Search Results
Overview
| Uniprot ID | Q08426 |
|---|---|
| Protein Name | Peroxisomal bifunctional enzyme |
| Gene Name | EHHADH |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 165 | ILADEALKLGILDKV |
| 250 | YPYEVGIKKEEELFL |
| 280 | FAERKANKWSTPSGA |
| 290 | TPSGASWKTASARPV |
| 33 | TTLLRDIKEGLQKAV |
| 330 | VIAVDSDKNQLATAN |
| 338 | NQLATANKMITSVLE |
| 346 | MITSVLEKEASKMQQ |
| 350 | VLEKEASKMQQSGHP |
| 362 | GHPWSGPKPRLTSSV |
| 38 | DIKEGLQKAVIDHTI |
| 46 | AVIDHTIKAIVICGA |
| 532 | AGLDVGWKSRKGQGL |
| 535 | DVGWKSRKGQGLTGP |
| 574 | ELGRFGQKTGKGWYQ |
| 577 | RFGQKTGKGWYQYDK |
| 584 | KGWYQYDKPLGRIHK |
| 591 | KPLGRIHKPDPWLSK |
| 598 | KPDPWLSKFLSRYRK |
| 605 | KFLSRYRKTHHIEPR |
| 660 | GYGWPRHKGGPMFYA |
| 700 | EPSDYLKKLASQGNP |
| 710 | SQGNPPLKEWQSLAG |
| 722 | LAGSPSSKL****** |
Function
Peroxisomal trifunctional enzyme possessing 2-enoyl-CoA hydratase, 3-hydroxyacyl-CoA dehydrogenase, and delta 3, delta 2-enoyl-CoA isomerase activities. Catalyzes two of the four reactions of the long chain fatty acids peroxisomal beta-oxidation pathway (By similarity). Can also use branched-chain fatty acids such as 2-methyl-2E-butenoyl-CoA as a substrate, which is hydrated into (2S,3S)-3-hydroxy-2-methylbutanoyl-CoA (By similarity). Optimal isomerase for 2,5 double bonds into 3,5 form isomerization in a range of enoyl-CoA species (Probable). Also able to isomerize both 3-cis and 3-trans double bonds into the 2-trans form in a range of enoyl-CoA species (By similarity). With HSD17B4, catalyzes the hydration of trans-2-enoyl-CoA and the dehydrogenation of 3-hydroxyacyl-CoA, but with opposite chiral specificity (PubMed:15060085). Regulates the amount of medium-chain dicarboxylic fatty acids which are essential regulators of all fatty acid oxidation pathways (By similarity). Also involved in the degradation of long-chain dicarboxylic acids through peroxisomal beta-oxidation (PubMed:15060085)
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005829 | cytosol |
| Cellular Component | GO:0005782 | peroxisomal matrix |
| Cellular Component | GO:0005777 | peroxisome |
| Molecular Function | GO:0003857 | (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
| Molecular Function | GO:0018812 | 3-hydroxyacyl-CoA dehydratase activity |
| Molecular Function | GO:0004165 | delta(3)-delta(2)-enoyl-CoA isomerase activity |
| Molecular Function | GO:0004300 | enoyl-CoA hydratase activity |
| Molecular Function | GO:0019899 | enzyme binding |
| Molecular Function | GO:0016863 | intramolecular oxidoreductase activity, transposing C=C bonds |
| Molecular Function | GO:0016509 | long-chain (3S)-3-hydroxyacyl-CoA dehydrogenase (NAD+) activity |
| Molecular Function | GO:0070403 | NAD+ binding |
| Biological Process | GO:0006635 | fatty acid beta-oxidation |
| Biological Process | GO:0033540 | fatty acid beta-oxidation using acyl-CoA oxidase |
| Biological Process | GO:0006633 | fatty acid biosynthetic 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.