DBT (gene): Difference between revisions

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<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
{{Infobox_gene}}
{{GNF_Protein_box
'''Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial''' is an [[enzyme]] that in humans is encoded by the ''DBT'' [[gene]].<ref name="pmid1420314">{{cite journal | vauthors = Lau KS, Chuang JL, Herring WJ, Danner DJ, Cox RP, Chuang DT | title = The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex | journal = Biochim Biophys Acta | volume = 1132 | issue = 3 | pages = 319–21 |date=Dec 1992 | pmid = 1420314 | pmc =  | doi =  10.1016/0167-4781(92)90169-z}}</ref><ref name="pmid1429740">{{cite journal | vauthors = Lau KS, Herring WJ, Chuang JL, McKean M, Danner DJ, Cox RP, Chuang DT | title = Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene | journal = J Biol Chem | volume = 267 | issue = 33 | pages = 24090–6 |date=Dec 1992 | pmid = 1429740 | pmc =  | doi =  }}</ref><ref name="entrez">{{cite web | title = Entrez Gene: DBT dihydrolipoamide branched chain transacylase E2| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1629| accessdate = }}</ref>
| image = PBB_Protein_DBT_image.jpg
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1k8m.
| PDB = {{PDB2|1k8m}}, {{PDB2|1k8o}}, {{PDB2|1zwv}}, {{PDB2|2coo}}, {{PDB2|2ihw}}, {{PDB2|2ii3}}, {{PDB2|2ii4}}, {{PDB2|2ii5}}
| Name = Dihydrolipoamide branched chain transacylase E2
| HGNCid = 2698
| Symbol = DBT
| AltSymbols =; BCATE2; E2; E2B; MGC9061
| OMIM = 248610
| ECnumber =
| Homologene = 1444
| MGIid = 105386
| GeneAtlas_image1 = PBB_GE_DBT_205371_s_at_tn.png
  | GeneAtlas_image2 = PBB_GE_DBT_205369_x_at_tn.png
  | GeneAtlas_image3 = PBB_GE_DBT_205370_x_at_tn.png
| Function = {{GNF_GO|id=GO:0005515 |text = protein binding}} {{GNF_GO|id=GO:0008415 |text = acyltransferase activity}} {{GNF_GO|id=GO:0016740 |text = transferase activity}} {{GNF_GO|id=GO:0031405 |text = lipoic acid binding}}
| Component = {{GNF_GO|id=GO:0005739 |text = mitochondrion}} {{GNF_GO|id=GO:0005947 |text = mitochondrial alpha-ketoglutarate dehydrogenase complex}}
| Process = {{GNF_GO|id=GO:0008152 |text = metabolic process}}
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 1629
    | Hs_Ensembl = ENSG00000137992
    | Hs_RefseqProtein = NP_001909
    | Hs_RefseqmRNA = NM_001918
    | Hs_GenLoc_db =   
    | Hs_GenLoc_chr = 1
    | Hs_GenLoc_start = 100432324
    | Hs_GenLoc_end = 100487978
    | Hs_Uniprot = P11182
    | Mm_EntrezGene = 13171
    | Mm_Ensembl = ENSMUSG00000000340
    | Mm_RefseqmRNA = NM_010022
    | Mm_RefseqProtein = NP_034152
    | Mm_GenLoc_db =   
    | Mm_GenLoc_chr = 3
    | Mm_GenLoc_start = 116505111
    | Mm_GenLoc_end = 116541982
    | Mm_Uniprot = Q3TMF5
  }}
}}
'''Dihydrolipoamide branched chain transacylase E2''', also known as '''DBT''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: DBT dihydrolipoamide branched chain transacylase E2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1629| accessdate = }}</ref>


