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Gene Review

BDH1  -  3-hydroxybutyrate dehydrogenase, type 1

Homo sapiens

Synonyms: 3-hydroxybutyrate dehydrogenase, BDH, D-beta-hydroxybutyrate dehydrogenase, mitochondrial, SDR9C1, Short chain dehydrogenase/reductase family 9C member 1
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Disease relevance of BDH1


High impact information on BDH1

  • Heart tissue showed normal LDH and BDH activities, except for some cells surrounding blood vessels, which activity was minimally decreased [5].
  • The HH-Histag-BDH-PC complex (and HH-BDH derived therefrom by enterokinase cleavage) has apparent Michaelis constants (K(m) values) for NAD(+), NADH, (R)-3-hydroxybutyrate (HOB), and acetoacetate (AcAc) similar to those for bovine heart or rat liver BDH [1].
  • (R)-3-Hydroxybutyrate dehydrogenase (BDH) is a lipid-requiring mitochondrial enzyme with a specific requirement of phosphatidylcholine (PC) for function [1].
  • A computed structural model of HH-BDH predicts the two active center sulfhydryls to be C69 (near the adenosine moiety of NAD) and C242 [1].

Biological context of BDH1

  • Analysis of the primary sequence of BDH, as determined by molecular cloning, predicts that lipid binding and substrate specificity are contributed by the C-terminal third of the protein [Marks, A. R., McIntyre, J. O., Duncan, T. M., Erdjument-Bromage, H., Tempst, P., & Fleischer, S. (1992) J. Biol. Chem. 267, 15459-15463] [2].
  • Thus, although C242 (in the C-terminal lipid binding domain of BDH) is close to the active site, it appears to be in a hydrophobic environment and only indirectly defines the substrate binding site at the catalytic center of BDH [1].

Anatomical context of BDH1

  • Monoclonal antibodies (mAbs) have been used to study structure-function relationships of (R)-3-hydroxybutyrate dehydrogenase (BDH) (EC, a lipid-requiring mitochondrial membrane enzyme with an absolute and specific requirement for phosphatidylcholine (PC) for enzymic activity [6].
  • The K(m)s for NAD+ and (R)-3-hydroxybutyrate (R-HOB) of expressed BDH are similar to those for bovine heart or rat liver BDH in mitochondria [2].
  • D-beta-hydroxybutyrate dehydrogenase (BDH) (EC, a membrane enzyme, has been purified to homogeneity from dromedary (Camelus dromedarius) liver mitochondria [7].

Associations of BDH1 with chemical compounds

  • The analogous pyrenyl-PE effects a similar maximal quenching of tryptophan fluorescence for both proteins but with approximately 15-fold lower (K(Q))(eff) (half-maximal quenching at approximately 1.5% pyrenyl-PE) referable to nonspecific interaction of pyrenyl-PE with HH-Histag-BDH or GST-CTBDH [8].
  • In the first step, AcAc and pyruvate are completely reduced, using 3-hydroxybutyrate dehydrogenase (EC and lactate dehydrogenase (EC in the presence of excess NADH at pH 7.5, to beta-hydroxybutyrate and lactate, respectively [9].
  • Phenylpyruvate as well as phenylalanine had no inhibitory effects on ketone-body-catabolizing enzymes, namely 3-hydroxybutyrate dehydrogenase, 3-oxo acid CoA-transferase and acetoacetyl-CoA thiolase, in rat brain [10].
  • Use of terpene-based solvents (Hemo-De, Histoclear, and Shandon and BDH xylene substitutes) in place of xylene in the Ehrlich indole test [11].

Other interactions of BDH1


Analytical, diagnostic and therapeutic context of BDH1

  • With both sulfhydryls derivatized, BDH has minimal activity, but site-directed mutagenesis of C69 and/or C242 now shows that neither of these cysteines is required for PC activation or catalysis (the double mutant, C69A/C242A, is highly active with essentially normal kinetic parameters) [1].
  • We conclude that enzyme histochemistry of LDH and BDH activity on cryostat sections is a useful tool for detecting irreversible myocardial cell damage as early as 2 h reperfusion after ischaemia of the pig heart [5].
  • A chemiluminescence-flow injection analysis of serum 3-hydroxybutyrate using a bioreactor consisting of 3-hydroxybutyrate dehydrogenase and NADH oxidase [13].



