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Literature summary for 6.2.1.3 extracted from

  • Normann, P.T.; Thomassen, M.S.; Christiansen, E.N.; Flatmark, T.
    Acyl-CoA synthetase activity of rat liver microsomes. Substrate specificity with special reference to very-long-chain and isomeric fatty acids (1981), Biochim. Biophys. Acta, 664, 416-427.
    View publication on PubMed

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
additional information
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additional information
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Rattus norvegicus

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
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Rattus norvegicus
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Organism

Organism UniProt Comment Textmining
Rattus norvegicus
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Source Tissue

Source Tissue Comment Organism Textmining
liver
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Rattus norvegicus
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + long-chain carboxylic acid + CoA optimal activity at 12:0 with saturated fatty acids as substrate, at 14:1 with mono-unsaturated fatty acids. The mono-unsaturated fatty acids from 14:1 to 22:1 give higher activity than the corresponding saturated fatty acids. Position of the double bond and the cis/trans configuration have little effect on the velocity values except for 22:1(11) (cis) which reveals a 2fold higher activity than 22:1(13)(cis) fatty acid. Polyunsaturated fatty acid 22:6(all cis) is a much better substrate than other C22 fatty acids Rattus norvegicus AMP + diphosphate + long-chain acyl-CoA
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