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{{PBB_Summary
{{PBB_Summary
| section_title =  
| section_title =  
| summary_text = The branched-chain alpha-keto acid dehydrogenase complex (BCKD) is an inner-mitochondrial enzyme complex involved in the breakdown of the branched-chain amino acids isoleucine, leucine, and valine. The BCKD complex is thought to be composed of a core of 24 transacylase (E2) subunits, and associated decarboxylase (E1), dehydrogenase (E3), and regulatory subunits. This gene encodes the transacylase (E2) subunit. Mutations in this gene result in maple syrup urine disease, type 2. Alternatively spliced transcript variants have been described, but their biological validity has not been determined.<ref name="entrez">{{cite web | title = Entrez Gene: DBT dihydrolipoamide branched chain transacylase E2| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=1629| accessdate = }}</ref>
| summary_text = The [[branched-chain alpha-keto acid dehydrogenase complex]] (BCKD) is an [[inner mitochondrial membrane|inner-mitochondrial]] enzyme complex involved in the breakdown of the branched-chain amino acids [[isoleucine]], [[leucine]], and [[valine]]. The BCKD complex is thought to be composed of a core of 24 [[transacylase]] (E2) subunits, and associated [[decarboxylase]] (E1), [[dehydrogenase]] (E3), and regulatory subunits. This gene encodes the transacylase (E2) subunit. [[Mutations]] in this gene result in [[maple syrup urine disease]], type 2. Alternatively spliced [[transcript variants]] have been described, but their biological validity has not been determined.<ref name="entrez" />
}}
}}


