Search Results
Overview
| Uniprot ID | Q99JY0 |
|---|---|
| Protein Name | Trifunctional enzyme subunit beta, mitochondrial |
| Gene Name | Hadhb |
| Organism | Mus musculus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 182 | RHSRNMRKMMLDLNK |
| 189 | KMMLDLNKAKTLGQR |
| 202 | QRLSLLSKFRLNFLS |
| 255 | RSHSLAKKAQDEGHL |
| 273 | VPFKVPGKDTVTKDN |
| 278 | PGKDTVTKDNGIRPS |
| 292 | SSLEQMAKLKPAFIK |
| 294 | LEQMAKLKPAFIKPY |
| 333 | RALAMGYKPKAYLRD |
| 362 | GPTYATPKVLEKAGL |
| 409 | NYMGRKTKVGSPPLE |
Function
Mitochondrial trifunctional enzyme catalyzes the last three of the four reactions of the mitochondrial beta-oxidation pathway. The mitochondrial beta-oxidation pathway is the major energy-producing process in tissues and is performed through cycles of four consecutive reactions. Each beta-oxidation cycle shortens the fatty acyl-CoA by two carbons, yielding one acetyl-CoA (for the citric acid cycle), one FADH(2), and one NADH (which donate electrons to the respiratory chain for ATP production). These cycles repeat until the chain is fully degraded to acetyl-CoA units. Among the enzymes involved in this pathway, the trifunctional protein, responsible for the hydration, dehydrogenation, and thiolysis steps, shows specificity for long-chain fatty acids, such as those from dietary and stored fats. Mitochondrial trifunctional enzyme is a heterotetrameric complex composed of two proteins, the trifunctional enzyme subunit alpha/HADHA carries the 2,3-enoyl-CoA hydratase and the 3-hydroxyacyl-CoA dehydrogenase activities while the trifunctional enzyme subunit beta/HADHB described here bears the 3-ketoacyl-CoA thiolase activity. These activities have been experimentally confirmed on a few substrates derived from beta-oxidation of long-chain saturated fatty acids such as palmitate (hexadecanoate) and laurate (dodecanoate). In addition, based on its established catalytic mechanism, and combined genetic interaction or mutant phenotype evidence, it is predicted to act also on other substrates, including long-chain unsaturated fatty acids such as oleate (9Z-octadecenoate), linoleate (9Z,12Z-octadecadienoate), linolenate (9Z,12Z,15Z-octadecatrienoate), and others
Protein Sequence
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005783 | endoplasmic reticulum |
| Cellular Component | GO:0016507 | mitochondrial fatty acid beta-oxidation multienzyme complex |
| Cellular Component | GO:0005743 | mitochondrial inner membrane |
| Cellular Component | GO:0042645 | mitochondrial nucleoid |
| Cellular Component | GO:0005741 | mitochondrial outer membrane |
| Cellular Component | GO:0005739 | mitochondrion |
| Cellular Component | GO:0005654 | nucleoplasm |
| Cellular Component | GO:0097228 | sperm principal piece |
| Molecular Function | GO:0003985 | acetyl-CoA C-acetyltransferase activity |
| Molecular Function | GO:0003988 | acetyl-CoA C-acyltransferase activity |
| Molecular Function | GO:0050633 | acetyl-CoA C-myristoyltransferase activity |
| Molecular Function | GO:0106222 | lncRNA binding |
| Molecular Function | GO:0044877 | protein-containing complex binding |
| Biological Process | GO:0071222 | cellular response to lipopolysaccharide |
| Biological Process | GO:0006635 | fatty acid beta-oxidation |
| Biological Process | GO:0010467 | gene expression |
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.