Long-chain acyl-CoA dehydrogenase

{{Infobox enzyme

| Name = Long-chain acyl-CoA dehydrogenase

| EC_number = 1.3.8.8

| CAS_number = 59536-74-2

| GO_code = 0004466

| image =

| width =

| caption =

}}

Long-chain acyl-CoA dehydrogenase ({{EC number|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.{{cite journal | vauthors = Crane FL, Hauge JG, Beinert H | title = Flavoproteins involved in the first oxidative step of the fatty acid cycle | journal = Biochimica et Biophysica Acta | volume = 17 | issue = 2 | pages = 292–4 | date = June 1955 | pmid = 13239683 | doi = 10.1016/0006-3002(55)90374-7 }}{{cite journal | vauthors = Hauge JG, Crane FL, Beinert H | title = On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl coA dehydrogenase | journal = The Journal of Biological Chemistry | volume = 219 | issue = 2 | pages = 727–33 | date = April 1956 | doi = 10.1016/S0021-9258(18)65732-1 | pmid = 13319294 | doi-access = free }}{{cite journal | vauthors = Hall CL, Heijkenskjöld L, Bártfai T, Ernster L, Kamin H | title = Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef hart mitochondria | journal = Archives of Biochemistry and Biophysics | volume = 177 | issue = 2 | pages = 402–14 | date = December 1976 | pmid = 1015826 | doi = 10.1016/0003-9861(76)90453-7 }}{{cite journal | vauthors = Ikeda Y, Okamura-Ikeda K, Tanaka K | title = 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 | journal = The Journal of Biological Chemistry | volume = 260 | issue = 2 | pages = 1311–25 | date = January 1985 | doi = 10.1016/S0021-9258(20)71245-7 | pmid = 3968063 | doi-access = free }}{{cite journal | vauthors = Djordjevic S, Dong Y, Paschke R, Frerman FE, Strauss AW, Kim JJ | title = Identification of the catalytic base in long chain acyl-CoA dehydrogenase | journal = Biochemistry | volume = 33 | issue = 14 | pages = 4258–64 | date = April 1994 | pmid = 8155643 | doi = 10.1021/bi00180a021 }} This enzyme catalyses the following chemical reaction

: a long-chain acyl-CoA + electron-transfer flavoprotein $\backslash rightleftharpoons$ 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.{{cite journal | vauthors = Ezzeddini R, Taghikhani M, Salek Farrokhi A, Somi MH, Samadi N, Esfahani A, Rasaee, MJ | title = Downregulation of fatty acid oxidation by involvement of HIF-1α and PPARγ in human gastric adenocarcinoma and its related clinical significance | journal = Journal of Physiology and Biochemistry | volume = 77 | issue = 2 | pages = 249–260 | date = May 2021 | pmid = 33730333 | doi = 10.1007/s13105-021-00791-3 | s2cid = 232300877 | url = https://pubmed.ncbi.nlm.nih.gov/33730333/| issn = }} Mitochondrial mutations in this enzyme may be associated with some forms of dilated cardiomyopathy.