Biology:Short-chain acyl-CoA dehydrogenase
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Short-chain acyl-CoA dehydrogenase | |||||||||
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Short-chain acyl-CoA dehydrogenase tetramer, Human | |||||||||
Identifiers | |||||||||
EC number | 1.3.8.1 | ||||||||
CAS number | 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 | ||||||||
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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 [math]\displaystyle{ \rightleftharpoons }[/math] 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
- ↑ "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. January 1954. doi:10.1016/S0021-9258(18)71291-X. PMID 13130522.
- ↑ "Studies on the fatty acid oxidizing system of animal tissues. III. Butyryl coenzyme A dehydrogenase". The Journal of Biological Chemistry 206 (1): 1–12. January 1954. doi:10.1016/S0021-9258(18)71290-8. PMID 13130521.
- ↑ "Acyl coenzyme A dehydrogenase". The Enzymes. 7 (2nd ed.). New York: Academic Press. 1963. pp. 447–466.
- ↑ "The purification and properties of ox liver short-chain acyl-CoA dehydrogenase". The Biochemical Journal 218 (2): 511–20. March 1984. doi:10.1042/bj2180511. PMID 6712627.
- ↑ "Structure and mechanism of action of the acyl-CoA dehydrogenases". FASEB Journal 9 (9): 718–25. June 1995. doi:10.1096/fasebj.9.9.7601336. PMID 7601336.
- ↑ "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. January 1985. doi:10.1016/S0021-9258(20)71245-7. PMID 3968063.
- ↑ "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. September 2005. doi:10.1016/j.femsle.2005.06.049. PMID 16024185.
External links
- Short-chain+acyl-CoA+dehydrogenase at the US National Library of Medicine Medical Subject Headings (MeSH)
Original source: https://en.wikipedia.org/wiki/Short-chain acyl-CoA dehydrogenase.
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