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Literature summary extracted from

  • Mizugaki, M.; Uchiyama, M.
    Possible role of NADPH-dependent enoyl coenzyme A reductase in -oxidation of unsaturated fatty acids (1973), Biochem. Biophys. Res. Commun., 50, 48-53.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.3.1.8 iodoacetamide
-
Rattus norvegicus
1.3.1.8 N-ethylmaleimide
-
Rattus norvegicus
1.3.1.8 p-chloromercuribenzoate
-
Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.3.1.8 1.2
-
2-cis-octenoyl-CoA
-
Rattus norvegicus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
1.3.1.8 mitochondrion
-
Rattus norvegicus 5739
-

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
1.3.1.8 additional information Rattus norvegicus role in beta-oxidation of fatty acids ?
-
?

Organism

EC Number Organism UniProt Comment Textmining
1.3.1.8 Rattus norvegicus
-
no information in the literature concerning reduction of cis-2-enoyl-CoA substrates, thus classification of rat enzyme according to EC 1.3.1.8 or EC 1.3.1.38 impossible
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
1.3.1.8 liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.3.1.8 2-cis-octenoyl-CoA + NADPH
-
Rattus norvegicus octanoyl-CoA + NADP+
-
?
1.3.1.8 2-trans-octenoyl-CoA + NAD(P)H trans isomer exhibits 1/3 of activity of cis isomer Rattus norvegicus octanoyl-CoA + NADP+
-
?
1.3.1.8 additional information role in beta-oxidation of fatty acids Rattus norvegicus ?
-
?

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.3.1.8 7 8.5
-
Rattus norvegicus

Cofactor

EC Number Cofactor Comment Organism Structure
1.3.1.8 NADPH inactive with NADH Rattus norvegicus