chemical compound and disease context of Bdh1

  • The coupling of a decrease in BDH activity with an increase in activity of succinyl-CoA: acetoacetyl-CoA transferase in hepatoma cells may play a role in generating additional energy required for the rapid growth of tumor cells [1].

Biological context of Bdh1

  • 5. The concentrations of hydroxyacyl-CoA dehydrogenase and carnitine palmitoyltransferase were equivalent to the more active enzymes of the tricarboxylic acid cycle, indicating the capacity for extensive lipid oxidation, and the presence of 3-hydroxybutyrate dehydrogenase suggests that these tissues can also oxidize ketone bodies [5].
  • The process of reactivation of BDH by phospholipids, which follows a second-order mechanism, reveals that (1) at least 2 mol of lecithins is essential for the reactivation of the enzyme, and (2) the enzyme contains two dependent binding sites for lecithins [6].
  • This result indicates that in vivo the control of the expression of the BDH gene by insulin is mainly transcriptional and/or post-transcriptional (mRNA stability) [7].
  • Alkylation at the active site of the D-3-hydroxybutyrate dehydrogenase (BDH), a membrane phospholipid-dependent enzyme, by 3-chloroacetyl pyridine adenine dinucleotide (3-CAPAD) [8].
  • With regard to the inhibitory effect on BDH and GDH following cadmium intoxication, it does not appear to be imputable to lipid peroxidation since in vitro investigations indicate that the presence of vitamin E does not remove the inhibition at all [9].

Anatomical context of Bdh1


Associations of Bdh1 with chemical compounds


Other interactions of Bdh1


Analytical, diagnostic and therapeutic context of Bdh1

  • In vitro translations of isolated RNA followed by immunoprecipitation revealed that the increase in BDH activity and content was correlated with an increase in the level of functional BDH-mRNA in both liver and brain [21].
  • Antiserum against rat liver BDH inhibited both enzymes to an equivalent extent in a titration assay [22].
  • Adrenalectomy and ovariectomy increase liver mRNA content and polypeptide level, as well as activity of BDH [23].
  • The expression of mitochondrial membrane-bound D-beta-hydroxybutyrate dehydrogenase (BDH), a ketone body-converting enzyme, has been estimated by two immunological techniques: immunohistofluorescence and Western blotting [24].


