Search Results
Overview
| Uniprot ID | O08749 |
|---|---|
| Protein Name | Dihydrolipoyl dehydrogenase, mitochondrial |
| Gene Name | Dld |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 104 | YYHMAHGKDFASRGI |
| 122 | EVRLNLEKMMEQKHS |
| 127 | LEKMMEQKHSAVKAL |
| 132 | EQKHSAVKALTGGIA |
| 143 | GGIAHLFKQNKVVHV |
| 146 | AHLFKQNKVVHVNGF |
| 159 | GFGKITGKNQVTATK |
| 166 | KNQVTATKADGSTQV |
| 277 | FKFKLNTKVTGATKK |
| 410 | GKSEEQLKEEGIEFK |
| 430 | FAANSRAKTNADTDG |
| 440 | ADTDGMVKILGHKST |
| 445 | MVKILGHKSTDRVLG |
| 66 | KSAQLGFKTVCIEKN |
Function
Lipoamide dehydrogenase is a component of the glycine cleavage system as well as an E3 component of three alpha-ketoacid dehydrogenase complexes (pyruvate-, alpha-ketoglutarate-, and branched-chain amino acid-dehydrogenase complex). The 2-oxoglutarate dehydrogenase complex is mainly active in the mitochondrion. A fraction of the 2-oxoglutarate dehydrogenase complex also localizes in the nucleus and is required for lysine succinylation of histones: associates with KAT2A on chromatin and provides succinyl-CoA to histone succinyltransferase KAT2A (By similarity). In monomeric form may have additional moonlighting function as serine protease (PubMed:17404228). Involved in the hyperactivation of spermatazoa during capacitation and in the spermatazoal acrosome reaction (By similarity). The pyruvate dehydrogenase (PDH) complex catalyzes the overall conversion of pyruvate to acetyl-CoA and CO(2), and thereby links cytoplasmic glycolysis and the mitochondrial tricarboxylic acid (TCA) cycle. It contains multiple copies of three enzymatic components: pyruvate dehydrogenase (E1), dihydrolipoamide acetyltransferase (E2) and dihydrolipoamide dehydrogenase (E3). The E3 subunit catalyzes reoxidation of the dihydrolipoyl moiety on lipoyl-bearing domains (LBDs) of E2 with NAD+ as the ultimate electron acceptor (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Biological Process | GO:0007369 | gastrulation |
| Cellular Component | GO:0043159 | acrosomal matrix |
| Cellular Component | GO:0160157 | branched-chain alpha-ketoacid dehydrogenase complex |
| Cellular Component | GO:0005929 | cilium |
| Cellular Component | GO:0005759 | mitochondrial matrix |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0031514 | motile cilium |
| Cellular Component | GO:0043209 | myelin sheath |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0005634 | nucleus |
| Cellular Component | GO:0160167 | oxoadipate dehydrogenase complex |
| Cellular Component | GO:0045252 | oxoglutarate dehydrogenase complex |
| Cellular Component | GO:0045254 | pyruvate dehydrogenase complex |
| Molecular Function | GO:0004148 | dihydrolipoyl dehydrogenase (NADH) activity |
| Molecular Function | GO:0050660 | flavin adenine dinucleotide binding |
| Molecular Function | GO:0043544 | lipoamide binding |
| Molecular Function | GO:0051287 | NAD binding |
| Biological Process | GO:0120551 | 2-oxoglutarate decarboxylation to succinyl-CoA |
| Biological Process | GO:0006103 | 2-oxoglutarate metabolic process |
| 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 |
| Biological Process | GO:0051068 | dihydrolipoamide metabolic process |
| Biological Process | GO:0019474 | L-lysine catabolic process to acetyl-CoA |
| Biological Process | GO:0009106 | lipoate metabolic process |
| Biological Process | GO:0006120 | mitochondrial electron transport, NADH to ubiquinone |
| Biological Process | GO:0006508 | proteolysis |
| Biological Process | GO:0006086 | pyruvate decarboxylation to acetyl-CoA |
| Biological Process | GO:0042391 | regulation of membrane potential |
| Biological Process | GO:0048240 | sperm capacitation |
| Biological Process | GO:0006099 | tricarboxylic acid cycle |
Reference
[1] Chang J, Wu W, Qian P, Lu Z, He X et al.. Multi-omics study on the effect of moderate-intensity exercise on protein lactylation in mouse muscle tissue.. Front Cell Dev Biol 12:1472338. 2024. PMID: 39935788.
[2] Zhuo W, Zhang M, Tan J, Gao Y, Wang Y et al.. Lysine lactylation analysis of proteins in the heart of the Kawasaki disease mouse model.. Front Cell Dev Biol 13:1550220. 2025. PMID: 40114965.
[3] Wu D, Tang Y, Li X, Xiong S, Zhang Z et al.. Characterization of protein lactylation in healthy and ischemic mouse hearts.. Front Cardiovasc Med 12:1644886. 2025. PMID: 41089239.