Long-chain acyl-CoA dehydrogenase
| Long-chain acyl-CoA dehydrogenase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 1.3.8.8 | ||||||||
| CAS no. | 59536-74-2 | ||||||||
| Databases | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| Gene Ontology | AmiGO / QuickGO | ||||||||
| |||||||||
Long-chain acyl-CoA dehydrogenase (EC 1.3.8.8, palmitoyl-CoA dehydrogenase, palmitoyl-coenzyme A dehydrogenase, long-chain acyl-coenzyme A dehydrogenase, long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase, ACADL (gene).) is an enzyme with systematic name long-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase.[1][2][3][4][5] This enzyme catalyses the following chemical reaction
- a long-chain acyl-CoA + electron-transfer flavoprotein a long-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein
This enzyme contains FAD as prosthetic group and participates in fatty acid metabolism and PPAR signaling pathway. Mitochondrial mutations in this enzyme may be associated with some forms of dilated cardiomyopathy.
References
- ^ Crane, F.L.; Hauge, J.G.; Beinert, H. (1955). "Flavoproteins involved in the first oxidative step of the fatty acid cycle". Biochim. Biophys. Acta. 17: 292–294. doi:10.1016/0006-3002(55)90374-7. PMID 13239683.
- ^ Hauge, J.G.; Crane, F.L.; Beinert, H. (1956). "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl CoA dehydrogenase". J. Biol. Chem. 219: 727–733. PMID 13319294.
- ^ Hall, C.L.; Heijkenkjold, L.; Bartfai, T.; Ernster, L.; Kamin, H. (1976). "Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef heart mitochondria". Arch. Biochem. Biophys. 177: 402–414. doi:10.1016/0003-9861(76)90453-7. PMID 1015826.
- ^ Ikeda, Y.; Ikeda, K.O.; Tanaka, K. (1985). "Purification and characterization of short-chain, medium-chain, and long-chain acyl-CoA dehydrogenases from rat liver mitochondria. Isolation of the holo- and apoenzymes and conversion of the apoenzyme to the holoenzyme". J. Biol. Chem. 260: 1311–1325. PMID 3968063.
- ^ Djordjevic, S.; Dong, Y.; Paschke, R.; Frerman, F.E.; Strauss, A.W.; Kim, J.J. (1994). "Identification of the catalytic base in long chain acyl-CoA dehydrogenase". Biochemistry. 33: 4258–4264. doi:10.1021/bi00180a021. PMID 8155643.
External links
- Long-chain+acyl-CoA+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)