BDH1

Protein-coding gene in the species Homo sapiens

BDH1
Identifiers
AliasesBDH1, BDH, SDR9C1, 3-hydroxybutyrate dehydrogenase, type 1, 3-hydroxybutyrate dehydrogenase 1
External IDsOMIM: 603063; MGI: 1919161; HomoloGene: 20860; GeneCards: BDH1; OMA:BDH1 - orthologs
Gene location (Human)
Chromosome 3 (human)
Chr.Chromosome 3 (human)[1]
Chromosome 3 (human)
Genomic location for BDH1
Genomic location for BDH1
Band3q29Start197,509,783 bp[1]
End197,573,323 bp[1]
Gene location (Mouse)
Chromosome 16 (mouse)
Chr.Chromosome 16 (mouse)[2]
Chromosome 16 (mouse)
Genomic location for BDH1
Genomic location for BDH1
Band16|16 B2Start31,241,098 bp[2]
End31,277,719 bp[2]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • right lobe of liver

  • mucosa of transverse colon

  • cerebellar hemisphere

  • right hemisphere of cerebellum

  • rectum

  • duodenum

  • right frontal lobe

  • olfactory zone of nasal mucosa

  • apex of heart

  • left ventricle
Top expressed in
  • epithelium of small intestine

  • interventricular septum

  • left lobe of liver

  • myocardium of ventricle

  • right ventricle

  • soleus muscle

  • human kidney

  • ileum

  • migratory enteric neural crest cell

  • extraocular muscle
More reference expression data
BioGPS
More reference expression data
Gene ontology
Molecular function
  • catalytic activity
  • 3-hydroxybutyrate dehydrogenase activity
  • oxidoreductase activity
Cellular component
  • nucleoplasm
  • mitochondrial matrix
  • mitochondrion
  • mitochondrial inner membrane
  • membrane
  • matrix side of mitochondrial inner membrane
Biological process
  • ketone body biosynthetic process
  • ketone body catabolic process
  • metabolism
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

622

71911

Ensembl

ENSG00000161267
ENSG00000275544

ENSMUSG00000046598

UniProt

Q02338

Q80XN0

RefSeq (mRNA)

NM_004051
NM_203314
NM_203315

NM_001122683
NM_175177

RefSeq (protein)

NP_004042
NP_976059
NP_976060

NP_001116155
NP_780386

Location (UCSC)Chr 3: 197.51 – 197.57 MbChr 16: 31.24 – 31.28 Mb
PubMed search[3][4]
Wikidata
View/Edit HumanView/Edit Mouse

D-beta-hydroxybutyrate dehydrogenase, mitochondrial is an enzyme that in humans is encoded by the BDH1 gene.[5][6][7]

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.[7]

See also

References

  1. ^ a b c ENSG00000275544 GRCh38: Ensembl release 89: ENSG00000161267, ENSG00000275544 – Ensembl, May 2017
  2. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000046598 – Ensembl, May 2017
  3. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  5. ^ Marks AR, McIntyre JO, Duncan TM, Erdjument-Bromage H, Tempst P, Fleischer S (Aug 1992). "Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart". J Biol Chem. 267 (22): 15459–63. doi:10.1016/S0021-9258(19)49556-2. PMID 1639787.
  6. ^ Persson B, Kallberg Y, Bray JE, Bruford E, Dellaporta SL, Favia AD, Duarte RG, Jornvall H, Kavanagh KL, Kedishvili N, Kisiela M, Maser E, Mindnich R, Orchard S, Penning TM, Thornton JM, Adamski J, Oppermann U (Feb 2009). "The SDR (short-chain dehydrogenase/reductase and related enzymes) nomenclature initiative". Chem Biol Interact. 178 (1–3): 94–8. Bibcode:2009CBI...178...94P. doi:10.1016/j.cbi.2008.10.040. PMC 2896744. PMID 19027726.
  7. ^ a b "Entrez Gene: BDH1 3-hydroxybutyrate dehydrogenase, type 1".

Further reading

  • Adami P, Duncan TM, McIntyre JO, et al. (1993). "Monoclonal antibodies for structure-function studies of (R)-3-hydroxybutyrate dehydrogenase, a lipid-dependent membrane-bound enzyme". Biochem. J. 292 (3): 863–72. doi:10.1042/bj2920863. PMC 1134194. PMID 7686368.
  • Langston HP, Jones L, Churchill S, Churchill PF (1996). "Purification and characterization of a (R)-3-hydroxybutyrate dehydrogenase deletion mutant. Evidence for C-terminal involvement in enzyme activation by lecithin". Arch. Biochem. Biophys. 327 (1): 45–52. doi:10.1006/abbi.1996.0091. PMID 8615695.
  • 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. PMID 8679568.
  • 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. PMID 8889549.
  • 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. PMID 10933785.
  • 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. PMID 11009606.
  • Xu XR, Huang J, Xu ZG, et al. (2002). "Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver". Proc. Natl. Acad. Sci. U.S.A. 98 (26): 15089–94. doi:10.1073/pnas.241522398. PMC 64988. PMID 11752456.
  • Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
  • Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.


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