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Literature summary for 1.3.1.8 extracted from

  • Nagi, M.N.; Prasad, M.R.; Cook, L.; Cinti, D.
    Biochemical properties of short- and long-chain rat liver microsomal trans-2-enoyl coenzyme A reductase (1983), Arch. Biochem. Biophys., 226, 50-64.
    View publication on PubMed

Localization

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

Organism

Organism UniProt Comment Textmining
Rattus norvegicus
-
separation in NADPH-specific short-chain enoyl-CoA reductase and NAD(P)H-dependent long-chain enoyl-CoA reductase
-
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-hexadecenoyl-CoA + NADPH
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Rattus norvegicus hexadecanoyl CoA + NADP+
-
?
2-trans-hexenoyl-CoA + NAD(P)H
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Rattus norvegicus hexanoyl-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