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Literature summary for 2.3.1.5 extracted from

  • Andres, H.H.; Klem, A.J.; Schopfer, L.M.; Harrison, J.K.; Weber, W.W.
    On the active site of liver acetyl-CoA. Arylamine N-acetyltransferase from rapid acetylator rabbits (III/J) (1988), J. Biol. Chem., 263, 7521-7527.
    View publication on PubMed

Inhibitors

Inhibitors Comment Organism Structure
Bromoacetanilide product analogue, kinetics Columba sp.
Bromoacetanilide product analogue, kinetics Oryctolagus cuniculus
Chloro-beta-naphthalide
-
Oryctolagus cuniculus
coenzyme A
-
Columba sp.
coenzyme A
-
Oryctolagus cuniculus
iodoacetic acid
-
Columba sp.
iodoacetic acid
-
Oryctolagus cuniculus

Localization

Localization Comment Organism GeneOntology No. Textmining

Organism

Organism UniProt Comment Textmining
Columba sp.
-
pigeon
-
Oryctolagus cuniculus
-
new Zealand white
-
Oryctolagus cuniculus
-
rapid acetylator type III/J
-

Reaction

Reaction Comment Organism Reaction ID
acetyl-CoA + an arylamine = CoA + an N-acetylarylamine mechanism and characterization of active site Oryctolagus cuniculus
acetyl-CoA + an arylamine = CoA + an N-acetylarylamine mechanism and characterization of active site Columba sp.

Source Tissue

Source Tissue Comment Organism Textmining
liver
-
Oryctolagus cuniculus
-
liver
-
Columba sp.
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
acetyl-CoA + 4-ethylaniline
-
Oryctolagus cuniculus CoA + 4-ethylacetanilide
-
?
acetyl-CoA + 4-ethylaniline
-
Columba sp. CoA + 4-ethylacetanilide
-
?

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
25
-
4-ethylaniline
-
Oryctolagus cuniculus

Ki Value [mM]

Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
0.67
-
Bromoacetanilide
-
Oryctolagus cuniculus