Short-chain acyl-CoA dehydrogenase

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Short-chain acyl-CoA dehydrogenase
Short-chain acyl-CoA dehydrogenase tetramer, Human
EC number
CAS number 9027-88-7
IntEnz IntEnz view
ExPASy NiceZyme view
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

Short-chain acyl-CoA dehydrogenase (EC, butyryl-CoA dehydrogenase, butanoyl-CoA dehydrogenase, butyryl dehydrogenase, unsaturated acyl-CoA reductase, ethylene reductase, enoyl-coenzyme A reductase, unsaturated acyl coenzyme A reductase, butyryl coenzyme A dehydrogenase, short-chain acyl CoA dehydrogenase, short-chain acyl-coenzyme A dehydrogenase, 3-hydroxyacyl CoA reductase, butanoyl-CoA:(acceptor) 2,3-oxidoreductase, ACADS (gene).) is an enzyme with systematic name short-chain acyl-CoA:electron-transfer flavoprotein 2,3-oxidoreductase.[1][2][3][4][5][6][7] This enzyme catalyses the following chemical reaction

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

This enzyime contains FAD as prosthetic group.


  1. ^ Mahler, H.R. (1954). "Studies on the fatty acid oxidizing system of animal tissue. IV. The prosthetic group of butyryl coenzyme A dehydrogenase". J. Biol. Chem. 206 (1): 13–26. PMID 13130522. 
  2. ^ Green, D.E.; Mii, S.; Mahler, H.R.; Bock, R.M. (1954). "Studies on the fatty acid oxidizing system of animal tissue. III. Butyryl coenzyme A dehydrogenase". J. Biol. Chem. 206 (1): 1–12. PMID 13130521. 
  3. ^ Beinert, H.; Lardy, H.; Myrbäck, K. (1963). "Acyl coenzyme A dehydrogenase". In Boyer, P.D. The Enzymes. 7 (2nd ed.). New York: Academic Press. pp. 447–466. 
  4. ^ Shaw, L.; Engel, P.C. (1984). "The purification and properties of ox liver short-chain acyl-CoA dehydrogenase". Biochem. J. 218 (2): 511–520. PMC 1153367Freely accessible. PMID 6712627. 
  5. ^ Thorpe, C.; Kim, J.J. (1995). "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB J. 9 (9): 718–725. PMID 7601336. 
  6. ^ Ikeda, Y.; Ikeda, K.O.; 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): 1311–1325. PMID 3968063. 
  7. ^ McMahon, B.; Gallagher, M.E.; Mayhew, S.G. (2005). "The protein coded by the PP2216 gene of Pseudomonas putida KT2440 is an acyl-CoA dehydrogenase that oxidises only short-chain aliphatic substrates". FEMS Microbiol. Lett. 250 (1): 121–127. doi:10.1016/j.femsle.2005.06.049. PMID 16024185. 

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