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Literature summary for 4.2.1.17 extracted from

  • Qin, Y.M.; Poutanen, M.H.; Helander, H.M.; Kvist, A.P.; Siivari, K.M.; Schmitz, W.; Conzelmann, E.; Hellman, U.; Hiltunen, J.K.
    Peroxisomal multifunctional enzyme of beta-oxidation metabolizing D-3-hydroxyacyl-CoA esters in rat liver: molecular cloning, expression and characterization (1997), Biochem. J., 321, 21-28 .
    View publication on PubMedView publication on EuropePMC
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Cloned(Commentary)

Cloned (Comment) Organism
expression in Pichia pastoris Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
peroxisome
-
 Rattus norvegicus 5777
-

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
crotonyl-CoA + H2O as active as trans-decenoyl-CoA Rattus norvegicus (3S)-3-hydroxybutanoyl-CoA
-
 ?
trans-decenoyl-CoA + H2O as active as crotonyl-CoA Rattus norvegicus ?
-
 ?

Synonyms

Synonyms Comment Organism
2-enoyl-CoA hydratase 1 is part of peroxisomal multifunctional enzyme perMFE-I together with L-specific 3-hydroxyacyl-CoA dehydrogenase (1.1.1.35) Rattus norvegicus
perMFE-I peroxisomal multifunctional enzyme perMFE-I has 2-enoyl-CoA hydratase 1 activity (L-specific, EC 4.2.1.17) and L-specific 3-hydroxyacyl-CoA dehydrogenase (1.1.1.35) activity. Peroxisomal multifunctional enzyme perMFE-II has 2-enoyl-CoA hydratase 2 (D-specific) activity and D-specific 3-hydroxyacyl-CoA dehydrogenase (1.1.1.36) activity Rattus norvegicus