Dihydrolipoyl transacylase
| Dihydrolipoyl transacylase | ||
|---|---|---|
|
||
| other names |
52 kDa mitochondrial autoantigen of primary biliary cirrhosis |
|
| Properties of human protein | ||
| Mass / length primary structure | 53,487 daltons / 421 amino acids | |
| Secondary to quaternary structure | 24-mer | |
| Cofactor | Lipoic acid | |
| Precursor | (481 aa) | |
| Identifier | ||
| Gene names | DBT BCATE2 | |
| External IDs | ||
| Enzyme classification | ||
| EC, category | 2.3.1.168 , transferase | |
| Response type | Transfer of a branched acyl group | |
| Substrate | CoA + enzyme (lysine) acyllipoate | |
| Products | Acyl CoA + Enzyme (Lysine) Lipoate | |
| Occurrence | ||
| Parent taxon | Creature | |
| Orthologue | ||
| human | House mouse | |
| Entrez | 1629 | 13171 |
| Ensemble | ENSG00000137992 | ENSMUSG00000000340 |
| UniProt | P11182 | P53395 |
| Refseq (mRNA) | NM_001918 | NM_010022 |
| Refseq (protein) | NP_001909 | NP_034152 |
| Gene locus | Chr 1: 100.19 - 100.25 Mb | Chr 3: 116.51 - 116.55 Mb |
| PubMed search | 1629 |
13171
|
The dihydrolipoyl acyl transferase (BCKAD-E2) ( gene name: DBT ) is an enzyme that occurs in all living things. It forms the E2 subunit of the branched-chain α-ketoacid dehydrogenase - enzyme complex , one essential step in the pathway of the branched chain amino acids valine , leucine and isoleucine catalyzed . This complex, located in the mitochondria of eukaryotes, contains 24 copies of BCKAD-E2 together with its cofactor lipoic acid . Mutations in the DBT gene can lead to a hereditary E2 enzyme deficiency, which is the cause of various types of the rare maple syrup disease .
BCKAD-E2 catalyzes the transfer of the acyl residue from the dihydrolipoyllysine amino acid residue belonging to the enzyme to a coenzyme A molecule. It thus functions analogously to dihydrolipoyl transacetylase in the pyruvate dehydrogenase complex (PDH-E2) or to dihydrolipoyl transsuccinylase in the ketoglutarate dehydrogenase complex (KGDH-E2). 2-Methylpropanoyl, but also isobutyryl, isovaleryl and acetyl are accepted as acyl radicals.
literature
- BP Mooney, JA Miernyk, DD Randall: The complex fate of alpha-ketoacids. In: Annual review of plant biology . Volume 53, 2002, pp. 357-375, ISSN 1543-5008 . doi : 10.1146 / annurev.arplant.53.100301.135251 . PMID 12221980 . (Review).
- H. Mitsubuchi, M. Owada, F. Endo: Markers associated with inborn errors of metabolism of branched-chain amino acids and their relevance to upper levels of intake in healthy people: an implication from clinical and molecular investigations on maple syrup urine disease. In: The Journal of Nutrition. Volume 135, Number 6 Suppl, June 2005, pp. 1565S-1570S, ISSN 0022-3166 . PMID 15930470 . (Review).
- CA Brautigam, RM Wynn u. a .: Structural and thermodynamic basis for weak interactions between dihydrolipoamide dehydrogenase and subunit-binding domain of the branched-chain alpha-ketoacid dehydrogenase complex. In: The Journal of biological chemistry . Volume 286, Number 26, July 2011, pp. 23476-23488. doi : 10.1074 / jbc.M110.202960 . PMID 21543315 . PMC 3123111 (free full text).
Individual evidence
- ↑ InterPro : IPR001078 2-oxoacid dehydrogenase acyltransferase, catalytic domain (English)
- ↑ UniProt P11182
- ↑ EC 2.3.1.168
