Acil-KoA dehidrogenaza srednje dugog lanca

Acil-KoA dehidrogenaza srednje dugog lanca
Tetramer acil-KoA dehidrogenaze srednje dugog lanca (čovjek)
Identifikatori
EC broj 1.3.8.7
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB RCSB PDB PDBe PDBj PDBsum

Acil-KoA dehidrogenaza srednje dugog lanca (EC 1.3.8.7, masna acil koenzim A dehidrogenaza (nespecifična), acil koenzim A dehidrogenaza (nespecifična), acil dehidrogenaza (nespecifična), masna-acil-KoA dehidrogenaza (nespecifična), acil KoA dehidrogenaza (nespecifična), general acil KoA dehidrogenaza (nespecifična), acil-koenzim A dehidrogenaza srednje dugog lanca, acil-KoA:(akceptor) 2,3-oksidoreduktaza (nespecifična), ACADM (gen).) je enzim sa sistematskim imenom acil-KoA srednje dugog lanca:elektron-transfer flavoprotein 2,3-oksidoreduktaza.[1][2][3][4][5][6][7][8] Ovaj enzim katalizuje sledeću hemijsku reakciju

acil-KoA srednje dugog lanca + elektron-transfer flavoprotein trans-2,3-dehidroacil-KoA srednje dugog lanca + redukovani elektron-transfer flavoprotein

Ovaj enzim sadrži FAD kao prostetičku grupu. On je jedan od nekoliko enzima koji katalizuju prvi korak u beta oksidaciji masnih kiselina. Enzim iz jetre svinja može da deluje na supstrat sa acil lancom dožine 4 do 16 ugljenika, ali je najaktivniji na jedinjenjima sa C8 do C12 dugim lancom.

Reference

  1. Crane, F.L., Hauge, J.G. and Beinert, H. (1955). „Flavoproteins involved in the first oxidative step of the fatty acid cycle”. Biochim. Biophys. Acta 17: 292-294. PMID 13239683. 
  2. Crane, F.L., Mii, S., Hauge, J.G., Green, D.E. and 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: 701-716. PMID 13295224. 
  3. Beinert, H. (1963). „Acyl coenzyme A dehydrogenase”. u: Boyer, P.D., Lardy, H. and Myrbäck, K.. The Enzymes. 7 (2nd izd.). New York: Academic Press. str. 447-466. 
  4. Ikeda, Y., Ikeda, K.O. and 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: 1311-1325. PMID 3968063. 
  5. Thorpe, C. and Kim, J.J. (1995). „Structure and mechanism of action of the acyl-CoA dehydrogenases”. FASEB J. 9: 718-725. PMID 7601336. 
  6. Kim, J.J., Wang, M. and Paschke, R. (1993). „Crystal structures of medium-chain acyl-CoA dehydrogenase from pig liver mitochondria with and without substrate”. Proc. Natl. Acad. Sci. USA 90: 7523-7527. PMID 8356049. 
  7. Peterson, K.L., Sergienko, E.E., Wu, Y., Kumar, N.R., Strauss, A.W., Oleson, A.E., Muhonen, W.W., Shabb, J.B. and Srivastava, D.K. (1995). „Recombinant human liver medium-chain acyl-CoA dehydrogenase: purification, characterization, and the mechanism of interactions with functionally diverse C8-CoA molecules”. Biochemistry 34: 14942-14953. PMID 7578106. 
  8. Toogood, H.S., van Thiel, A., Basran, J., Sutcliffe, M.J., Scrutton, N.S. and 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: 32904-32912. PMID 15159392. 

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