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Literature summary 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

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

Inhibitors

EC Number Inhibitors Comment Organism Structure
2.3.1.71 3'-dephospho-CoA
-
 Bos taurus
2.3.1.71 CoA in absence of KCl, 0.1 mM CoA inhibits activity over 40% irrespective of the concentration of glycine. In presence of KCl, CoA inhibits activity only slightly, less than 10%. In presence of potassium phosphate the inhibition is reduced to less than 2%. 2.5 mM, almost complete inhibition of salt-free enzyme Bos taurus
2.3.1.71 hippuric acid competitive with respect to benzoyl-CoA Bos taurus
2.3.1.71 K+ K+ is a competitive inhibitor for benzoyl-coenzyme A, not a competitive inhibitor for salicylyl-CoA, K+ increases Km-value for glycine 10fold Bos taurus
2.3.1.71 Li+ 110 mM Bos taurus
2.3.1.71 Mg2+
-
 Bos taurus
2.3.1.71 Na+ 110 mM Bos taurus
2.3.1.71 potassium phosphate
-
 Bos taurus
2.3.1.71 Rb+ 110 mM Bos taurus
2.3.1.192 citrate 40 mM, 22% residual activity Bos taurus
2.3.1.192 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
2.3.1.192 K2SO4 55 mM, 67% residual activity at physiological substrate concentration, 110% of initial activity at high substrate concentration Bos taurus
2.3.1.192 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
2.3.1.192 Mg2+ 1 mM, about 10% activation, 10 mM, inihibition at physiological substrate concentration, activation at high substrate concnetration Bos taurus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
2.3.1.71 2
-
 glycine reaction with benzoyl-CoA or salicylyl-CoA Bos taurus

Localization

EC Number Localization Comment Organism GeneOntology No. Textmining
2.3.1.71 mitochondrion
-
 Bos taurus 5739
-
2.3.1.192 mitochondrion
-
 Bos taurus 5739
-

Metals/Ions

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

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
2.3.1.71 34000
-
 gel filtration Bos taurus
2.3.1.192 32000
-
 gel filtration Bos taurus
2.3.1.192 33500
-
 1 * 33500, SDS-PAGE Bos taurus

Organism

EC Number Organism UniProt Comment Textmining
2.3.1.71 Bos taurus
-
-
-
2.3.1.192 Bos taurus
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
2.3.1.71
-
 Bos taurus
2.3.1.192
-
 Bos taurus

Source Tissue

EC Number Source Tissue Comment Organism Textmining
2.3.1.71 liver
-
 Bos taurus
-
2.3.1.192 liver
-
 Bos taurus
-

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
2.3.1.71 1
-
-
 Bos taurus
2.3.1.192 49
-
 pH 8.0, 30°C Bos taurus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
2.3.1.71 benzoyl-CoA + glycine
-
 Bos taurus CoA + N-benzoylglycine
-
 ?
2.3.1.71 salicyl-CoA + glycine
-
 Bos taurus CoA + salicyluric acid
-
 ?
2.3.1.192 1-naphthylacetyl-CoA + glycine best substrate Bos taurus 1-naphthylacetylglycine + CoA
-
 ?
2.3.1.192 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 ?
-
 ?
2.3.1.192 phenylacetyl-CoA + glycine best substrate Bos taurus phenylacetylglycine + CoA
-
 ?
2.3.1.192 phenylacetyl-CoA + L-arginine at 20% of the rate with glycine Bos taurus ? + CoA
-
 ?
2.3.1.192 phenylacetyl-CoA + L-glutamine at 6% of the rate with glycine Bos taurus ? + CoA
-
 ?

Subunits

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

Ki Value [mM]

EC Number Ki Value [mM] Ki Value maximum [mM] Inhibitor Comment Organism Structure
2.3.1.71 0.03
-
 hippuric acid
-
 Bos taurus

pI Value

EC Number Organism Comment pI Value Maximum pI Value
2.3.1.192 Bos taurus isoelectric focusing
-
 7.5

IC50 Value

EC Number IC50 Value IC50 Value Maximum Comment Organism Inhibitor Structure
2.3.1.192 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