BDH1

From Wikipedia, the free encyclopedia

3-hydroxybutyrate dehydrogenase, type 1

Identifiers

BDH1; BDH; MGC2723; MGC4347; MGC9788

External IDs

OMIM: 603063 MGI: 1919161 HomoloGene: 20860

Gene ontology
Molecular Function:	• 3-hydroxybutyrate dehydrogenase activity • oxidoreductase activity
Cellular Component:	• mitochondrion • mitochondrial inner membrane • mitochondrial matrix
Biological Process:	• metabolic process

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_004051 (mRNA)
NP_004042 (protein)

XM_991576 (mRNA)
XP_996670 (protein)

Location

Chr 3: 198.72 - 198.78 Mb

Chr 16: 31.34 - 31.38 Mb

Pubmed search

[1]

[2]

3-hydroxybutyrate dehydrogenase, type 1, also known as BDH1, is a human gene.^[1]

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.^[1]

[edit] See also

3-hydroxybutyrate dehydrogenase

[edit] References

^ ^a ^b Entrez Gene: BDH1 3-hydroxybutyrate dehydrogenase, type 1.

[edit] Further reading

Marks AR, McIntyre JO, Duncan TM, et al. (1992). "Molecular cloning and characterization of (R)-3-hydroxybutyrate dehydrogenase from human heart.". J. Biol. Chem. 267 (22): 15459–63. PMID 1639787.
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 ( Pt 3): 863–72. 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. 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. 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. 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. 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. doi:10.1073/pnas.242603899. 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. PMID 15489334.