  1. Regulation of D-beta-hydroxybutyrate dehydrogenase in rat hepatoma cell lines. Zhang, W.W., Churchill, S., Lindahl, R., Churchill, P. Cancer Res. (1989) [Pubmed]
  2. Cloning and expression of a functional rat liver D-beta-hydroxybutyrate dehydrogenase-beta-galactosidase fusion protein in Escherichia coli. Churchill, S., Churchill, P. Biochem. Cell Biol. (1991) [Pubmed]
  3. Concerning the decreased D-3-hydroxybutyrate dehydrogenase activity in the liver and heart of hyperthyroid rats. Lippolis, R., Morini, P., Conserva, A.R., Casalino, E., Landriscina, C. Mol. Cell. Biochem. (1990) [Pubmed]
  4. Primary structure of rat liver D-beta-hydroxybutyrate dehydrogenase from cDNA and protein analyses: a short-chain alcohol dehydrogenase. Churchill, P., Hempel, J., Romovacek, H., Zhang, W.W., Brennan, M., Churchill, S. Biochemistry (1992) [Pubmed]
  5. Activity and androgenic control of enzymes associated with the tricarboxylic acid cycle, lipid oxidation and mitochondrial shuttles in the epididymis and epididymal spermatozoa of the rat. Brooks, D.E. Biochem. J. (1978) [Pubmed]
  6. Kinetic aspects of the role of phospholipids in D-beta-hydroxybutyrate dehydrogenase activity. el Kebbaj, M.S., Latruffe, N. Arch. Biochem. Biophys. (1986) [Pubmed]
  7. Variations of specific mRNA and polypeptide contents of rat liver D-beta-hydroxybutyrate dehydrogenase during an experimental diabetes mellitus. Bailly, A., Lone, Y.C., Latruffe, N. Biochimie (1990) [Pubmed]
  8. Alkylation at the active site of the D-3-hydroxybutyrate dehydrogenase (BDH), a membrane phospholipid-dependent enzyme, by 3-chloroacetyl pyridine adenine dinucleotide (3-CAPAD). el Kebbaj, M.S., Latruffe, N. Biochimie (1997) [Pubmed]
  9. Enzyme activity alteration by cadmium administration to rats: the possibility of iron involvement in lipid peroxidation. Casalino, E., Sblano, C., Landriscina, C. Arch. Biochem. Biophys. (1997) [Pubmed]
  10. Reactivation of D-beta-hydroxybutyrate dehydrogenase with short-chain lecithins: stoichiometry and kinetic mechanism. Cortese, J.D., Vidal, J.C., Churchill, P., McIntyre, J.O., Fleischer, S. Biochemistry (1982) [Pubmed]
  11. Decreased rate of ketone-body oxidation and decreased activity of D-3-hydroxybutyrate dehydrogenase and succinyl-CoA:3-oxo-acid CoA-transferase in heart mitochondria of diabetic rats. Grinblat, L., Pacheco Bolaños, L.F., Stoppani, A.O. Biochem. J. (1986) [Pubmed]
  12. Regional enzyme development in rat brain. Enzymes of energy metabolism. Leong, S.F., Clark, J.B. Biochem. J. (1984) [Pubmed]
  13. Metabolism of glucose, glutamine, long-chain fatty acids and ketone bodies by murine macrophages. Newsholme, P., Curi, R., Gordon, S., Newsholme, E.A. Biochem. J. (1986) [Pubmed]
  14. Effect of phenylalanine metabolites on the activities of enzymes of ketone-body utilization in brain of suckling rats. Benavides, J., Gimenez, C., Valdivieso, F., Mayor, F. Biochem. J. (1976) [Pubmed]
  15. A histochemical study of the distribution of beta-hydroxybutyrate dehydrogenase in developing rat cerebellum. Gesink, D.S., Wilson, J.E. J. Neurochem. (1985) [Pubmed]
  16. 3-Hydroxyisobutyrate dehydrogenase, an impurity in commercial 3-hydroxybutyrate dehydrogenase. Worrall, E.B., Gassain, S., Cox, D.J., Sugden, M.C., Palmer, T.N. Biochem. J. (1987) [Pubmed]
  17. Glycemia, ketonemia, and brain enzymes of ketone body utilization in suckling and adult rats undernourished from intrauterine life. Escrivá, F., Rodríguez, C., Pascual-Leone, A.M. J. Neurochem. (1985) [Pubmed]
  18. Origin of the ammonia found in protein-free extracts of rat-liver mitochondria and rat hepatocytes. Wanders, R.J., Hoek, J.B., Tager, J.M. Eur. J. Biochem. (1980) [Pubmed]
  19. Distribution of enzymes of fatty acid and ketone body metabolism in periportal and perivenous rat-liver tissue. Katz, N.R., Fischer, W., Giffhorn, S. Eur. J. Biochem. (1983) [Pubmed]
  20. Thyroid hormone regulation of nuclear-encoded mitochondrial inner membrane polypeptides of the liver. Joste, V., Goitom, Z., Nelson, B.D. Eur. J. Biochem. (1989) [Pubmed]
  21. Developmental regulation of D-beta-hydroxybutyrate dehydrogenase in rat liver and brain. Zhang, W.W., Churchill, S., Churchill, P. FEBS Lett. (1989) [Pubmed]
  22. Comparison of D-beta-hydroxybutyrate dehydrogenase from rat liver and brain mitochondria. Zhang, W.W., Redman, K., Churchill, S., Churchill, P. Biochem. Cell Biol. (1990) [Pubmed]
  23. Post-transcriptional analysis of rat mitochondrial D-3-hydroxybutyrate dehydrogenase control through development and physiological stages. Bailly, A., Lone, Y.C., Latruffe, N. Biol. Cell (1991) [Pubmed]
  24. Immunological study of the tissue expression of D-beta-hydroxybutyrate dehydrogenase, a ketone body-converting enzyme. Coquard, C., Adami, P., Cherkaoui-Malki, M., Fellmann, D., Latruffe, N. Biol. Cell (1987) [Pubmed]
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