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Literature summary for 6.2.1.2 extracted from

  • Vessey, D.A.; Kelley, M.
    Characterization of the reaction mechanism for the XL-I form of bovine liver xenobiotic/medium-chain fatty acid:CoA ligase (2001), Biochem. J., 357, 283-288.
    View publication on PubMedView publication on EuropePMC
Search for more literature for 6.2.1.2

Inhibitors

Inhibitors Comment Organism Structure
AMP product inhibitor Bos taurus
benzoate competitive inhibitor of butyrate Bos taurus
benzoyl-CoA product inhibitor Bos taurus
Butyrate competitive inhibitor of benzoate Bos taurus
butyryl-CoA competitive inhibitor with respect to both butyrate and benzoate Bos taurus
diphosphate weak product inhibitor, competitive with respect to CoA and mixed inhibitor with respect to benzoate. Mixed type inhibitor with respect to CoA in butyrate:CoA ligase activity Bos taurus

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.007
-
 benzoate
-
 Bos taurus
0.06
-
 CoA
-
 Bos taurus
0.2
-
 ATP
-
 Bos taurus

Localization

Localization Comment Organism GeneOntology No. Textmining
mitochondrion
-
 Bos taurus 5739
-

Metals/Ions

Metals/Ions Comment Organism Structure
Mg2+ activates Bos taurus

Organism

Organism UniProt Comment Textmining
Bos taurus
-
-
-

Purification (Commentary)

Purification (Comment) Organism
-
 Bos taurus

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
 Bos taurus
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
ATP + benzoate + CoA bi uni uni bi ping pong mechanism with ATP binding first, followed in order by benzoate binding, diphosphate release, CoA binding, benzoyl-CoA release and AMP release Bos taurus AMP + diphosphate + benzoyl-CoA
-
 ?
ATP + butyrate + CoA
-
 Bos taurus AMP + diphosphate + butyryl-CoA
-
 ?

Synonyms

Synonyms Comment Organism
xenobiotic/medium-chain fatty acid:CoA ligase
-
 Bos taurus