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Literature summary for 1.3.1.8 extracted from

  • Nagi, M.N.; Cook, L.; Laguna, J.C.; Cinti, D.L.
    Dual action of 2-decynoyl coenzyme A: inhibitor of hepatic mitochondrial trans-2-enoyl coenzyme A reductase and peroxisomal bifunctional protein and substrate for the mitochondrial beta-oxidation system (1988), Arch. Biochem. Biophys., 267, 1-12.
    View publication on PubMed
Search for more literature for 1.3.1.8

Inhibitors

Inhibitors Comment Organism Structure
2-decynoyl-CoA
-
 Rattus norvegicus

Localization

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

Organism

Organism UniProt Comment Textmining
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

Source Tissue Comment Organism Textmining
liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-trans-decenoyl-CoA + NAD(P)H
-
 Rattus norvegicus decanoyl-CoA + NADP+
-
 ?
additional information NADPH specific trans-enoyl-CoA reductases isolated from rat liver microsomes and mitochondria impossible to classify according to EC 1.3.1.8 or EC 1.3.1.38 because no cis-isomers of 2-enoyl-CoA have been tested as substrates Rattus norvegicus ?
-
 ?

Cofactor

Cofactor Comment Organism Structure
NADPH inactive with NADH Rattus norvegicus