Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
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MetaCyc Reaction: 1.3.1.8

Superclasses: Reactions Classified By Conversion Type Simple Reactions Chemical Reactions
Reactions Classified By Substrate Small-Molecule Reactions

EC Number: 1.3.1.8

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.

Instance reactions:
docosanoyl-CoA + NADP+trans-docos-2-enoyl-CoA + NADPH + H+ (1.3.1.93)

arachidoyl-CoA + NADP+trans-arachido-2-enoyl-CoA + NADPH + H+ (1.3.1.93)

stearoyl-CoA + NADP+trans-octadec-2-enoyl-CoA + NADPH + H+ (1.3.1.-)

lignoceroyl-CoA + NADP+trans-lignocer-2-enoyl-CoA + NADPH + H+ (1.3.1.93)

cerotoyl-CoA + NADP+trans-cerot-2-enoyl-CoA + NADPH + H+ (1.3.1.93)

butanoyl-CoA + NADP+ ← crotonyl-CoA + NADPH + H+ (1.3.1.86)

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 Inferred by computational analysis [Latendresse, 2013]

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.

In E.coli, cis-specific and trans-specific enzymes exist [EC 1.3.1.37, cis-2-enoyl-CoA reductase (NADPH) and EC 1.3.1.38, trans-2-enoyl-CoA reductase (NADPH)].

Citations: [Seubert68, Dommes82]

Unification Links: KEGG:R00385

Relationship Links: BRENDA:EC:1.3.1.8 , ENZYME:EC:1.3.1.8 , IUBMB-ExplorEnz:EC:1.3.1.8 , UniProt:RELATED-TO:P71539


References

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

Latendresse, 2013: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."

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


Report Errors or Provide Feedback
Please cite the following article in publications resulting from the use of MetaCyc: Caspi et al, Nucleic Acids Research 42:D459-D471 2014
Page generated by SRI International Pathway Tools version 18.5 on Sat Nov 22, 2014, biocyc13.