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{{Infobox_gene}}
{{PBB_Controls
'''2-Oxoisovalerate dehydrogenase subunit beta, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''BCKDHB'' [[gene]].<ref name="entrez">{{cite web|title=Entrez Gene: BCKDHB branched chain keto acid dehydrogenase E1, beta polypeptide (maple syrup urine disease)|url=https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=594}}</ref>
| update_page = yes
| require_manual_inspection = no
| update_protein_box = yes
| update_summary = yes
| update_citations = yes
}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== Function ==
{{GNF_Protein_box
| image = PBB_Protein_BCKDHB_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1dtw.
| PDB = {{PDB2|1dtw}}, {{PDB2|1ols}}, {{PDB2|1olu}}, {{PDB2|1olx}}, {{PDB2|1u5b}}, {{PDB2|1v11}}, {{PDB2|1v16}}, {{PDB2|1v1m}}, {{PDB2|1v1r}}, {{PDB2|1wci}}, {{PDB2|1x7w}}, {{PDB2|1x7x}}, {{PDB2|1x7y}}, {{PDB2|1x7z}}, {{PDB2|1x80}}, {{PDB2|2beu}}, {{PDB2|2bev}}, {{PDB2|2bew}}, {{PDB2|2bfb}}, {{PDB2|2bfc}}, {{PDB2|2bfd}}, {{PDB2|2bfe}}, {{PDB2|2bff}}, {{PDB2|2j9f}}
| Name = Branched chain keto acid dehydrogenase E1, beta polypeptide (maple syrup urine disease)
| HGNCid = 987
| Symbol = BCKDHB
| AltSymbols =; E1B
| OMIM = 248611
| ECnumber = 
| Homologene = 39
| MGIid = 88137
| GeneAtlas_image1 = PBB_GE_BCKDHB_210653_s_at_tn.png
| GeneAtlas_image2 = PBB_GE_BCKDHB_213321_at_tn.png
| Function = {{GNF_GO|id=GO:0003826 |text = alpha-ketoacid dehydrogenase activity}} {{GNF_GO|id=GO:0003863 |text = 3-methyl-2-oxobutanoate dehydrogenase (2-methylpropanoyl-transferring) activity}} {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0016831 |text = carboxy-lyase activity}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005947 |text = mitochondrial alpha-ketoglutarate dehydrogenase complex}}
| Process = {{GNF_GO|id=GO:0009083 |text = branched chain family amino acid catabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 594
    | Hs_Ensembl = ENSG00000083123
    | Hs_RefseqProtein = NP_000047
    | Hs_RefseqmRNA = NM_000056
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 6
    | Hs_GenLoc_start = 80873083
    | Hs_GenLoc_end = 81112706
    | Hs_Uniprot = P21953
    | Mm_EntrezGene = 12040
    | Mm_Ensembl = ENSMUSG00000032263
    | Mm_RefseqmRNA = XM_918156
    | Mm_RefseqProtein = XP_923249
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 83721868
    | Mm_GenLoc_end = 83920957
    | Mm_Uniprot = 
  }}
}}
'''Branched chain keto acid dehydrogenase E1, beta polypeptide (maple syrup urine disease)''', also known as '''BCKDHB''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: BCKDHB branched chain keto acid dehydrogenase E1, beta polypeptide (maple syrup urine disease)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=594| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
Branched-chain keto acid dehydrogenase is a [[multienzyme]] complex associated with the inner membrane of [[Mitochondrion|mitochondria]], and functions in the [[catabolism]] of branched-chain [[amino acid]]s. 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.<ref name="entrez" />
{{PBB_Summary
| section_title =
| summary_text = 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.<ref name="entrez">{{cite web | title = Entrez Gene: BCKDHB branched chain keto acid dehydrogenase E1, beta polypeptide (maple syrup urine disease)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=594| accessdate = }}</ref>
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==External links==
* {{UCSC gene info|BCKDHB}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin|2}}
{{PBB_Further_reading
*{{cite journal|vauthors=Popov KM, Zhao Y, Shimomura Y|title=Branched-chain alpha-ketoacid dehydrogenase kinase. Molecular cloning, expression, and sequence similarity with histidine protein kinases|journal=J. Biol. Chem.|volume=267|issue=19|pages=13127–30|year=1992|pmid=1377677|display-authors=etal}}
| citations =
*{{cite journal|vauthors=Mitsubuchi H, Nobukuni Y, Endo F, Matsuda I|title=Structural organization and chromosomal localization of the gene for the E1 beta subunit of human branched chain alpha-keto acid dehydrogenase|journal=J. Biol. Chem.|volume=266|issue=22|pages=14686–91|year=1991|pmid=1860867}}
