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Literature summary for 2.3.1.192 extracted from

  • Kelley, M.; Vessey, D.A.
    The effects of ions on the conjugation of xenobiotics by the aralkyl-CoA and arylacetyl-CoA N-acyltransferases from bovine liver mitochondria (1990), J. Biochem. Toxicol., 5, 125-135.
    View publication on PubMed

Activating Compound

Activating Compound Comment Organism Structure
KCl 110 mM, 72% residual activity at physiologic substrate concentration, 195% of initial activity at high substrate concentration Bos taurus
phosphate 37 mM, 140-175% of initial activity at low and high substrate concentration Bos taurus

Inhibitors

Inhibitors Comment Organism Structure
citrate 40 mM, 22% residual activity Bos taurus
CoA at physiologic concentrations of substrate, the arylacetyl transferase is extensively inhibited by CoA, inhibition is greatly reduced by ions. The 3-phosphate group on CoA is important for binding to the salt-free enzyme but in the presence of ions its importance is diminished Bos taurus
K2SO4 55 mM, 67% residual activity at physiological substrate concentration, 110% of initial activity at high substrate concentration Bos taurus
KCl 110 mM, 72% residual activity at physiologic substrate concentration, 195% of initial activity at high substrate concentration. Inhibition results in a large decrease in the affinity of the enzyme for phenylacetyl-CoA. In the presence of KCl the KD values for phenylacetyl-CoA and naphthylacetyl-CoA are similar, but the KD for glycine is extremely high for 1-naphthylacetyl-CoA conjugation Bos taurus
Mg2+ 1 mM, about 10% activation, 10 mM, inihibition at physiological substrate concentration, activation at high substrate concnetration Bos taurus

Localization

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

Metals/Ions

Metals/Ions Comment Organism Structure
Ca2+ activation at both physiological and high substrate concentration Bos taurus
K2SO4 55 mM, 67% residual activity at physiological substrate concentration, 110% of initial activity at high substrate concentration Bos taurus
Mg2+ 1 mM, about 10% activation, 10 mM, inihibition at physiological substrate concentration, activation at high substrate concentration Bos taurus

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
32000
-
gel filtration Bos taurus
33500
-
1 * 33500, SDS-PAGE 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
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
49
-
pH 8.0, 30°C Bos taurus

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1-naphthylacetyl-CoA + glycine best substrate Bos taurus 1-naphthylacetylglycine + CoA
-
?
additional information arginine and glutamine can substitute for glycine in the phenylacetyl-CoA assay and, while the rates are lower, they are equivalently affected by salt. No substrate: benzoyl-CoA, butyryl-CoA, and salicyl-CoA Bos taurus ?
-
?
phenylacetyl-CoA + glycine best substrate Bos taurus phenylacetylglycine + CoA
-
?
phenylacetyl-CoA + L-arginine at 20% of the rate with glycine Bos taurus ? + CoA
-
?
phenylacetyl-CoA + L-glutamine at 6% of the rate with glycine Bos taurus ? + CoA
-
?

Subunits

Subunits Comment Organism
monomer 1 * 33500, SDS-PAGE Bos taurus

pI Value

Organism Comment pI Value Maximum pI Value
Bos taurus isoelectric focusing
-
7.5

IC50 Value

IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
0.1
-
pH 8.0, 30°C, assay at 3.5 mM glycine, 0.020 mM phenylacetyl-CoA and in the absence of ions Bos taurus CoA