  1. Phosphatidylcholine activation of human heart (R)-3-hydroxybutyrate dehydrogenase mutants lacking active center sulfhydryls: site-directed mutagenesis of a new recombinant fusion protein. Chelius, D., Loeb-Hennard, C., Fleischer, S., McIntyre, J.O., Marks, A.R., De, S., Hahn, S., Jehl, M.M., Moeller, J., Philipp, R., Wise, J.G., Trommer, W.E. Biochemistry (2000) [Pubmed]
  2. Wild type and mutant human heart (R)-3-hydroxybutyrate dehydrogenase expressed in insect cells. Green, D., Marks, A.R., Fleischer, S., McIntyre, J.O. Biochemistry (1996) [Pubmed]
  3. D-3-hydroxybutyrate dehydrogenase from Pseudomonas fragi: molecular cloning of the enzyme gene and crystal structure of the enzyme. Ito, K., Nakajima, Y., Ichihara, E., Ogawa, K., Katayama, N., Nakashima, K., Yoshimoto, T. J. Mol. Biol. (2006) [Pubmed]
  4. Biochemical and genetic characterization of a D(-)-3-hydroxybutyrate dehydrogenase from Acidovorax sp. strain SA1. Takanashi, M., Shibahara, T., Shiraki, M., Saito, T. J. Biosci. Bioeng. (2004) [Pubmed]
  5. Combined enzyme histochemical and ultrastructural study on cryostat sections of pig heart to detect early reperfusion damage after ischaemia. Frederiks, W.M., Tukkie, R., Gründeman, P.F., Hoebe, C., Schellens, J.P. J. Pathol. (1995) [Pubmed]
  6. Monoclonal antibodies for structure-function studies of (R)-3-hydroxybutyrate dehydrogenase, a lipid-dependent membrane-bound enzyme. Adami, P., Duncan, T.M., McIntyre, J.O., Carter, C.E., Fu, C., Melin, M., Latruffe, N., Fleischer, S. Biochem. J. (1993) [Pubmed]
  7. Purification and characterization of the D-beta-hydroxybutyrate dehydrogenase from dromedary liver mitochondria. Nasser, B., El Kebbaj, M.S., Cottin, P., Latruffe, N. Comp. Biochem. Physiol. B, Biochem. Mol. Biol. (2002) [Pubmed]
  8. (R)-3-hydroxybutyrate dehydrogenase: selective phosphatidylcholine binding by the C-terminal domain. Loeb-Hennard, C., McIntyre, J.O. Biochemistry (2000) [Pubmed]
  9. Multipoint kinetic method for simultaneously measuring the combined concentrations of acetoacetate-beta-hydroxybutyrate and lactate-pyruvate. Nuwayhid, N.F., Johnson, G.F., Feld, R.D. Clin. Chem. (1989) [Pubmed]
  10. Effect of hyperphenylalaninaemia on lipid synthesis from ketone bodies by rat brain. Patel, M.S., Owen, O.E. Biochem. J. (1976) [Pubmed]
  11. Use of terpene-based solvents (Hemo-De, Histoclear, and Shandon and BDH xylene substitutes) in place of xylene in the Ehrlich indole test. Gubash, S.M., Bennett, E.E. J. Clin. Microbiol. (1989) [Pubmed]
  12. Bioluminescence procedures for the measurement of NAD(P) dependent enzyme catalytic activities in submicrogram quantities of rabbit and human nephron structures. Guder, W.G., Pürschel, S., Vandewalle, A., Wirthensohn, G. J. Clin. Chem. Clin. Biochem. (1984) [Pubmed]
  13. A chemiluminescence-flow injection analysis of serum 3-hydroxybutyrate using a bioreactor consisting of 3-hydroxybutyrate dehydrogenase and NADH oxidase. Tabata, M., Totani, M. Anal. Biochem. (1995) [Pubmed]
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