BRENDA - Enzyme Database
show all sequences of 2.3.1.192

The effects of ions on the conjugation of xenobiotics by the aralkyl-CoA and arylacetyl-CoA N-acyltransferases from bovine liver mitochondria

Kelley, M.; Vessey, D.A.; J. Biochem. Toxicol. 5, 125-135 (1990)

Data extracted from this reference:

Activating Compound
Activating Compound
Commentary
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
Commentary
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
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Bos taurus
5739
-
Metals/Ions
Metals/Ions
Commentary
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]
Commentary
Organism
32000
-
gel filtration
Bos taurus
33500
-
1 * 33500, SDS-PAGE
Bos taurus
Organism
Organism
Primary Accession No. (UniProt)
Commentary
Textmining
Bos taurus
-
-
-
Purification (Commentary)
Commentary
Organism
-
Bos taurus
Source Tissue
Source Tissue
Commentary
Organism
Textmining
liver
-
Bos taurus
-
Specific Activity [micromol/min/mg]
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
49
-
pH 8.0, 30°C
Bos taurus
Substrates and Products (Substrate)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-naphthylacetyl-CoA + glycine
best substrate
487438
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
487438
Bos taurus
?
-
-
-
-
phenylacetyl-CoA + glycine
best substrate
487438
Bos taurus
phenylacetylglycine + CoA
-
-
-
?
phenylacetyl-CoA + L-arginine
at 20% of the rate with glycine
487438
Bos taurus
? + CoA
-
-
-
?
phenylacetyl-CoA + L-glutamine
at 6% of the rate with glycine
487438
Bos taurus
? + CoA
-
-
-
?
Subunits
Subunits
Commentary
Organism
monomer
1 * 33500, SDS-PAGE
Bos taurus
pI Value
Organism
Commentary
pI Value Maximum
pI Value
Bos taurus
isoelectric focusing
-
7.5
IC50 Value
IC50 Value
IC50 Value Maximum
Commentary
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
Activating Compound (protein specific)
Activating Compound
Commentary
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
IC50 Value (protein specific)
IC50 Value
IC50 Value Maximum
Commentary
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
Inhibitors (protein specific)
Inhibitors
Commentary
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 (protein specific)
Localization
Commentary
Organism
GeneOntology No.
Textmining
mitochondrion
-
Bos taurus
5739
-
Metals/Ions (protein specific)
Metals/Ions
Commentary
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] (protein specific)
Molecular Weight [Da]
Molecular Weight Maximum [Da]
Commentary
Organism
32000
-
gel filtration
Bos taurus
33500
-
1 * 33500, SDS-PAGE
Bos taurus
Purification (Commentary) (protein specific)
Commentary
Organism
-
Bos taurus
Source Tissue (protein specific)
Source Tissue
Commentary
Organism
Textmining
liver
-
Bos taurus
-
Specific Activity [micromol/min/mg] (protein specific)
Specific Activity Minimum [µmol/min/mg]
Specific Activity Maximum [µmol/min/mg]
Commentary
Organism
49
-
pH 8.0, 30°C
Bos taurus
Substrates and Products (Substrate) (protein specific)
Substrates
Commentary Substrates
Literature (Substrates)
Organism
Products
Commentary (Products)
Literature (Products)
Organism (Products)
Reversibility
1-naphthylacetyl-CoA + glycine
best substrate
487438
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
487438
Bos taurus
?
-
-
-
-
phenylacetyl-CoA + glycine
best substrate
487438
Bos taurus
phenylacetylglycine + CoA
-
-
-
?
phenylacetyl-CoA + L-arginine
at 20% of the rate with glycine
487438
Bos taurus
? + CoA
-
-
-
?
phenylacetyl-CoA + L-glutamine
at 6% of the rate with glycine
487438
Bos taurus
? + CoA
-
-
-
?
Subunits (protein specific)
Subunits
