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Literature summary for 1.3.1.8 extracted from

  • Prasad, M.R.; Nagi, M.N.; Cook, L.; Cinti, D.L.
    Kinetic evidence for two separate trans-2-enoyl CoA reductases in rat hepatic microsomes: NADPH-specific short chain- and NAD(P)H-dependent long chain-reductase (1983), Biochem. Biophys. Res. Commun., 113, 659-665.
    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
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Rattus norvegicus
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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
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2-trans-hexadecenoyl-CoA + NADPH
-
Rattus norvegicus hexadecanoyl CoA + NADP+
-
?
2-trans-hexenoyl-CoA + NAD(P)H
-
Rattus norvegicus hexanoyl-CoA + NADP+
-
?
2-trans-octenoyl-CoA + NAD(P)H
-
Rattus norvegicus octanoyl-CoA + NADP+
-
?
crotonyl-CoA + NAD(P)H
-
Rattus norvegicus butanoyl-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