|Superclasses:||Reactions Classified By Conversion Type → Simple Reactions → Chemical Reactions|
|Reactions Classified By Substrate → Small-Molecule Reactions|
EC Number: 184.108.40.206
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: Marked as unbalanced.
adrenoyl-CoA + NADP+ ← trans-adre-2-enoyl-CoA + NADPH + H+ (220.127.116.11)
lignoceroyl-CoA + NADP+ ← trans-lignocer-2-enoyl-CoA + NADPH + H+ (18.104.22.168)
(9Z,12Z,15Z,18Z,21Z)-tetracosapentaenoyl-CoA + NADP+ ← (2Z,9Z,12Z,15Z,18Z,21Z)-tetracosahexaenoyl-CoA + NADPH + H+ (22.214.171.124)
cerotoyl-CoA + NADP+ ← trans-cerot-2-enoyl-CoA + NADPH + H+ (126.96.36.199)
docosanoyl-CoA + NADP+ ← trans-docos-2-enoyl-CoA + NADPH + H+ (188.8.131.52)
icosanoyl-CoA + NADP+ ← trans-arachido-2-enoyl-CoA + NADPH + H+ (184.108.40.206)
palmitoyl-CoA + NADP+ ← trans-hexadec-2-enoyl-CoA + NADPH + H+ (220.127.116.11)
stearoyl-CoA + NADP+ ← trans-octadec-2-enoyl-CoA + NADPH + H+ (1.3.1.-)
butanoyl-CoA + NADP+ ← crotonyl-CoA + NADPH + H+ (18.104.22.168)
a 2,3,4-saturated fatty acyl CoA + NADP+ ← a trans-2-enoyl-CoA + NADPH + H+ (22.214.171.124)
a very-long-chain 2,3,4-saturated fatty acyl CoA + NADP+ ← a very-long-chain trans-2,3-dehydroacyl-CoA + NADPH + H+ (126.96.36.199)
Enzyme Commission Primary Name: acyl-CoA dehydrogenase (NADP+)
Enzyme Commission Synonyms: 2-enoyl-CoA reductase, dehydrogenase, acyl coenzyme A (nicotinamide adenine dinucleotide phosphate), enoyl coenzyme A reductase, crotonyl coenzyme A reductase, crotonyl-CoA reductase, acyl-CoA dehydrogenase (NADP+)
Standard Gibbs Free Energy (ΔrG'° in kcal/mol): 38.025757 [Latendresse13]
Enzyme Commission Summary:
The liver enzyme acts on enoyl-CoA derivatives of carbon chain length 4 to 16, with optimum activity on 2-hexenoyl-CoA.
Unification Links: KEGG:R00385
Dommes82: Dommes V, Luster W, Cvetanovic M, Kunau WH (1982). "Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli." Eur J Biochem 125(2);335-41. PMID: 6749495
Seubert68: Seubert W, Lamberts I, Kramer R, Ohly B (1968). "On the mechanism of malonyl-CoA-independent fatty acid synthesis. I. The mechanism of elongation of long-chain fatty acids by acetyl-CoA." Biochim Biophys Acta 164(3);498-517. PMID: 4387390
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