Reaction: (1) a (2E)-2-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+
(2) a (2E)-2-enoyl-CoA + NADP+ = a (2E,4Z)-2,4-dienoyl-CoA + NADPH + H+
Other name(s): fadH (gene name); 4-enoyl-CoA reductase (NADPH) (ambiguous); 4-enoyl coenzyme A (reduced nicotinamide adenine dinucleotide phosphate) reductase (ambiguous); 4-enoyl-CoA reductase (ambiguous); 2,4-dienoyl-CoA reductase (NADPH) (ambiguous); trans-2,3-didehydroacyl-CoA:NADP+ 4-oxidoreductase
Systematic name: (2E)-2-enoyl-CoA:NADP+ 4-oxidoreductase
Comments: This bacterial enzyme catalyses the reduction of either (2E,4E)-2,4-dienoyl-CoA or (2E,4Z)-2,4-dienoyl-CoA to (2E)-2-enoyl-CoA. The enzyme from Escherichia coli contains FAD, FMN, and an [4Fe-4S] iron sulfur cluster. cf. EC 1.3.1.124, 2,4-dienoyl-CoA reductase [(3E)-enoyl-CoA-producing].
Links to other databases: BRENDA, EXPASY, KEGG, MetaCyc, PDB, CAS registry number: 82869-38-3
References:
1. Dommes, V., Luster, W., Cvetanovic, M. and Kunau, W.-H. Purification by affinity chromatography of 2,4-dienoyl-CoA reductases from bovine liver and Escherichia coli. Eur. J. Biochem. 125 (1982) 335-341. [PMID: 6749495]
2. Dommes, V. and Kunau, W.H. 2,4-Dienoyl coenzyme A reductases from bovine liver and Escherichia coli. Comparison of properties. J. Biol. Chem. 259 (1984) 1781-1788. [PMID: 6363415]
3. You, S.Y., Cosloy, S. and Schulz, H. Evidence for the essential function of 2,4-dienoyl-coenzyme A reductase in the β-oxidation of unsaturated fatty acids in vivo. Isolation and characterization of an Escherichia coli mutant with a defective 2,4-dienoyl-coenzyme A reductase. J. Biol. Chem. 264 (1989) 16489-16495. [PMID: 2506179]
4. He, X.Y., Yang, S.Y. and Schulz, H. Cloning and expression of the fadH gene and characterization of the gene product 2,4-dienoyl coenzyme A reductase from Escherichia coli. Eur. J. Biochem. 248 (1997) 516-520. [PMID: 9346310]
5. Liang, X., Thorpe, C. and Schulz, H. 2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-sulfur flavoprotein that functions in fatty acid β-oxidation. Arch. Biochem. Biophys. 380 (2000) 373-379. [PMID: 10933894]
6. Hubbard, P.A., Liang, X., Schulz, H. and Kim, J.J. The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase. J. Biol. Chem. 278 (2003) 37553-37560. [PMID: 12840019]
7. Tu, X., Hubbard, P.A., Kim, J.J. and Schulz, H. Two distinct proton donors at the active site of Escherichia coli 2,4-dienoyl-CoA reductase are responsible for the formation of different products. Biochemistry 47 (2008) 1167-1175. [PMID: 18171025]