BDH1

3-hydroxybutyrate dehydrogenase, type 1, also known as BDH1, is a human gene.cite web | title = Entrez Gene: BDH1 3-hydroxybutyrate dehydrogenase, type 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=622| accessdate = ]

PBB_Summary
section_title =
summary_text = 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.cite web | title = Entrez Gene: BDH1 3-hydroxybutyrate dehydrogenase, type 1| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=622| accessdate = ]

ee also

* 3-hydroxybutyrate dehydrogenase

References

Further reading

PBB_Further_reading
citations =
*cite journal | author=Marks AR, McIntyre JO, Duncan TM, "et al." |title=Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart. |journal=J. Biol. Chem. |volume=267 |issue= 22 |pages= 15459–63 |year= 1992 |pmid= 1639787 |doi=
*cite journal | author=Adami P, Duncan TM, McIntyre JO, "et al." |title=Monoclonal antibodies for structure-function studies of (R)-3-hydroxybutyrate dehydrogenase, a lipid-dependent membrane-bound enzyme. |journal=Biochem. J. |volume=292 ( Pt 3) |issue= |pages= 863–72 |year= 1993 |pmid= 7686368 |doi=
*cite journal | author=Langston HP, Jones L, Churchill S, Churchill PF |title=Purification and characterization of a (R)-3-hydroxybutyrate dehydrogenase deletion mutant. Evidence for C-terminal involvement in enzyme activation by lecithin. |journal=Arch. Biochem. Biophys. |volume=327 |issue= 1 |pages= 45–52 |year= 1996 |pmid= 8615695 |doi= 10.1006/abbi.1996.0091
*cite journal | author=Green D, Marks AR, Fleischer S, McIntyre JO |title=Wild type and mutant human heart (R)-3-hydroxybutyrate dehydrogenase expressed in insect cells. |journal=Biochemistry |volume=35 |issue= 25 |pages= 8158–65 |year= 1996 |pmid= 8679568 |doi= 10.1021/bi952807n
*cite journal | author=Hillier LD, Lennon G, Becker M, "et al." |title=Generation and analysis of 280,000 human expressed sequence tags. |journal=Genome Res. |volume=6 |issue= 9 |pages= 807–28 |year= 1997 |pmid= 8889549 |doi=
*cite journal | author=Chelius D, Loeb-Hennard C, Fleischer S, "et al." |title=Phosphatidylcholine activation of human heart (R)-3-hydroxybutyrate dehydrogenase mutants lacking active center sulfhydryls: site-directed mutagenesis of a new recombinant fusion protein. |journal=Biochemistry |volume=39 |issue= 32 |pages= 9687–97 |year= 2000 |pmid= 10933785 |doi=
*cite journal | author=Loeb-Hennard C, McIntyre JO |title=(R)-3-hydroxybutyrate dehydrogenase: selective phosphatidylcholine binding by the C-terminal domain. |journal=Biochemistry |volume=39 |issue= 39 |pages= 11928–38 |year= 2000 |pmid= 11009606 |doi=
*cite journal | author=Xu XR, Huang J, Xu ZG, "et al." |title=Insight into hepatocellular carcinogenesis at transcriptome level by comparing gene expression profiles of hepatocellular carcinoma with those of corresponding noncancerous liver. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=98 |issue= 26 |pages= 15089–94 |year= 2002 |pmid= 11752456 |doi= 10.1073/pnas.241522398
*cite journal | author=Strausberg RL, Feingold EA, Grouse LH, "et al." |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899
*cite journal | author=Gerhard DS, Wagner L, Feingold EA, "et al." |title=The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). |journal=Genome Res. |volume=14 |issue= 10B |pages= 2121–7 |year= 2004 |pmid= 15489334 |doi= 10.1101/gr.2596504

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