Commentary
Organism
monomer
1 * 33500, SDS-PAGE
Bos taurus
pI Value (protein specific)
Organism
Commentary
pI Value Maximum
pI Value
Bos taurus
isoelectric focusing
-
7.5
Other publictions for EC 2.3.1.192
No.
1st author
Pub Med
title
organims
journal
volume
pages
year
Activating Compound
Application
Cloned(Commentary)
Crystallization (Commentary)
Engineering
General Stability
Inhibitors
KM Value [mM]
Localization
Metals/Ions
Molecular Weight [Da]
Natural Substrates/ Products (Substrates)
Organic Solvent Stability
Organism
Oxidation Stability
Posttranslational Modification
Purification (Commentary)
Reaction
Renatured (Commentary)
Source Tissue
Specific Activity [micromol/min/mg]
Storage Stability
Substrates and Products (Substrate)
Subunits
Temperature Optimum [°C]
Temperature Range [°C]
Temperature Stability [°C]
Turnover Number [1/s]
pH Optimum
pH Range
pH Stability
Cofactor
Ki Value [mM]
pI Value
IC50 Value
Activating Compound (protein specific)
Application (protein specific)
Cloned(Commentary) (protein specific)
Cofactor (protein specific)
Crystallization (Commentary) (protein specific)
Engineering (protein specific)
General Stability (protein specific)
IC50 Value (protein specific)
Inhibitors (protein specific)
Ki Value [mM] (protein specific)
KM Value [mM] (protein specific)
Localization (protein specific)
Metals/Ions (protein specific)
Molecular Weight [Da] (protein specific)
Natural Substrates/ Products (Substrates) (protein specific)
Organic Solvent Stability (protein specific)
Oxidation Stability (protein specific)
Posttranslational Modification (protein specific)
Purification (Commentary) (protein specific)
Renatured (Commentary) (protein specific)
Source Tissue (protein specific)
Specific Activity [micromol/min/mg] (protein specific)
Storage Stability (protein specific)
Substrates and Products (Substrate) (protein specific)
Subunits (protein specific)
Temperature Optimum [°C] (protein specific)
Temperature Range [°C] (protein specific)
Temperature Stability [°C] (protein specific)
Turnover Number [1/s] (protein specific)
pH Optimum (protein specific)
pH Range (protein specific)
pH Stability (protein specific)
pI Value (protein specific)
Expression
General Information
General Information (protein specific)
Expression (protein specific)
KCat/KM [mM/s]
KCat/KM [mM/s] (protein specific)
708944
Vessey
Determination of the sequence ...
Bos taurus
J. Biochem. Mol. Toxicol.
12
275-279
1998
-
-
1
-
-
-
-
-
2
-
1
-
-
2
-
1
-
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
1
-
-
-
-
-
-
-
-
2
-
1
-
-
-
1
-
-
2
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
487441
Kelley
Characterization of the acyl-C ...
Homo sapiens
J. Biochem. Toxicol.
9
153-158
1994
-
-
-
-
-
-
2
1
1
-
-
-
-
1
-
-
1
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
1
1
-
-
-
-
-
-
1
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
487438
Kelley
The effects of ions on the con ...
Bos taurus
J. Biochem. Toxicol.
5
125-135
1990
2
-
-
-
-
-
5
-
1
3
2
-
-
1
-
-
1
-
-
1
1
-
5
1
-
-
-
-
-
-
-
-
-
1
1
2
-
-
-
-
-
-
1
5
-
-
1
3
2
-
-
-
-
1
-
1
1
-
5
1
-
-
-
-
-
-
-
1
-
-
-
-
-
-
707446
Kelley
Interaction of 2,4-dichlorophe ...
Bos taurus
Biochem. Pharmacol.
35
289-295
1986
-
-
-
-
-
-
2
2
1
-
-
-
-
3
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
2
-
2
1
-
-
-
-
-
-
-
-
1
-
-
4
-
-
-
-
-
-
-
-
-
-
-
-
-
-
-
486265
Nandi
Benzoyl-coenzyme A:glycine N-a ...
Bos taurus
J. Biol. Chem.
254
7230-7237
1979
-
-
-
-
-
-
8
-
-
1
1
-
-
2
-
-
1
1
-
1
1
-
4
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-
-
-
-
-
-
8
-
-
-
1
1
-
-
-
-
1
-
1
1
-
4
1
-
-
-
-
1
-
-
-
-
-
-
-
-
-