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Literature summary for 6.2.1.3 extracted from

  • Vessey, D.A.; Kelley, M.; Warren, R.S.
    Characterization of triacsin C inhibition of short-, medium-, and long-chain fatty acid: CoA ligases of human liver (2004), J. Biochem. Mol. Toxicol., 18, 100-106.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Triacsin C competitive inhibitor of palmitate binding for microsomal and mitochondrial enzyme, uncompetitive inhibitor versus CoA. Biphasic Dixon plot, a high-affinity site with a Ki of 0.0001 mM accounts for a maximum of 70% of the inhibition. A low affinity site with a Ki of 0.006 mM accounts for a maximum of 30% inhibition Homo sapiens

Localization

Localization Comment Organism GeneOntology No. Textmining
microsome
-
Homo sapiens
-
-
mitochondrion
-
Homo sapiens 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ high affinity triacsin C inhibition of both mitochondrial and microsomal enzyme form requires high concentrations of free Mg2+. Low affinity triacsin C inhibition is also enhanced by low Mg2+ Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens
-
-
-

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Homo sapiens
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + palmitate + CoA
-
Homo sapiens AMP + diphosphate + palmitoyl-CoA
-
?

Synonyms

Synonyms Comment Organism
LACS
-
Homo sapiens
long-chain fatty acid:CoA ligase
-
Homo sapiens
long-chain fatty acyl-CoA synthetase
-
Homo sapiens

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
additional information
-
additional information biphasic Dixon plot with the inhibitor triacsin C. A high-affinity site with a Ki of 0.0001 mM accounts for a maximum of 70% of the inhibition. A low affinity site with a Ki of 0.006 mM accounts for a maximum of 30% inhibition Homo sapiens