DBT (gene)

Dihydrolipoamide branched chain transacylase E2
PDB rendering based on 1k8m.
Available structures PDB Ortholog search: Template:Homologene2PDBe PDBe, Template:Homologene2uniprot RCSB List of PDB id codes 1k8m​, 1k8o​, 1zwv​, 2coo​, 2ihw​, 2ii3​, 2ii4​, 2ii5​
Identifiers
Symbols	DBT ; BCATE2; E2; E2B; MGC9061
External IDs	Template:OMIM5 Template:MGI HomoloGene: 1444
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Biological process Template:GNF GO
RNA expression pattern
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Dihydrolipoamide branched chain transacylase E2, also known as DBT, is a human gene.

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.

Further reading

• Patel MS, Harris RA (1995). "Mammalian alpha-keto acid dehydrogenase complexes: gene regulation and genetic defects". FASEB J. 9 (12): 1164–72. PMID 7672509.
• 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. PMID 1377677.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lau KS, Chuang JL, Herring WJ; et al. (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. PMID 1420314.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Lau KS, Herring WJ, Chuang JL; et al. (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.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 1847055.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 1889817.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 1943690.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 1990841.CS1 maint: Multiple names: authors list (link)
• 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. PMID 2001734.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 2010537.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 2708389.CS1 maint: Multiple names: authors list (link)
• 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. PMID 2742576.CS1 maint: Multiple names: authors list (link)
• 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. PMID 2837277.CS1 maint: Multiple names: authors list (link)
• 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. PMID 2932110.
• 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. PMID 3189339.
• 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. PMID 3245861.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• 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. PMID 6895847.CS1 maint: Multiple names: authors list (link)
• 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. PMID 7918575.CS1 maint: Multiple names: authors list (link)
• 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. PMID 8430702.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)