(Redirected from
EC 1.3.99.2)
| 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 | |||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB structures | RCSB PDB PDBe PDBsum | ||||||||
| |||||||||
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
- Acyl-CoA dehydrogenase
- Butyryl-CoA (also known as butanoyl-CoA)
References
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
- ^ 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.
External links
- Short-chain+acyl-CoA+dehydrogenase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
