Medium-chain acyl-CoA dehydrogenase

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Medium-chain acyl-CoA dehydrogenase
1egc.jpg
Medium-chain acyl-CoA dehydrogenase tetramer, Human
Identifiers
EC number1.3.8.7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum

Medium-chain acyl-CoA dehydrogenase (EC 1.3.8.7, 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).) is an enzyme with systematic name medium-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase.[1][2][3][4][5][6][7][8] This enzyme catalyses the following chemical reaction

a medium-chain acyl-CoA + electron-transfer flavoprotein a medium-chain trans-2,3-dehydroacyl-CoA + reduced electron-transfer flavoprotein

This enzyme contains FAD as prosthetic group.

References[edit]

  1. ^ Crane FL, Hauge JG, Beinert H (June 1955). "Flavoproteins involved in the first oxidative step of the fatty acid cycle". Biochimica et Biophysica Acta. 17 (2): 292–4. doi:10.1016/0006-3002(55)90374-7. PMID 13239683.
  2. ^ Crane FL, Mii S, Hauge JG, Green DE, Beinert H (February 1956). "On the mechanism of dehydrogenation of fatty acyl derivatives of coenzyme A. I. The general fatty acyl coenzyme A dehydrogenase". The Journal of Biological Chemistry. 218 (2): 701–6. PMID 13295224.
  3. ^ Beinert, H. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D.; Lardy, H.; Myrbäck, K. (eds.). The Enzymes. 7 (2nd ed.). New York: Academic Press. pp. 447–466.
  4. ^ Ikeda Y, Okamura-Ikeda K, Tanaka K (January 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". The Journal of Biological Chemistry. 260 (2): 1311–25. PMID 3968063.
  5. ^ Thorpe C, Kim JJ (June 1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB Journal. 9 (9): 718–25. doi:10.1096/fasebj.9.9.7601336. PMID 7601336.
  6. ^ Kim JJ, Wang M, Paschke R (August 1993). "Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate". Proceedings of the National Academy of Sciences of the United States of America. 90 (16): 7523–7. doi:10.1073/pnas.90.16.7523. PMC 47174. PMID 8356049.
  7. ^ Peterson KL, Sergienko EE, Wu Y, Kumar NR, Strauss AW, Oleson AE, Muhonen WW, Shabb JB, Srivastava DK (November 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. doi:10.1021/bi00045a039. PMID 7578106.
  8. ^ Toogood HS, van Thiel A, Basran J, Sutcliffe MJ, Scrutton NS, Leys D (July 2004). "Extensive domain motion and electron transfer in the human electron transferring flavoprotein.medium chain Acyl-CoA dehydrogenase complex". The Journal of Biological Chemistry. 279 (31): 32904–12. doi:10.1074/jbc.M404884200. PMID 15159392.

External links[edit]