|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 :||medium-chain acyl-CoA dehydrogenase
Supersedes EC numbers: 22.214.171.124, 126.96.36.199
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: 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).
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 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 188.8.131.52, short-chain acyl-CoA dehydrogenase, EC 184.108.40.206, long-chain acyl-CoA dehydrogenase, and EC 220.127.116.11, very-long-chain acyl-CoA dehydrogenase.
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
Kim93: 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
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
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
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