BCKDHB

BCKDHB
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1DTW, 1OLS, 1OLU, 1OLX, 1U5B, 1V11, 1V16, 1V1M, 1V1R, 1WCI, 1X7W, 1X7X, 1X7Y, 1X7Z, 1X80, 2BEU, 2BEV, 2BEW, 2BFB, 2BFC, 2BFD, 2BFE, 2BFF, 2J9F
Identifiers
Aliases	BCKDHB, E1B, dJ279A18.1, BCKDE1B, BCKDH E1-beta, branched chain keto acid dehydrogenase E1, beta polypeptide, branched chain keto acid dehydrogenase E1 subunit beta
External IDs	OMIM: 248611; MGI: 88137; HomoloGene: 39; GeneCards: BCKDHB; OMA:BCKDHB - orthologs
Gene location (Human)
Chr.	Chromosome 6 (human)
End	80,346,270 bp
Gene location (Mouse)
Chr.	Chromosome 9 (mouse)
End	84,006,293 bp
RNA expression pattern
	Top expressed in
	right lobe of liver; ; rectum; ; mucosa of transverse colon; ; Achilles tendon; ; olfactory zone of nasal mucosa; ; ventricular zone; ; popliteal artery; ; tibial arteries; ; body of stomach; ; left ventricle;
	Top expressed in
	left lobe of liver; ; brown adipose tissue; ; white adipose tissue; ; epithelium of stomach; ; myocardium of ventricle; ; interventricular septum; ; plantaris muscle; ; subcutaneous adipose tissue; ; cardiac muscles; ; parotid gland;
	More reference expression data
	; ;
	More reference expression data
Gene ontology
Molecular function	oxidoreductase activity; protein binding; 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity; catalytic activity;
Cellular component	mitochondrial matrix; mitochondrial alpha-ketoglutarate dehydrogenase complex; mitochondrion;
Biological process	metabolism; branched-chain amino acid catabolic process; response to nutrient;
	Sources:Amigo / QuickGO
Orthologs
	594
	12040
	ENSG00000083123
	ENSMUSG00000032263
	P21953
	Q6P3A8
	NM_000056; NM_183050; NM_001318975
	NM_199195; NM_001305935
	NP_000047; NP_001305904; NP_898871
	NP_001292864; NP_954665
	Wikidata
View/Edit Human	View/Edit Mouse

2-Oxoisovalerate dehydrogenase subunit beta, mitochondrial is an enzyme that in humans is encoded by the BCKDHB gene.^[5]

Function

Branched-chain keto acid dehydrogenase is a multienzyme complex associated with the inner membrane of mitochondria, and functions in the catabolism of branched-chain amino acids. The complex consists of multiple copies of 3 components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2), and lipoamide dehydrogenase (E3). This gene encodes the E1 beta subunit, and mutations therein have been associated with maple syrup urine disease (MSUD), type 1B. Alternative splicing at this locus results in transcript variants with different 3' noncoding regions, but encoding the same isoform.^[5]

References

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000083123 – Ensembl, May 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000032263 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ ^a ^b "Entrez Gene: BCKDHB branched chain keto acid dehydrogenase E1, beta polypeptide (maple syrup urine disease)".

