Long-chain acyl-CoA dehydrogenase
(Redirected from 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.[6] Mitochondrial mutations in this enzyme may be associated with some forms of dilated cardiomyopathy.
References
[edit]- ^ Crane FL, Hauge JG, Beinert H (June 1955). "Flavoproteins involved in the first oxidative step of the fatty acid cycle". Biochimica et Biophysica Acta. 17 (2): 292–4. doi:10.1016/0006-3002(55)90374-7. PMID 13239683.
- ^ Hauge JG, Crane FL, Beinert H (April 1956). "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl coA dehydrogenase". The Journal of Biological Chemistry. 219 (2): 727–33. doi:10.1016/S0021-9258(18)65732-1. PMID 13319294.
- ^ Hall CL, Heijkenskjöld L, Bártfai T, Ernster L, Kamin H (December 1976). "Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef hart mitochondria". Archives of Biochemistry and Biophysics. 177 (2): 402–14. doi:10.1016/0003-9861(76)90453-7. PMID 1015826.
- ^ Ikeda Y, Okamura-Ikeda K, Tanaka K (January 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". The Journal of Biological Chemistry. 260 (2): 1311–25. doi:10.1016/S0021-9258(20)71245-7. PMID 3968063.
- ^ Djordjevic S, Dong Y, Paschke R, Frerman FE, Strauss AW, Kim JJ (April 1994). "Identification of the catalytic base in long chain acyl-CoA dehydrogenase". Biochemistry. 33 (14): 4258–64. doi:10.1021/bi00180a021. PMID 8155643.
- ^ Ezzeddini R, Taghikhani M, Salek Farrokhi A, Somi MH, Samadi N, Esfahani A, Rasaee, MJ (May 2021). "Downregulation of fatty acid oxidation by involvement of HIF-1α and PPARγ in human gastric adenocarcinoma and its related clinical significance". Journal of Physiology and Biochemistry. 77 (2): 249–260. doi:10.1007/s13105-021-00791-3. PMID 33730333. S2CID 232300877.
External links
[edit]- Long-chain+acyl-CoA+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
