Metabolic Modeling Tutorial
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Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
Metabolic Modeling Tutorial
discounted EARLY registration ends Dec 31, 2014
BioCyc websites down
12/28 - 12/31
for maintenance.
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MetaCyc Reaction: 1.3.8.7

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

EC Number: 1.3.8.7

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

Supersedes EC numbers: 1.3.2.2, 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: medium-chain acyl-CoA dehydrogenase

Enzyme Commission Synonyms: fatty acyl coenzyme A dehydrogenase (ambiguous), acyl coenzyme A dehydrogenase (ambiguous), acyl dehydrogenase (ambiguous), fatty-acyl-CoA dehydrogenase (ambiguous), acyl CoA dehydrogenase (ambiguous), general acyl CoA dehydrogenase (ambiguous), medium-chain acyl-coenzyme A dehydrogenase, acyl-CoA:(acceptor) 2,3-oxidoreductase (ambiguous), ACADM (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 4 to 16 carbon atoms, but is most active with C8 to C12 compounds [CRANE56]. The enzyme from rat does not accept C16 at all and is most active with C6-C8 compounds [Ikeda85]. cf. EC 1.3.8.1, short-chain acyl-CoA dehydrogenase, EC 1.3.8.8, long-chain acyl-CoA dehydrogenase, and EC 1.3.8.9, very-long-chain acyl-CoA dehydrogenase.

Citations: [Thorpe95, Crane55, Kim93b, Peterson95, Toogood04]

Gene-Reaction Schematic: ?

Relationship Links: BRENDA:EC:1.3.8.7 , ENZYME:EC:1.3.8.7 , IUBMB-ExplorEnz:EC:1.3.8.7

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

CRANE56: Crane FL, Mii S, Hauge JG, Green DE, Beinert H (1956). "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase." J Biol Chem 218(2);701-6. PMID: 13295224

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

Kim93b: Kim JJ, Wang M, Paschke R (1993). "Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate." Proc Natl Acad Sci U S A 90(16);7523-7. PMID: 8356049

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

Peterson95: Peterson KL, Sergienko EE, Wu Y, Kumar NR, Strauss AW, Oleson AE, Muhonen WW, Shabb JB, Srivastava DK (1995). "Recombinant human liver medium-chain acyl-CoA dehydrogenase: purification, characterization, and the mechanism of interactions with functionally diverse C8-CoA molecules." Biochemistry 34(45);14942-53. PMID: 7578106

Thorpe95: Thorpe C, Kim JJ (1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases." FASEB J 9(9);718-25. PMID: 7601336

Toogood04: Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D (2004). "Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex." J Biol Chem 279(31);32904-12. PMID: 15159392


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 Sun Dec 21, 2014, biocyc14.