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Literature summary extracted from

  • 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 (2000), Arch. Biochem. Biophys., 380, 373-379.
    View publication on PubMed

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.3.1.34 expressed in Escherichia coli Escherichia coli

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
1.3.1.34 Iron 4Fe-4S-cluster or iron-sulfur-cluster Escherichia coli

Organism

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

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.34 2-trans,4-cis-decadienoyl-CoA + NADPH
-
 Escherichia coli 3-trans-decenoyl-CoA + NADP+
-
 ?
1.3.1.34 2-trans,4-cis-decadienoyl-CoA + NADPH
-
 Escherichia coli 2-decenoyl-CoA + NADP+ initial reaction product ?
1.3.1.34 2-trans,4-trans-decadienoyl-CoA + NADPH
-
 Escherichia coli 3-decenoyl-CoA + NADP+
-
 ?
1.3.1.34 5-phenyl-2,4-pentadienoyl-CoA + NADPH
-
 Escherichia coli ?
-
 ?

Synonyms

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

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.34 FAD determined by HPLC or fluorometrically, molar ratio of cofactor to enzyme: 1 Escherichia coli
1.3.1.34 FMN determined by HPLC or fluorometrically, molar ratio of cofactor to enzyme: 1 Escherichia coli
1.3.1.34 NADPH hydrogen transfer of a hydride ion from NADPH to the substrate via the enzyme bound FAD Escherichia coli