DBT (gene)

DBT
Available structures PDB Ortholog search: PDBe RCSB 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) [1] Band 1p21.2 Start 100,186,919 bp [1] End 100,249,834 bp [1]
Gene location (Mouse) Chr. Chromosome 3 (mouse) [2] Band 3 G1|3 50.37 cM Start 116,306,719 bp [2] End 116,343,630 bp [2]
RNA expression pattern 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 PubMed search [3] [4]
Wikidata
View/Edit Human View/Edit Mouse

Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial is an enzyme that in humans is encoded by the DBT gene. ^{[5] [6] [7]}

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. ^[7]

References

1. GRCh38: Ensembl release 89: ENSG00000137992 – Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000000340 – 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.
5. 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.
6. 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. doi: 10.1016/S0021-9258(18)35950-7 . PMID   1429740.
7. "Entrez Gene: DBT dihydrolipoamide branched chain transacylase E2".

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 . PMID   7672509. S2CID   25326935.
• 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.
• 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. PMID   1847055.
• 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.
• 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.
• 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. PMC   1683011 . PMID   1990841.
• 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 . PMID   2001734.
• 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. PMC   295137 . PMID   2010537.
• 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 . PMID   2708389.
• 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. PMID   2742576.
• 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. PMID   2837277.
• 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. 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. PMC   1715554 . 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. doi: 10.1016/S0021-9258(18)68766-6 . PMID   3245861.
• 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. PMC   1163502 . PMID   6895847.
• 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.
• 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. PMC   1682180 . PMID   8430702.