==References==
==References==
{{reflist|2}}
{{reflist}}
 
==Further reading==
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading  
| citations =  
| citations =  
*{{cite journal  | author=Patel MS, Harris RA |title=Mammalian alpha-keto acid dehydrogenase complexes: gene regulation and genetic defects. |journal=FASEB J. |volume=9 |issue= 12 |pages= 1164-72 |year= 1995 |pmid= 7672509 |doi=  }}
*{{cite journal  | vauthors=Patel MS, Harris RA |title=Mammalian alpha-keto acid dehydrogenase complexes: gene regulation and genetic defects |journal=FASEB J. |volume=9 |issue= 12 |pages= 1164–72 |year= 1995 |pmid= 7672509 |doi=  }}
*{{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  | author=Popov KM |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=  |name-list-format=vanc| author2=Zhao Y  | author3=Shimomura Y  | display-authors=3  | last4=Kuntz  | first4=MJ  | last5=Harris  | first5=RA }}
*{{cite journal | author=Lau KS, Chuang JL, Herring WJ, ''et al.'' |title=The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex. |journal=Biochim. Biophys. Acta |volume=1132 |issue= 3 |pages= 319-21 |year= 1992 |pmid= 1420314 |doi=  }}
*{{cite journal  | author=Fisher CW |title=A 17-bp insertion and a Phe215----Cys missense mutation in the dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive maple syrup urine disease patient WG-34 |journal=Biochem. Biophys. Res. Commun. |volume=174 |issue= 2 |pages= 804–9 |year= 1991 |pmid= 1847055 |doi=10.1016/0006-291X(91)91489-Y |name-list-format=vanc| author2=Lau KS | author3=Fisher CR | display-authors=3  | last4=Wynn  | first4=R.Max  | last5=Cox  | first5=Rody P. | last6=Chuang  | first6=David T.  }}
*{{cite journal  | author=Lau KS, Herring WJ, Chuang JL, ''et al.'' |title=Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene. |journal=J. Biol. Chem. |volume=267 |issue= 33 |pages= 24090-6 |year= 1992 |pmid= 1429740 |doi=  }}
*{{cite journal  | author=Zneimer SM |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  |name-list-format=vanc| author2=Lau KS  | author3=Eddy RL  | display-authors=3  | last4=Shows  | first4=Thomas B.  | last5=Chuang  | first5=Jacinta L.  | last6=Chuang  | first6=David T.  | last7=Cox  | first7=Rody P. }}
*{{cite journal  | author=Fisher CW, Lau KS, Fisher CR, ''et al.'' |title=A 17-bp insertion and a Phe215----Cys missense mutation in the dihydrolipoyl transacylase (E2) mRNA from a thiamine-responsive maple syrup urine disease patient WG-34. |journal=Biochem. Biophys. Res. Commun. |volume=174 |issue= 2 |pages= 804-9 |year= 1991 |pmid= 1847055 |doi= }}
*{{cite journal  | author=Chuang DT |title=Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex |journal=Mol. Biol. Med. |volume=8 |issue= 1 |pages= 49–63 |year= 1991 |pmid= 1943690 |doi=  |name-list-format=vanc| author2=Fisher CW  | author3=Lau KS  | display-authors=3  | last4=Griffin  | first4=TA  | last5=Wynn  | first5=RM  | last6=Cox  | first6=RP }}
*{{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=Herring WJ, Litwer S, Weber JL, Danner DJ |title=Molecular genetic basis of maple syrup urine disease in a family with two defective alleles for branched chain acyltransferase and localization of the gene to human chromosome 1 |journal=Am. J. Hum. Genet. |volume=48 |issue= 2 |pages= 342–50 |year= 1991 |pmid= 1990841 |doi= | pmc=1683011 }}
*{{cite journal  | author=Chuang DT, Fisher CW, Lau KS, ''et al.'' |title=Maple syrup urine disease: domain structure, mutations and exon skipping in the dihydrolipoyl transacylase (E2) component of the branched-chain alpha-keto acid dehydrogenase complex. |journal=Mol. Biol. Med. |volume=8 |issue= 1 |pages= 49-63 |year= 1991 |pmid= 1943690 |doi=  }}
*{{cite journal  | author=Lau KS |title=Premature termination of transcription and alternative splicing in the human transacylase (E2) gene of the branched-chain alpha-ketoacid dehydrogenase complex |journal=FEBS Lett. |volume=279 |issue= 2 |pages= 229–32 |year= 1991 |pmid= 2001734 |doi=10.1016/0014-5793(91)80155-V |name-list-format=vanc| author2=Lee J | author3=Fisher CW  | display-authors=3  | last4=Cox  | first4=Rody P.  | last5=Chuang  | first5=David T. }}
*{{cite journal  | author=Herring WJ, Litwer S, Weber JL, Danner DJ |title=Molecular genetic basis of maple syrup urine disease in a family with two defective alleles for branched chain acyltransferase and localization of the gene to human chromosome 1. |journal=Am. J. Hum. Genet. |volume=48 |issue= 2 |pages= 342-50 |year= 1991 |pmid= 1990841 |doi=  }}
*{{cite journal  | author=Mitsubuchi H |title=Maple syrup urine disease caused by a partial deletion in the inner E2 core domain of the branched chain alpha-keto acid dehydrogenase complex due to aberrant splicing. A single base deletion at a 5'-splice donor site of an intron of the E2 gene disrupts the consensus sequence in this region |journal=J. Clin. Invest. |volume=87 |issue= 4 |pages= 1207–11 |year= 1991 |pmid= 2010537 |doi=10.1172/JCI115120 | pmc=295137 |name-list-format=vanc| author2=Nobukuni Y  | author3=Akaboshi I  | display-authors=3  | last4=Indo  | first4=Y  | last5=Endo  | first5=F  | last6=Matsuda  | first6=I }}
*{{cite journal  | author=Lau KS, Lee J, Fisher CW, ''et al.'' |title=Premature termination of transcription and alternative splicing in the human transacylase (E2) gene of the branched-chain alpha-ketoacid dehydrogenase complex. |journal=FEBS Lett. |volume=279 |issue= 2 |pages= 229-32 |year= 1991 |pmid= 2001734 |doi=  }}
*{{cite journal  | vauthors=Danner DJ, Litwer S, Herring WJ, Pruckler J |title=Construction and nucleotide sequence of a cDNA encoding the full-length preprotein for human branched chain acyltransferase |journal=J. Biol. Chem. |volume=264 |issue= 13 |pages= 7742–6 |year= 1989 |pmid= 2708389 |doi=  }}
