DBT (gene)

DBT
Available structures PDB Ortholog search:PDBeRCSB List of PDB id codes 1K8M,1K8O,1ZWV,2COO,3RNM
Identifiers
Aliases	DBT,BCATE2, BCKAD-E2, BCKADE2, E2, E2B, BCOADC-E2, dihydrolipoamide branched chain transacylase E2, BCKDH-E2
External IDs	OMIM:248610;MGI:105386;HomoloGene:1444;GeneCards:DBT;OMA:DBT - orthologs
Gene location (Human) Chr. Chromosome 1 (human) Band 1p21.2 Start 100,186,919bp End 100,249,834bp
Gene location (Mouse) Chr. Chromosome 3 (mouse) Band 3 G1|3 50.37 cM Start 116,306,719bp End 116,343,630bp
RNA expressionpattern Bgee Human Mouse(ortholog) Top expressed in buccal mucosa cell renal medulla endothelial cell cardia ventral tegmental area nipple pylorus trigeminal ganglion external globus pallidus inferior ganglion of vagus nerve Top expressed in brown adipose tissue parotid gland intercostal muscle left lobe of liver lacrimal gland epithelium of stomach retinal pigment epithelium human kidney right kidney myocardium of ventricle More reference expression data BioGPS More reference expression data
Gene ontology Molecular function acyltransferase activity ubiquitin protein ligase binding transferase activity dihydrolipoyllysine-residue (2-methylpropanoyl)transferase activity acetyltransferase activity lipoic acid binding Cellular component mitochondrial matrix mitochondrial alpha-ketoglutarate dehydrogenase complex mitochondrial nucleoid mitochondrion cytoplasm Biological process metabolism branched-chain amino acid catabolic process Sources:Amigo/QuickGO
Orthologs Species Human Mouse Entrez 1629 13171 Ensembl ENSG00000137992 ENSMUSG00000000340 UniProt P11182 P53395 RefSeq (mRNA) NM_001918 NM_010022 NM_001357344 RefSeq (protein) NP_001909 NP_034152 NP_001344273 Location (UCSC) Chr 1: 100.19 – 100.25 Mb Chr 3: 116.31 – 116.34 Mb PubMedsearch
Wikidata
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Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrialis anenzymethat in humans is encoded by theDBTgene.

Thebranched-chain alpha-keto acid dehydrogenase complex(BCKD) is aninner-mitochondrialenzyme complex involved in the breakdown of the branched-chain amino acidsisoleucine,leucine,andvaline.The BCKD complex is thought to be composed of a core of 24transacylase(E2) subunits, and associateddecarboxylase(E1),dehydrogenase(E3), and regulatory subunits. This gene encodes the transacylase (E2) subunit.Mutationsin this gene result inmaple syrup urine disease,type 2. Alternatively splicedtranscript variantshave been described, but their biological validity has not been determined.

Further reading

• Patel MS, Harris RA (1995)."Mammalian alpha-keto acid dehydrogenase complexes: gene regulation and genetic defects".FASEB J.9(12): 1164–72.doi:10.1096/fasebj.9.12.7672509.PMID7672509.S2CID25326935.
• 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.PMID1377677.
• Fisher CW, Lau KS, Fisher CR, et al. (1991). "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".Biochem. Biophys. Res. Commun.174(2): 804–9.doi:10.1016/0006-291X(91)91489-Y.PMID1847055.
• 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.PMID1889817.
• Chuang DT, Fisher CW, Lau KS, et al. (1991). "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".Mol. Biol. Med.8(1): 49–63.PMID1943690.
• Herring WJ, Litwer S, Weber JL, Danner DJ (1991)."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".Am. J. Hum. Genet.48(2): 342–50.PMC1683011.PMID1990841.
• Lau KS, Lee J, Fisher CW, et al. (1991)."Premature termination of transcription and alternative splicing in the human transacylase (E2) gene of the branched-chain alpha-ketoacid dehydrogenase complex".FEBS Lett.279(2): 229–32.Bibcode:1991FEBSL.279..229L.doi:10.1016/0014-5793(91)80155-V.PMID2001734.
• Mitsubuchi H, Nobukuni Y, Akaboshi I, et al. (1991)."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".J. Clin. Invest.87(4): 1207–11.doi:10.1172/JCI115120.PMC295137.PMID2010537.
• Danner DJ, Litwer S, Herring WJ, Pruckler J (1989)."Construction and nucleotide sequence of a cDNA encoding the full-length preprotein for human branched chain acyltransferase".J. Biol. Chem.264(13): 7742–6.doi:10.1016/S0021-9258(18)83297-5.PMID2708389.
• Nobukuni Y, Mitsubuchi H, Endo F, Matsuda I (1989). "Complete primary structure of the transacylase (E2b) subunit of the human branched chain alpha-keto acid dehydrogenase complex".Biochem. Biophys. Res. Commun.161(3): 1035–41.doi:10.1016/0006-291X(89)91347-8.PMID2742576.
• Lau KS, Griffin TA, Hu CW, Chuang DT (1988). "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".Biochemistry.27(6): 1972–81.doi:10.1021/bi00406a025.PMID2837277.
• Litwer S, Danner DJ (1985). "Identification of a cDNA clone in lambda gt11 for the transacylase component of branched chain ketoacid dehydrogenase".Biochem. Biophys. Res. Commun.131(2): 961–7.doi:10.1016/0006-291X(85)91333-6.PMID2932110.
• Litwer S, Danner DJ (1988)."Mitochondrial import and processing of an in vitro synthesized human prebranched chain acyltransferase fragment".Am. J. Hum. Genet.43(5): 764–9.PMC1715554.PMID3189339.
• Hummel KB, Litwer S, Bradford AP, et al. (1988)."Nucleotide sequence of a cDNA for branched chain acyltransferase with analysis of the deduced protein structure".J. Biol. Chem.263(13): 6165–8.doi:10.1016/S0021-9258(18)68766-6.PMID3245861.
• Chuang DT, Niu WL, Cox RP (1982)."Activities of branched-chain 2-oxo acid dehydrogenase and its components in skin fibroblasts from normal and classical-maple-syrup-urine-disease subjects".Biochem. J.200(1): 59–67.doi:10.1042/bj2000059.PMC1163502.PMID6895847.
• 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.PMID7918575.
• Fisher CW, Fisher CR, Chuang JL, et al. (1993)."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".Am. J. Hum. Genet.52(2): 414–24.PMC1682180.PMID8430702.