Entry - *603063 - 3-HYDROXYBUTYRATE DEHYDROGENASE 1; BDH1 - OMIM
 
* 603063

3-HYDROXYBUTYRATE DEHYDROGENASE 1; BDH1


Alternative titles; symbols

3-HYDROXYBUTYRATE DEHYDROGENASE; BDH


HGNC Approved Gene Symbol: BDH1

Cytogenetic location: 3q29     Genomic coordinates (GRCh38): 3:197,509,783-197,573,343 (from NCBI)


TEXT

Cloning and Expression

(R)-3-hydroxybutyrate dehydrogenase (BDH; EC 1.1.1.30) is a mitochondrial membrane enzyme with an absolute and specific requirement for phosphatidylcholine, which acts as an allosteric activator of BDH enzymatic activity. BDH has served as a prototype for lipid-requiring enzymes. By screening a human heart cDNA library with degenerate oligonucleotides based on peptide sequences from purified bovine BDH, Marks et al. (1992) isolated cDNAs encoding BDH. The deduced 343-amino acid protein contains a 46-residue leader peptide, which is cleaved to produce the mature form. Sequence analysis revealed that the first two-thirds of the BDH protein is homologous to short-chain alcohol dehydrogenases (SCADHs), with the homology encompassing the putative coenzyme-binding and active sites of the SCADHs; this region of BDH also has the predicted secondary structure motif of alternating alpha-helices and beta-sheets that is characteristic of SCADHs. The authors suggested that the remainder of the BDH protein contains elements that form the substrate- and lipid-binding sites. Northern blot analysis revealed that BDH is expressed in rabbit heart tissue.


Mapping

Persson et al. (2009) stated that the BDH gene maps to chromosome 3q29.


REFERENCES

  1. Marks, A. R., McIntyre, J. O., Duncan, T. M., Erdjument-Bromage, H., Tempst, P., Fleischer, S. Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart. J. Biol. Chem. 267: 15459-15463, 1992. [PubMed: 1639787, related citations]

  2. Persson, B., Kallberg, Y., Bray, J. E., Bruford, E., Dellaporta, S. L., Favia, A. D., Duarte, R. G., Jornvall, H., Kavanagh, K. L., Kedishvili, N., Kisiela, M., Maser, E., Mindnich, R., Orchard, S., Penning, T. M., Thornton, J. M., Adamski, J., Oppermann, U. The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative. Chem. Biol. Interact. 178: 94-98, 2009. [PubMed: 19027726, related citations] [Full Text]


Creation Date:
Rebekah S. Rasooly : 9/25/1998
terry : 10/21/2009
carol : 7/9/2009
psherman : 9/28/1998
psherman : 9/25/1998

* 603063

3-HYDROXYBUTYRATE DEHYDROGENASE 1; BDH1


Alternative titles; symbols

3-HYDROXYBUTYRATE DEHYDROGENASE; BDH


HGNC Approved Gene Symbol: BDH1

Cytogenetic location: 3q29     Genomic coordinates (GRCh38): 3:197,509,783-197,573,343 (from NCBI)


TEXT

Cloning and Expression

(R)-3-hydroxybutyrate dehydrogenase (BDH; EC 1.1.1.30) is a mitochondrial membrane enzyme with an absolute and specific requirement for phosphatidylcholine, which acts as an allosteric activator of BDH enzymatic activity. BDH has served as a prototype for lipid-requiring enzymes. By screening a human heart cDNA library with degenerate oligonucleotides based on peptide sequences from purified bovine BDH, Marks et al. (1992) isolated cDNAs encoding BDH. The deduced 343-amino acid protein contains a 46-residue leader peptide, which is cleaved to produce the mature form. Sequence analysis revealed that the first two-thirds of the BDH protein is homologous to short-chain alcohol dehydrogenases (SCADHs), with the homology encompassing the putative coenzyme-binding and active sites of the SCADHs; this region of BDH also has the predicted secondary structure motif of alternating alpha-helices and beta-sheets that is characteristic of SCADHs. The authors suggested that the remainder of the BDH protein contains elements that form the substrate- and lipid-binding sites. Northern blot analysis revealed that BDH is expressed in rabbit heart tissue.


Mapping

Persson et al. (2009) stated that the BDH gene maps to chromosome 3q29.


REFERENCES

  1. Marks, A. R., McIntyre, J. O., Duncan, T. M., Erdjument-Bromage, H., Tempst, P., Fleischer, S. Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart. J. Biol. Chem. 267: 15459-15463, 1992. [PubMed: 1639787]

  2. Persson, B., Kallberg, Y., Bray, J. E., Bruford, E., Dellaporta, S. L., Favia, A. D., Duarte, R. G., Jornvall, H., Kavanagh, K. L., Kedishvili, N., Kisiela, M., Maser, E., Mindnich, R., Orchard, S., Penning, T. M., Thornton, J. M., Adamski, J., Oppermann, U. The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative. Chem. Biol. Interact. 178: 94-98, 2009. [PubMed: 19027726] [Full Text: https://doi.org/10.1016/j.cbi.2008.10.040]


Creation Date:
Rebekah S. Rasooly : 9/25/1998

Edit History:
terry : 10/21/2009
carol : 7/9/2009
psherman : 9/28/1998
psherman : 9/25/1998