Short-chain acyl-CoA dehydrogenase

Short-chain acyl-CoA dehydrogenase
Short-chain acyl-CoA dehydrogenase tetramer, Human
Identifiers
EC no.1.3.8.1
CAS no.9027-88-7
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
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PMCarticles
PubMedarticles
NCBIproteins

Short-chain acyl-CoA dehydrogenase (EC 1.3.8.1, 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 enzyme contains FAD as prosthetic group.

See also

References

  1. ^ Mahler HR (January 1954). "Studies on the fatty acid oxidizing system of animal tissues. IV. The prosthetic group of butyryl coenzyme A dehydrogenase". The Journal of Biological Chemistry. 206 (1): 13–26. doi:10.1016/S0021-9258(18)71291-X. PMID 13130522.
  2. ^ Green DE, Mii S, Mahler HR, Bock RM (January 1954). "Studies on the fatty acid oxidizing system of animal tissues. III. Butyryl coenzyme A dehydrogenase". The Journal of Biological Chemistry. 206 (1): 1–12. doi:10.1016/S0021-9258(18)71290-8. PMID 13130521.
  3. ^ Beinert H (1963). "Acyl coenzyme A dehydrogenase". In Boyer PD, Lardy H, Myrbäck K (eds.). The Enzymes. Vol. 7 (2nd ed.). New York: Academic Press. pp. 447–466.
  4. ^ Shaw L, Engel PC (March 1984). "The purification and properties of ox liver short-chain acyl-CoA dehydrogenase". The Biochemical Journal. 218 (2): 511–20. doi:10.1042/bj2180511. PMC 1153367. PMID 6712627.
  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. S2CID 42549744.
  6. ^ 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. doi:10.1016/S0021-9258(20)71245-7. PMID 3968063.
  7. ^ McMahon B, Gallagher ME, Mayhew SG (September 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 Microbiology Letters. 250 (1): 121–7. doi:10.1016/j.femsle.2005.06.049. PMID 16024185.

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