Popov KM, Zhao Y, Shimomura Y, et al. (1992). "Branched-chain alpha-ketoacid dehydrogenase kinase. Molecular cloning, expression, and sequence similarity with histidine protein kinases". J. Biol. Chem. 267 (19): 13127–30. doi:10.1016/S0021-9258(18)42179-5. PMID 1377677.
Mitsubuchi H, Nobukuni Y, Endo F, Matsuda I (1991). "Structural organization and chromosomal localization of the gene for the E1 beta subunit of human branched chain alpha-keto acid dehydrogenase". J. Biol. Chem. 266 (22): 14686–91. doi:10.1016/S0021-9258(18)98740-5. PMID 1860867.
Zneimer SM, Lau KS, Eddy RL, et al. (1991). "Regional assignment of two genes of the human branched-chain alpha-keto acid dehydrogenase complex: the E1 beta gene (BCKDHB) to chromosome 6p21-22 and the E2 gene (DBT) to chromosome 1p31". Genomics. 10 (3): 740–7. doi:10.1016/0888-7543(91)90458-Q. PMID 1889817.
Nobukuni Y, Mitsubuchi H, Akaboshi I, et al. (1991). "Maple syrup urine disease. Complete defect of the E1 beta subunit of the branched chain alpha-ketoacid dehydrogenase complex due to a deletion of an 11-bp repeat sequence which encodes a mitochondrial targeting leader peptide in a family with the disease". J. Clin. Invest. 87 (5): 1862–6. doi:10.1172/JCI115209. PMC 295312. PMID 2022752.
Chuang JL, Cox RP, Chuang DT (1990). "Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex". FEBS Lett. 262 (2): 305–9. Bibcode:1990FEBSL.262..305C. doi:10.1016/0014-5793(90)80215-5. PMID 2335211. S2CID 84069883.
Nobukuni Y, Mitsubuchi H, Endo F, et al. (1990). "Maple syrup urine disease. Complete primary structure of the E1 beta subunit of human branched chain alpha-ketoacid dehydrogenase complex deduced from the nucleotide sequence and a gene analysis of patients with this disease". J. Clin. Invest. 86 (1): 242–7. doi:10.1172/JCI114690. PMC 296713. PMID 2365818.
Wynn RM, Kochi H, Cox RP, Chuang DT (1994). "Differential processing of human and rat E1 alpha precursors of the branched-chain alpha-keto acid dehydrogenase complex caused by an N-terminal proline in the rat sequence". Biochim. Biophys. Acta. 1201 (1): 125–8. doi:10.1016/0304-4165(94)90161-9. PMID 7918575.
Nobukuni Y, Mitsubuchi H, Hayashida Y, et al. (1993). "Heterogeneity of mutations in maple syrup urine disease (MSUD): screening and identification of affected E1 alpha and E1 beta subunits of the branched-chain alpha-keto-acid dehydrogenase multienzyme complex". Biochim. Biophys. Acta. 1225 (1): 64–70. doi:10.1016/0925-4439(93)90123-i. PMID 8161368.
Chuang JL, Cox RP, Chuang DT (1996). "Maple syrup urine disease: the E1beta gene of human branched-chain alpha-ketoacid dehydrogenase complex has 11 rather than 10 exons, and the 3' UTR in one of the two E1beta mRNAs arises from intronic sequences". Am. J. Hum. Genet. 58 (6): 1373–7. PMC 1915070. PMID 8651316.
Edelmann L, Wasserstein MP, Kornreich R, et al. (2001). "Maple syrup urine disease: identification and carrier-frequency determination of a novel founder mutation in the Ashkenazi Jewish population". Am. J. Hum. Genet. 69 (4): 863–8. doi:10.1086/323677. PMC 1226071. PMID 11509994.
Chang CF, Chou HT, Chuang JL, et al. (2002). "Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex". J. Biol. Chem. 277 (18): 15865–73. doi:10.1074/jbc.M110952200. PMID 11839747.
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. USA. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
Wynn RM, Machius M, Chuang JL, et al. (2003). "Roles of His291-alpha and His146-beta' in the reductive acylation reaction catalyzed by human branched-chain alpha-ketoacid dehydrogenase: refined phosphorylation loop structure in the active site". J. Biol. Chem. 278 (44): 43402–10. doi:10.1074/jbc.M306204200. PMID 12902323.
Li J, Wynn RM, Machius M, et al. (2004). "Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase". J. Biol. Chem. 279 (31): 32968–78. doi:10.1074/jbc.M403611200. PMID 15166214.
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.
Machius M, Wynn RM, Chuang JL, et al. (2006). "A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase". Structure. 14 (2): 287–98. doi:10.1016/j.str.2005.10.009. PMID 16472748.
Li J, Machius M, Chuang JL, et al. (2007). "The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism". J. Biol. Chem. 282 (16): 11904–13. doi:10.1074/jbc.M610843200. PMID 17329260.

External links

Human BCKDHB genome location and BCKDHB gene details page in the UCSC Genome Browser.

This article on a gene on human chromosome 6 is a stub. You can help Wikipedia by expanding it.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000083123 – Ensembl, May 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000032263 – 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.

[entrez-5] "Entrez Gene: BCKDHB branched chain keto acid dehydrogenase E1, beta polypeptide (maple syrup urine disease)".

[1]

[2]

[3]

[4]

[5]

v t e Enzymes: multienzyme complexes
Photosynthesis	Photosynthetic reaction center complex proteins Photosystem I II
Dehydrogenase	Pyruvate dehydrogenase complex E1 E2 E3 Oxoglutarate dehydrogenase OGDH DLST DLD Branched-chain alpha-keto acid dehydrogenase complex BCKDHA BCKDHB DBT DLD
Other	CAD Carbamoyl phosphate synthase II Aspartate carbamoyltransferase Dihydroorotase P450-containing systems Cytochrome b6f complex Electron transport chain Fatty acid synthetase complex Glycine decarboxylase complex Mitochondrial trifunctional protein HADHA HADHB Phosphoenolpyruvate sugar phosphotransferase system Polyketide synthase Sucrase-isomaltase complex Tryptophan synthase

v t e Aldehyde/oxo oxidoreductases (EC 1.2)
1.2.1: NAD or NADP	Aldehyde dehydrogenase Acetaldehyde dehydrogenase Long-chain-aldehyde dehydrogenase Mycothiol-dependent formaldehyde dehydrogenase
1.2.2: cytochrome	Formate dehydrogenase (cytochrome)
1.2.3: oxygen	Aldehyde oxidase
1.2.4: disulfide	Oxoglutarate dehydrogenase complex Pyruvate dehydrogenase Branched-chain alpha-keto acid dehydrogenase complex BCKDHA BCKDHB DBT DLD
1.2.7: iron–sulfur protein	Pyruvate synthase

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

Function

References

Further reading

External links