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Literature summary for 6.2.1.3 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

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

KM Value [mM]

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

Organism

Organism UniProt Comment Textmining
Pseudomonas aeruginosa
-
-
-
Rattus norvegicus
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Rattus norvegicus
-

Substrates and Products (Substrate)

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