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: 1.3.8.8

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

EC Number: 1.3.8.8

Enzymes and Genes:
long-chain-acyl-CoA dehydrogenase Inferred from experiment : ACADL ( Homo sapiens )

Supersedes EC numbers: 1.3.2.2, 1.3.99.13, 1.3.99.3

The reaction direction shown, that is, A + B ↔ C + D versus C + D ↔ A + B, is in accordance with the Enzyme Commission system.

Mass balance status: The left side is missing: H: 1

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).

Standard Gibbs Free Energy (ΔrG in kcal/mol): 42.211 Inferred by computational analysis [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 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.7, medium-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.

Citations: [Hall76, Crane55, Djordjevic94]

Gene-Reaction Schematic: ?

Unification Links: KEGG:R00392

Relationship Links: BRENDA:EC:1.3.8.8 , ENZYME:EC:1.3.8.8 , IUBMB-ExplorEnz:EC:1.3.8.8 , UniProt:RELATED-TO:P15650 , UniProt:RELATED-TO:Q8IUN8

Credits:
Revised 06-Jan-2011 by Caspi R , SRI International


References

Crane55: Crane FL, Hauge JG, Beinert H (1955). "Flavoproteins involved in the first oxidative step of the fatty acid cycle." Biochim Biophys Acta 17(2);292-4. PMID: 13239683

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

Latendresse13: Latendresse M. (2013). "Computing Gibbs Free Energy of Compounds and Reactions in MetaCyc."


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 Tue Nov 25, 2014, BIOCYC14B.