Acil-KoA dehidrogenaza kratkog lanca
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| Acil-KoA dehidrogenaza kratkog lanca | |||||||||
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| Tetramer acil-KoA dehidrogenaze kratkog lanca (čovjek) | |||||||||
| Identifikatori | |||||||||
| EC broj | 1.3.8.1 | ||||||||
| CAS broj | 9027-88-7 | ||||||||
| IntEnz | IntEnz view | ||||||||
| BRENDA | BRENDA entry | ||||||||
| ExPASy | NiceZyme view | ||||||||
| KEGG | KEGG entry | ||||||||
| MetaCyc | metabolic pathway | ||||||||
| PRIAM | profile | ||||||||
| PDB | RCSB PDB PDBe PDBj PDBsum | ||||||||
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Acil-KoA dehidrogenaza kratkog lanca (EC 1.3.8.1, butanoil-KoA dehidrogenaza, butirilna dehidrogenaza, nezasićena acil-KoA reduktaza, etilenska reduktaza, enoil-koenzim A reduktaza, nezasićena acil koenzim A reduktaza, butiril koenzim A dehidrogenaza, kratkolančana acil KoA dehidrogenaza, kratkolančana acil-koenzim A dehidrogenaza, 3-hidroksiacil KoA reduktaza, butanoil-KoA:(akceptor) 2,3-oksidoreduktaza, ACADS (gen).) je enzim sa sistematskim imenom kratkolančani acil-KoA:elektron-transfer flavoprotein 2,3-oksidoreduktaza.[1][2][3][4][5][6][7] Ovaj enzim katalizuje sledeću hemijsku reakciju
- kratkolančani acil-KoA + elektron-transfer flavoprotein kratkolančani trans-2,3-dehidroacil-KoA + redukovani elektron-transfer flavoprotein
Ovaj enzim sadrži FAD kao prosthetičku grupu. On je jedan od nekoliko enzima koji katalizuju prvi korak u beta oksidaciji masnih kiselina.
Reference[uredi | uredi kod]
- ↑ 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: 13-26. PMID 13130522.
- ↑ Green, D.E., Mii, S., Mahler, H.R. and Bock, R.M. (1954). „Studies on the fatty acid oxidizing system of animal tissue. III. Butyryl coenzyme A dehydrogenase”. J. Biol. Chem. 206: 1-12. PMID 13130521.
- ↑ 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.
- ↑ Shaw, L. and Engel, P.C. (1984). „The purification and properties of ox liver short-chain acyl-CoA dehydrogenase”. Biochem. J. 218: 511-520. PMID 6712627.
- ↑ Thorpe, C. and Kim, J.J. (1995). „Structure and mechanism of action of the acyl-CoA dehydrogenases”. FASEB J. 9: 718-725. PMID 7601336.
- ↑ 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.
- ↑ McMahon, B., Gallagher, M.E. and 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: 121-127. PMID 16024185.
Literatura[uredi | uredi kod]
- Nicholas C. Price, Lewis Stevens (1999). Fundamentals of Enzymology: The Cell and Molecular Biology of Catalytic Proteins (Third izd.). USA: Oxford University Press. ISBN 019850229X.
- Eric J. Toone (2006). Advances in Enzymology and Related Areas of Molecular Biology, Protein Evolution (Volume 75 izd.). Wiley-Interscience. ISBN 0471205036.
- Branden C, Tooze J.. Introduction to Protein Structure. New York, NY: Garland Publishing. ISBN: 0-8153-2305-0.
- Irwin H. Segel. Enzyme Kinetics: Behavior and Analysis of Rapid Equilibrium and Steady-State Enzyme Systems (Book 44 izd.). Wiley Classics Library. ISBN 0471303097.
- Robert A. Copeland (2013). Evaluation of Enzyme Inhibitors in Drug Discovery: A Guide for Medicinal Chemists and Pharmacologists (2nd izd.). Wiley-Interscience. ISBN 111848813X.
- Gerhard Michal, Dietmar Schomburg (2012). Biochemical Pathways: An Atlas of Biochemistry and Molecular Biology (2nd izd.). Wiley. ISBN 0470146842.