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Literature summary for 1.3.1.34 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
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Cloned(Commentary)

Cloned (Comment) Organism
expressed in Escherichia coli Escherichia coli

Metals/Ions

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

Organism

Organism UniProt Comment Textmining
Escherichia coli
-
-
-

Substrates and Products (Substrate)

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

Synonyms

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

Cofactor

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