Long-chain acyl-CoA dehydrogenase

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Long-chain acyl-CoA dehydrogenase
Identifiers
EC number1.3.8.8
CAS number59536-74-2
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / 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[edit]

  1. ^ 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.
  2. ^ 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. PMID 13319294.
  3. ^ 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.
  4. ^ 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. PMID 3968063.
  5. ^ 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.

External links[edit]