Search Results
Overview
| Uniprot ID | P11182 |
|---|---|
| Protein Name | Lipoamide acyltransferase component of branched-chain alpha-keto acid dehydrogenase complex, mitochondrial |
| Gene Name | DBT |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 170 | HQEIKGRKTLATPAV |
| 196 | SEVVGSGKDGRILKE |
| 252 | PVFTGKDKTEPIKGF |
Function
The branched-chain alpha-keto dehydrogenase complex catalyzes the overall conversion of alpha-keto acids to acyl-CoA and CO(2). It contains multiple copies of three enzymatic components: branched-chain alpha-keto acid decarboxylase (E1), lipoamide acyltransferase (E2) and lipoamide dehydrogenase (E3). Within this complex, the catalytic function of this enzyme is to accept, and to transfer to coenzyme A, acyl groups that are generated by the branched-chain alpha-keto acid decarboxylase component
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0160157 | branched-chain alpha-ketoacid dehydrogenase complex |
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0042645 | mitochondrial nucleoid |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0016747 | acyltransferase activity, transferring groups other than amino-acyl groups |
| Molecular Function | GO:0043754 | dihydrolipoamide branched chain acyltransferase activity |
| Molecular Function | GO:0031625 | ubiquitin protein ligase binding |
| Biological Process | GO:0120552 | branched-chain alpha-keto acid decarboxylation to branched-chain acyl-CoA |
| Biological Process | GO:0009083 | branched-chain amino acid catabolic process |
Reference
[1] Yang Z, Yan C, Ma J, Peng P, Ren X et al.. Lactylome analysis suggests lactylation-dependent mechanisms of metabolic adaptation in hepatocellular carcinoma.. Nat Metab 5(1):61-79. 2023 Jan. PMID: 36593272.
[2] Hong H, Chen X, Wang H, Gu X, Yuan Y et al.. Global profiling of protein lysine lactylation and potential target modified protein analysis in hepatocellular carcinoma.. Proteomics 23(9):e2200432. 2023 May. PMID: 36625413.
[3] Lin Y, Chen M, Wang D, Yu Y, Chen R et al.. Multi-Proteomic Analysis Reveals the Effect of Protein Lactylation on Matrix and Cholesterol Metabolism in Tendinopathy.. J Proteome Res 22(6):1712-1722. 2023 Jun 2. PMID: 37159428.