*{{cite journal | author=Popov KM, Zhao Y, Shimomura Y, ''et al.'' |title=Branched-chain alpha-ketoacid dehydrogenase kinase. Molecular cloning, expression, and sequence similarity with histidine protein kinases. |journal=J. Biol. Chem. |volume=267 |issue= 19 |pages= 13127-30 |year= 1992 |pmid= 1377677 |doi= }}
*{{cite journal|vauthors=Zneimer SM, Lau KS, Eddy RL|title=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|journal=Genomics|volume=10|issue=3|pages=740–7|year=1991|pmid=1889817|doi=10.1016/0888-7543(91)90458-Q|display-authors=etal}}
*{{cite journal | author=Mitsubuchi H, Nobukuni Y, Endo F, Matsuda I |title=Structural organization and chromosomal localization of the gene for the E1 beta subunit of human branched chain alpha-keto acid dehydrogenase. |journal=J. Biol. Chem. |volume=266 |issue= 22 |pages= 14686-91 |year= 1991 |pmid= 1860867 |doi=  }}
*{{cite journal|vauthors=Nobukuni Y, Mitsubuchi H, Akaboshi I|title=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|journal=J. Clin. Invest.|volume=87|issue=5|pages=1862–6|year=1991|pmid=2022752|doi=10.1172/JCI115209|pmc=295312|display-authors=etal}}
*{{cite journal | author=Zneimer SM, Lau KS, Eddy RL, ''et al.'' |title=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. |journal=Genomics |volume=10 |issue= 3 |pages= 740-7 |year= 1991 |pmid= 1889817 |doi= }}
*{{cite journal|vauthors=Chuang JL, Cox RP, Chuang DT|title=Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex|journal=FEBS Lett.|volume=262|issue=2|pages=305–9|year=1990|pmid=2335211|doi=10.1016/0014-5793(90)80215-5}}
*{{cite journal | author=Nobukuni Y, Mitsubuchi H, Akaboshi I, ''et al.'' |title=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. |journal=J. Clin. Invest. |volume=87 |issue= 5 |pages= 1862-6 |year= 1991 |pmid= 2022752 |doi= }}
*{{cite journal|vauthors=Nobukuni Y, Mitsubuchi H, Endo F|title=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|journal=J. Clin. Invest.|volume=86|issue=1|pages=242–7|year=1990|pmid=2365818|doi=10.1172/JCI114690|pmc=296713|display-authors=etal}}
*{{cite journal | author=Chuang JL, Cox RP, Chuang DT |title=Molecular cloning of the mature E1b-beta subunit of human branched-chain alpha-keto acid dehydrogenase complex. |journal=FEBS Lett. |volume=262 |issue= 2 |pages= 305-9 |year= 1990 |pmid= 2335211 |doi= }}
*{{cite journal|vauthors=Wynn RM, Kochi H, Cox RP, Chuang DT|title=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|journal=Biochim. Biophys. Acta|volume=1201|issue=1|pages=125–8|year=1994|pmid=7918575|doi=10.1016/0304-4165(94)90161-9}}
*{{cite journal | author=Nobukuni Y, Mitsubuchi H, Endo F, ''et al.'' |title=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. |journal=J. Clin. Invest. |volume=86 |issue= 1 |pages= 242-7 |year= 1990 |pmid= 2365818 |doi= }}
*{{cite journal|vauthors=Nobukuni Y, Mitsubuchi H, Hayashida Y|title=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|journal=Biochim. Biophys. Acta|volume=1225|issue=1|pages=64–70|year=1993|pmid=8161368|doi=10.1016/0925-4439(93)90123-i|display-authors=etal}}
*{{cite journal | author=Wynn RM, Kochi H, Cox RP, Chuang DT |title=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. |journal=Biochim. Biophys. Acta |volume=1201 |issue= 1 |pages= 125-8 |year= 1994 |pmid= 7918575 |doi= }}
*{{cite journal|vauthors=Chuang JL, Cox RP, Chuang DT|title=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|journal=Am. J. Hum. Genet.|volume=58|issue=6|pages=1373–7|year=1996|pmid=8651316|pmc=1915070}}
*{{cite journal | author=Nobukuni Y, Mitsubuchi H, Hayashida Y, ''et al.'' |title=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. |journal=Biochim. Biophys. Acta |volume=1225 |issue= 1 |pages= 64-70 |year= 1993 |pmid= 8161368 |doi= }}
*{{cite journal|vauthors=Edelmann L, Wasserstein MP, Kornreich R|title=Maple syrup urine disease: identification and carrier-frequency determination of a novel founder mutation in the Ashkenazi Jewish population|journal=Am. J. Hum. Genet.|volume=69|issue=4|pages=863–8|year=2001|pmid=11509994|doi=10.1086/323677|pmc=1226071|display-authors=etal}}
*{{cite journal | author=Chuang JL, Cox RP, Chuang DT |title=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. |journal=Am. J. Hum. Genet. |volume=58 |issue= 6 |pages= 1373-7 |year= 1996 |pmid= 8651316 |doi= }}
*{{cite journal|vauthors=Chang CF, Chou HT, Chuang JL|title=Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex|journal=J. Biol. Chem.|volume=277|issue=18|pages=15865–73|year=2002|pmid=11839747|doi=10.1074/jbc.M110952200|display-authors=etal}}