*{{cite journal  | author=Mitsubuchi H, Nobukuni Y, Akaboshi I, ''et al.'' |title=Maple syrup urine disease caused by a partial deletion in the inner E2 core domain of the branched chain alpha-keto acid dehydrogenase complex due to aberrant splicing. A single base deletion at a 5'-splice donor site of an intron of the E2 gene disrupts the consensus sequence in this region. |journal=J. Clin. Invest. |volume=87 |issue= 4 |pages= 1207-11 |year= 1991 |pmid= 2010537 |doi=  }}
*{{cite journal  | vauthors=Nobukuni Y, Mitsubuchi H, Endo F, Matsuda I |title=Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex |journal=Biochem. Biophys. Res. Commun. |volume=161 |issue= 3 |pages= 1035–41 |year= 1989 |pmid= 2742576 |doi=10.1016/0006-291X(89)91347-8 }}
*{{cite journal  | author=Danner DJ, Litwer S, Herring WJ, Pruckler J |title=Construction and nucleotide sequence of a cDNA encoding the full-length preprotein for human branched chain acyltransferase. |journal=J. Biol. Chem. |volume=264 |issue= 13 |pages= 7742-6 |year= 1989 |pmid= 2708389 |doi=  }}
*{{cite journal  | vauthors=Lau KS, Griffin TA, Hu CW, Chuang DT |title=Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs |journal=Biochemistry |volume=27 |issue= 6 |pages= 1972–81 |year= 1988 |pmid= 2837277 |doi=10.1021/bi00406a025 }}
*{{cite journal  | author=Nobukuni Y, Mitsubuchi H, Endo F, Matsuda I |title=Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex. |journal=Biochem. Biophys. Res. Commun. |volume=161 |issue= 3 |pages= 1035-41 |year= 1989 |pmid= 2742576 |doi=  }}
*{{cite journal  | vauthors=Litwer S, Danner DJ |title=Identification of a cDNA clone in lambda gt11 for the transacylase component of branched chain ketoacid dehydrogenase |journal=Biochem. Biophys. Res. Commun. |volume=131 |issue= 2 |pages= 961–7 |year= 1985 |pmid= 2932110 |doi=10.1016/0006-291X(85)91333-6 }}
*{{cite journal | author=Lau KS, Griffin TA, Hu CW, Chuang DT |title=Conservation of primary structure in the lipoyl-bearing and dihydrolipoyl dehydrogenase binding domains of mammalian branched-chain alpha-keto acid dehydrogenase complex: molecular cloning of human and bovine transacylase (E2) cDNAs. |journal=Biochemistry |volume=27 |issue= 6 |pages= 1972-81 |year= 1988 |pmid= 2837277 |doi=  }}
*{{cite journal  | vauthors=Litwer S, Danner DJ |title=Mitochondrial import and processing of an in vitro synthesized human prebranched chain acyltransferase fragment |journal=Am. J. Hum. Genet. |volume=43 |issue= 5 |pages= 764–9 |year= 1988 |pmid= 3189339 |doi= | pmc=1715554 }}
*{{cite journal  | author=Litwer S, Danner DJ |title=Identification of a cDNA clone in lambda gt11 for the transacylase component of branched chain ketoacid dehydrogenase. |journal=Biochem. Biophys. Res. Commun. |volume=131 |issue= 2 |pages= 961-7 |year= 1985 |pmid= 2932110 |doi=  }}
*{{cite journal  | author=Hummel KB |title=Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure |journal=J. Biol. Chem. |volume=263 |issue= 13 |pages= 6165–8 |year= 1988 |pmid= 3245861 |doi= |name-list-format=vanc| author2=Litwer S  | author3=Bradford AP  | display-authors=3  | last4=Aitken  | first4=A  | last5=Danner  | first5=DJ  | last6=Yeaman  | first6=SJ  }}
*{{cite journal  | author=Litwer S, Danner DJ |title=Mitochondrial import and processing of an in vitro synthesized human prebranched chain acyltransferase fragment. |journal=Am. J. Hum. Genet. |volume=43 |issue= 5 |pages= 764-9 |year= 1988 |pmid= 3189339 |doi=  }}
*{{cite journal  | vauthors=Chuang DT, Niu WL, Cox RP |title=Activities of branched-chain 2-oxo acid dehydrogenase and its components in skin fibroblasts from normal and classical-maple-syrup-urine-disease subjects |journal=Biochem. J. |volume=200 |issue= 1 |pages= 59–67 |year= 1982 |pmid= 6895847 |doi=  | pmc=1163502  }}
*{{cite journal  | author=Hummel KB, Litwer S, Bradford AP, ''et al.'' |title=Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure. |journal=J. Biol. Chem. |volume=263 |issue= 13 |pages= 6165-8 |year= 1988 |pmid= 3245861 |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=Chuang DT, Niu WL, Cox RP |title=Activities of branched-chain 2-oxo acid dehydrogenase and its components in skin fibroblasts from normal and classical-maple-syrup-urine-disease subjects. |journal=Biochem. J. |volume=200 |issue= 1 |pages= 59-67 |year= 1982 |pmid= 6895847 |doi=  }}
*{{cite journal  | author=Fisher CW |title=Occurrence of a 2-bp (AT) deletion allele and a nonsense (G-to-T) mutant allele at the E2 (DBT) locus of six patients with maple syrup urine disease: multiple-exon skipping as a secondary effect of the mutations |journal=Am. J. Hum. Genet. |volume=52 |issue= 2 |pages= 414–24 |year= 1993 |pmid= 8430702 |doi=  | pmc=1682180  |name-list-format=vanc| author2=Fisher CR  | author3=Chuang JL  | display-authors=3  | last4=Lau  | first4=KS  | last5=Chuang  | first5=DT  | last6=Cox  | first6=RP }}
*{{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  | author=Fisher CW, Fisher CR, Chuang JL, ''et al.'' |title=Occurrence of a 2-bp (AT) deletion allele and a nonsense (G-to-T) mutant allele at the E2 (DBT) locus of six patients with maple syrup urine disease: multiple-exon skipping as a secondary effect of the mutations. |journal=Am. J. Hum. Genet. |volume=52 |issue= 2 |pages= 414-24 |year= 1993 |pmid= 8430702 |doi=  }}
}}
}}
{{refend}}
{{refend}}
{{PDB Gallery|geneid=1629}}
{{Aldehyde/Oxo oxidoreductases}}
{{Multienzyme complexes}}
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{{protein-stub}}
[[Category:Mitochondrial proteins]]
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Latest revision as of 16:12, 18 October 2018

