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Literature summary for 1.3.1.8 extracted from

  • Nagi, M.N.; Cook, L.; Ghesquier, D.; Cinti, D.L.
    Site of inhibition of rat liver microsomal fatty acid chain elongation system by dec-2-ynoyl coenzyme A. Possible mechanism of inhibition (1986), J. Biol. Chem., 261, 13598-13605.
    View publication on PubMed

Inhibitors

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

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Rattus norvegicus
-
-

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.
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 ?
-
?

Synonyms

Synonyms Comment Organism
trans-2-enoyl-CoA reductase
-
Rattus norvegicus

Cofactor

Cofactor Comment Organism Structure
NADPH inactive with NADH Rattus norvegicus