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Literature summary for 5.1.2.3 extracted from

  • Smeland, T.E.; Cuebas, D.; Schulz, H.
    Epimerization of 3-hydroxy-4-trans-decenoyl coenzyme A by a dehydration/hydration mechanism catalyzed by the multienzyme complex of fatty acid oxidation from Escherichia coli (1991), J. Biol. Chem., 266, 23904-23908.
    View publication on PubMed

Organism

Organism UniProt Comment Textmining
Escherichia coli
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-
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Purification (Commentary)

Purification (Comment) Organism
multienzyme complex which exhibits activities of EC 4.2.1.17, EC 2.3.1.16, EC 5.1.2.3, EC 1.1.1.35, and EC 5.3.3.3 Escherichia coli

Reaction

Reaction Comment Organism Reaction ID
(S)-3-Hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA the multienzyme complex catalyzes the rapid and direct dehydration of D-3-hydroxy-4-trans-decenoyl-CoA to 2-trans,4-trans-decadienoyl-CoA, which is slowly hydated to L-3-hydroxy-4-trans-decenoyl-CoA Escherichia coli
(S)-3-Hydroxybutanoyl-CoA = (R)-3-hydroxybutanoyl-CoA epimerization occurs solely by a dehydration/hydration mechanism Escherichia coli

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
D-3-Hydroxy-4-trans-decenoyl-CoA
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Escherichia coli L3-Hydroxy-4-trans-decenoyl-CoA
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