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Literature summary extracted from

  • Tomoda, H.; Igarashi, K.; Omura, S.
    Inhibition of acyl-CoA synthetase by triacsins (1987), Biochim. Biophys. Acta, 921, 595-598.
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
6.2.1.3 Triacsin A non-competitive with respect to ATP and coenzyme A Pseudomonas aeruginosa
6.2.1.3 Triacsin A non-competitive with respect to ATP and coenzyme A Rattus norvegicus
6.2.1.3 Triacsin C
-
 Rattus norvegicus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.2.1.3 0.041
-
 linoleate ATP, , oleate activation Pseudomonas aeruginosa
6.2.1.3 0.101
-
 oleic acid
-
 Pseudomonas aeruginosa
6.2.1.3 1.93
-
 coenzyme A oleate activation Pseudomonas aeruginosa

Organism

EC Number Organism UniProt Comment Textmining
6.2.1.3 Pseudomonas aeruginosa
-
-
-
6.2.1.3 Rattus norvegicus
-
-
-

Source Tissue

EC Number Source Tissue Comment Organism Textmining
6.2.1.3 liver
-
 Rattus norvegicus
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
6.2.1.3 ATP + linoleate + CoA
-
 Pseudomonas aeruginosa AMP + diphosphate + linoleoyl-CoA
-
 ?
6.2.1.3 ATP + oleate + CoA
-
 Rattus norvegicus AMP + diphosphate + oleoyl-CoA
-
 ?
6.2.1.3 ATP + oleate + CoA
-
 Pseudomonas aeruginosa AMP + diphosphate + oleoyl-CoA
-
 ?