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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

Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial is an enzyme that in humans is encoded by the DBT gene.[1][2][3]

The branched-chain alpha-keto acid dehydrogenase complex (BCKD) is an inner-mitochondrial enzyme complex involved in the breakdown of the branched-chain amino acids isoleucine, leucine, and valine. The BCKD complex is thought to be composed of a core of 24 transacylase (E2) subunits, and associated decarboxylase (E1), dehydrogenase (E3), and regulatory subunits. This gene encodes the transacylase (E2) subunit. Mutations in this gene result in maple syrup urine disease, type 2. Alternatively spliced transcript variants have been described, but their biological validity has not been determined.[3]

References

  1. ↑ Lau KS, Chuang JL, Herring WJ, Danner DJ, Cox RP, Chuang DT (Dec 1992). "The complete cDNA sequence for dihydrolipoyl transacylase (E2) of human branched-chain alpha-keto acid dehydrogenase complex". Biochim Biophys Acta. 1132 (3): 319–21. doi:10.1016/0167-4781(92)90169-z. PMID 1420314.
  2. ↑ Lau KS, Herring WJ, Chuang JL, McKean M, Danner DJ, Cox RP, Chuang DT (Dec 1992). "Structure of the gene encoding dihydrolipoyl transacylase (E2) component of human branched chain alpha-keto acid dehydrogenase complex and characterization of an E2 pseudogene". J Biol Chem. 267 (33): 24090–6. PMID 1429740.
  3. ↑ 3.0 3.1 "Entrez Gene: DBT dihydrolipoamide branched chain transacylase E2".

Further reading



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