Search Results
Overview
| Uniprot ID | Q86WU2 |
|---|---|
| Protein Name | D-lactate dehydrogenase, mitochondrial |
| Gene Name | LDHD |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 141 | VEPGVTRKALNAHLR |
| 24 | GYCSQKAKGELCRDF |
| 472 | EHGIGMGKRQLLQEE |
Function
The mitochondrial D-lactate dehydrogenase is a stereoselective dehydrogenase that targets a wide variety of D-2-hydroxyacids, particularly those with small to moderately sized hydrophobic groups attached to the C2 atom. It includes D-lactate which is generated in small amounts either endogenously through the methylglyoxal metabolism pathway or exogenously via intestinal bacterial activity and dietary intake. The dehydrogenase acts specifically on D-lactate, not on its stereoisomer L-lactate, and prevents the toxic accumulation of D-lactate in the organism (PubMed:30931947, PubMed:38373542). By converting branched-chain D-2-hydroxyacids into branched-chain ketoacids, it may indirectly regulate branched-chain amino acid metabolism (By similarity)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0005739 | mitochondrion |
| Molecular Function | GO:0140174 | (2R)-2-hydroxycarboxylate dehydrogenase activity |
| Molecular Function | GO:0004458 | D-lactate dehydrogenase (cytochrome) activity |
| Molecular Function | GO:0140170 | D-lactate dehydrogenase (FAD) activity |
| Molecular Function | GO:0008720 | D-lactate dehydrogenase (NAD+) activity |
| Molecular Function | GO:0071949 | FAD binding |
| Molecular Function | GO:0050660 | flavin adenine dinucleotide binding |
| Molecular Function | GO:0004457 | lactate dehydrogenase activity |
| Molecular Function | GO:0046872 | metal ion binding |
| Biological Process | GO:1903457 | lactate 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.