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Literature summary extracted from

  • Hubbard, P.A.; Liang, X.; Schulz, H.; Kim, J.J.
    The crystal structure and reaction mechanism of Escherichia coli 2,4-dienoyl-CoA reductase (2003), J. Biol. Chem., 278, 37553-37560.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.34 expression in strain BL21(DE3) Escherichia coli

Crystallization (Commentary)

EC Number Crystallization (Comment) Organism
1.3.1.34 15 mg/ml purified recombinant enzyme, hanging drop vapour diffusion method, reservoir solution: 30% PEG 5000 monomethyl ether, 0.2 M sodium acetate, 0.1 M ammonium sulfate, 0.1 M 3-(N-morpholino)ethane sulfonic acid, pH 6.5, precipitant solution: 18% PEG 5000 monomethyl ether, 180 mM sodium acetate, 90 mM ammonium sulfate, 90 mM 3-(N-morpholino)ethane sulfonic acid, mixture in a ratio 1:1.5, 1 week, no cryoprotection, X-ray diffraction structure determination and analysis at 2.2 A resolution, heavy atom derivatives Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.1.34 Fe2+ enzyme is a iron-sulfur flavoenzyme Escherichia coli

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.34 Escherichia coli
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.3.1.34 recombinant enzyme from strain BL21(DE3) via DEAE ion exchange and affinity chromatography Escherichia coli

Reaction

EC Number Reaction Comment Organism Reaction ID
1.3.1.34 a (2E)-2-enoyl-CoA + NADP+ = a (2E,4E)-2,4-dienoyl-CoA + NADPH + H+ reaction mechanism, active site structure, substrate binding site, His252 is the catalytic residue Escherichia coli
a

Synonyms

EC Number Synonyms Comment Organism
1.3.1.34 2,4-dienoyl-CoA reductase
-
 Escherichia coli
1.3.1.34 DCR
-
 Escherichia coli

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.34 flavin enzyme is a iron-sulfur flavoenzyme Escherichia coli