|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 18.104.22.168
Enzymes and Genes:
|Homo sapiens :||long-chain-acyl-CoA dehydrogenase
Supersedes EC numbers: 22.214.171.124, 126.96.36.199, 188.8.131.52
The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.
Most BioCyc compounds have been protonated to a reference pH value of 7.3, and some reactions have been computationally balanced for hydrogen by adding free protons. Please see the PGDB Concepts Guide for more information.
Mass balance status: Balanced.
Enzyme Commission Primary Name: long-chain acyl-CoA dehydrogenase
Enzyme Commission Synonyms: palmitoyl-CoA dehydrogenase, palmitoyl-coenzyme A dehydrogenase, long-chain acyl-coenzyme A dehydrogenase, long-chain-acyl-CoA:(acceptor) 2,3-oxidoreductase, ACADL (gene name).
Taxonomic Range: Metazoa
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 41.78192 [Latendresse13]
Enzyme Commission Summary:
Contains FAD as prosthetic group. One of several enzymes that catalyse the first step in fatty acids β-oxidation. The enzyme from pig liver can accept substrates with acyl chain lengths of 6 to at least 16 carbon atoms. The highest activity was found with C12, and the rates with C8 and C16 were 80 and 70%, respectively [HAUGE56]. The enzyme from rat can accept substrates with C8-C22. It is most active with C14 and C16, and has no activity with C4, C6 or C24 [Ikeda85]. cf. EC 184.108.40.206, short-chain acyl-CoA dehydrogenase, EC 220.127.116.11, medium-chain acyl-CoA dehydrogenase, and EC 18.104.22.168, very-long-chain acyl-CoA dehydrogenase.
Unification Links: KEGG:R00392
Djordjevic94: Djordjevic S, Dong Y, Paschke R, Frerman FE, Strauss AW, Kim JJ (1994). "Identification of the catalytic base in long chain acyl-CoA dehydrogenase." Biochemistry 33(14);4258-64. PMID: 8155643
Hall76: Hall CL, Heijkenskjold L, Bartfai T, Ernster L, Kamin H (1976). "Acyl coenzyme A dehydrogenases and electron-transferring flavoprotein from beef hart mitochondria." Arch Biochem Biophys 177(2);402-14. PMID: 1015826
HAUGE56: Hauge JG, Crane FL, Beinert H (1956). "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. III. Palmityl coA dehydrogenase." J Biol Chem 219(2);727-33. PMID: 13319294
Ikeda85: Ikeda Y, Okamura-Ikeda K, 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(2);1311-25. PMID: 3968063
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