EC 1.3.1.34 - 2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing]

  IntEnz view ENZYME view

IntEnz Enzyme Nomenclature
EC 1.3.1.34

Names

Accepted name:
2,4-dienoyl-CoA reductase [(2E)-enoyl-CoA-producing]
Other names:
4-enoyl coenzyme A (reduced nicotinamide adenine dinucleotide phosphate) reductase
4-enoyl-CoA reductase
4-enoyl-CoA reductase (NADPH2)
4-enoyl-CoA reductase (NADPH) [ambiguous]
2,4-dienoyl-CoA reductase (NADPH) [ambiguous]
Systematic name:
(2E)-2-enoyl-CoA:NADP+ 4-oxidoreductase

Reactions

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.

Links to other databases

Enzymes and pathways: NC-IUBMB , BRENDA , ExplorEnz , ENZYME@ExPASy , KEGG , MetaCyc , UniPathway
Protein domains and families: PROSITE:PDOC00060
Structural data: CSA , EC2PDB
Gene Ontology: GO:0008670
CAS Registry Number: 82869-38-3
UniProtKB/Swiss-Prot: (17) [show] [UniProt]

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 : 335-341 (1982). [PMID: 6749495]
  2. Dommes, V., Kunau, W. H.
    2,4-Dienoyl coenzyme A reductases from bovine liver and Escherichia coli. Comparison of properties.
    J. Biol. Chem. 259 : 1781-1788 (1984). [PMID: 6363415]
  3. You, S. Y., Cosloy, S., Schulz, H.
    Evidence for the essential function of 2,4-dienoyl-coenzyme A reductase in the beta-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 : 16489-16495 (1989). [PMID: 2506179]
  4. He, X. Y., Yang, S. Y., 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 : 516-520 (1997). [PMID: 9346310]
  5. Liang, X., Thorpe, C., Schulz, H.
    2,4-Dienoyl-CoA reductase from Escherichia coli is a novel iron-sulfur flavoprotein that functions in fatty acid beta-oxidation.
    Arch. Biochem. Biophys. 380 : 373-379 (2000). [PMID: 10933894]
  6. Hubbard, P. A., Liang, X., Schulz, H., Kim, J. J.
    The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase.
    J. Biol. Chem. 278 : 37553-37560 (2003). [PMID: 12840019]
  7. Tu, X., Hubbard, P. A., Kim, J. J., 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 : 1167-1175 (2008). [PMID: 18171025]

[EC 1.3.1.34 created 1984, modified 1986, modified 2020]