*{{cite journal | author=Edelmann L, Wasserstein MP, Kornreich R, ''et al.'' |title=Maple syrup urine disease: identification and carrier-frequency determination of a novel founder mutation in the Ashkenazi Jewish population. |journal=Am. J. Hum. Genet. |volume=69 |issue= 4 |pages= 863-8 |year= 2001 |pmid= 11509994 |doi= }}
*{{cite journal|vauthors=Strausberg RL, Feingold EA, Grouse LH|title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences|journal=Proc. Natl. Acad. Sci. USA|volume=99|issue=26|pages=16899–903|year=2003|pmid=12477932|doi=10.1073/pnas.242603899|pmc=139241|display-authors=etal}}
*{{cite journal | author=Chang CF, Chou HT, Chuang JL, ''et al.'' |title=Solution structure and dynamics of the lipoic acid-bearing domain of human mitochondrial branched-chain alpha-keto acid dehydrogenase complex. |journal=J. Biol. Chem. |volume=277 |issue= 18 |pages= 15865-73 |year= 2002 |pmid= 11839747 |doi= 10.1074/jbc.M110952200 }}
*{{cite journal|vauthors=Wynn RM, Machius M, Chuang JL|title=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|journal=J. Biol. Chem.|volume=278|issue=44|pages=43402–10|year=2003|pmid=12902323|doi=10.1074/jbc.M306204200|display-authors=etal}}
*{{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|vauthors=Li J, Wynn RM, Machius M|title=Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase|journal=J. Biol. Chem.|volume=279|issue=31|pages=32968–78|year=2004|pmid=15166214|doi=10.1074/jbc.M403611200|display-authors=etal}}
*{{cite journal | author=Wynn RM, Machius M, Chuang JL, ''et al.'' |title=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. |journal=J. Biol. Chem. |volume=278 |issue= 44 |pages= 43402-10 |year= 2003 |pmid= 12902323 |doi= 10.1074/jbc.M306204200 }}
*{{cite journal|vauthors=Gerhard DS, Wagner L, Feingold EA|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|pmc=528928|display-authors=etal}}
*{{cite journal | author=Li J, Wynn RM, Machius M, ''et al.'' |title=Cross-talk between thiamin diphosphate binding and phosphorylation loop conformation in human branched-chain alpha-keto acid decarboxylase/dehydrogenase. |journal=J. Biol. Chem. |volume=279 |issue= 31 |pages= 32968-78 |year= 2004 |pmid= 15166214 |doi= 10.1074/jbc.M403611200 }}
*{{cite journal|vauthors=Machius M, Wynn RM, Chuang JL|title=A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase|journal=Structure|volume=14|issue=2|pages=287–98|year=2006|pmid=16472748|doi=10.1016/j.str.2005.10.009|display-authors=etal}}
*{{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 }}
*{{cite journal|vauthors=Li J, Machius M, Chuang JL|title=The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism|journal=J. Biol. Chem.|volume=282|issue=16|pages=11904–13|year=2007|pmid=17329260|doi=10.1074/jbc.M610843200|display-authors=etal}}
*{{cite journal | author=Machius M, Wynn RM, Chuang JL, ''et al.'' |title=A versatile conformational switch regulates reactivity in human branched-chain alpha-ketoacid dehydrogenase. |journal=Structure |volume=14 |issue= 2 |pages= 287-98 |year= 2006 |pmid= 16472748 |doi= 10.1016/j.str.2005.10.009 }}
*{{cite journal | author=Li J, Machius M, Chuang JL, ''et al.'' |title=The two active sites in human branched-chain alpha-keto acid dehydrogenase operate independently without an obligatory alternating-site mechanism. |journal=J. Biol. Chem. |volume=282 |issue= 16 |pages= 11904-13 |year= 2007 |pmid= 17329260 |doi= 10.1074/jbc.M610843200 }}
}}
{{refend}}
{{refend}}


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Revision as of 02:31, 30 August 2017

VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

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Ensembl

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UniProt

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RefSeq (mRNA)

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RefSeq (protein)

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Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

2-Oxoisovalerate dehydrogenase subunit beta, mitochondrial is an enzyme that in humans is encoded by the BCKDHB gene.[1]

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.[1]

References

  1. ↑ 1.0 1.1 "Entrez Gene: BCKDHB branched chain keto acid dehydrogenase E1, beta polypeptide (maple syrup urine disease)".

External links

Further reading


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