We're sorry, but BRENDA doesn't work properly without JavaScript. Please make sure you have JavaScript enabled in your browser settings.
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
IUBMB Comments Not identical with EC 2.3.1.13 (glycine N-acyltransferase).
This enzyme was purified from bovine liver mitochondria. L-asparagine, L-glutamine and L-arginine are alternative substrates to glycine, but have higher Km values.
The enzyme appears in viruses and cellular organisms
Synonyms
phenylacetyltransferase, arylacetyl acyl-coa:amino acid n-acyltransferase,
more
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
arylacetyl acyl-CoA:amino acid N-acyltransferase
-
-
arylacetyl-CoA N-acyltransferase
-
-
-
-
phenylacetyltransferase
-
-
arylacetyltransferase
-
-
-
-
arylacetyltransferase
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
phenylacetyl-CoA + glycine = CoA + phenylacetylglycine
phenylacetyl-CoA + glycine = CoA + phenylacetylglycine
-
-
-
-
phenylacetyl-CoA + glycine = CoA + phenylacetylglycine
sequential reaction mechanism in which the acyl-CoA substrate adds to the enzyme first, glycine adds before CoA leaves, and the peptide product dissociates last
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
phenylacetyl-CoA:glycine N-phenylacetyltransferase
Not identical with EC 2.3.1.13 (glycine N-acyltransferase).
This enzyme was purified from bovine liver mitochondria. L-asparagine, L-glutamine and L-arginine are alternative substrates to glycine, but have higher Km values.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
1-naphthylacetyl-CoA + glycine
1-naphthylacetylglycine + CoA
-
best substrate
-
-
?
1-naphtylacetyl-CoA + L-glutamine
? + CoA
-
3-5% of the rate with phenacetyl-CoA
-
-
?
2,4-dichlorophenoxyacetyl-CoA + glycine
2,4-dichlorophenoxyacetylglycine + CoA
-
-
-
-
?
indoleacetyl-CoA + glycine
N-indoleacetylglycine + CoA
-
-
-
-
?
indoleacetyl-CoA + L-glutamine
? + CoA
-
3-5% of the rate with phenacetyl-CoA
-
-
?
phenoxyacetyl-CoA + glycine
phenoxyacetylglycine + CoA
-
overall rate of conjugation of the phenoxyherbicides are slow relative to the standard substrate phenylacetyl-CoA
-
-
?
phenylacetyl-CoA + glycine
phenylacetylglycine + CoA
phenylacetyl-CoA + L-arginine
? + CoA
-
at 20% of the rate with glycine
-
-
?
phenylacetyl-CoA + L-asparagine
? + CoA
-
stereospecific for the L-isomer of asparagine
-
-
?
phenylacetyl-CoA + L-glutamine
? + CoA
phenylacetyl-CoA + L-glutamine
phenylacetyl-L-glutamine + CoA
-
may substitue for glycine, but at lower rate
-
-
?
additional information
?
-
phenylacetyl-CoA + glycine
phenylacetylglycine + CoA
-
-
-
-
?
phenylacetyl-CoA + glycine
phenylacetylglycine + CoA
-
best substrate
-
-
?
phenylacetyl-CoA + glycine
phenylacetylglycine + CoA
-
glycine is the preferred acceptor
-
-
?
phenylacetyl-CoA + L-glutamine
? + CoA
-
at 6% of the rate with glycine
-
-
?
phenylacetyl-CoA + L-glutamine
? + CoA
-
stereospecific for the L-isomer of glutamine
-
-
?
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
-
-
?
additional information
?
-
-
no substrate: 2,4,5-trichlorophenoxyacetyl-CoA
-
-
?
additional information
?
-
-
glycination of phenylacetyl-CoA by human phenacetyltransferase can only be detected at a concentration of glycine above 50 mM, and the rates are below 2% of the rate of glutamination
-
-
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Ca2+
-
activation at both physiological and high substrate concentration
K2SO4
-
55 mM, 67% residual activity at physiological substrate concentration, 110% of initial activity at high substrate concentration
Mg2+
-
1 mM, about 10% activation, 10 mM, inihibition at physiological substrate concentration, activation at high substrate concentration
additional information
-
addition of monovalent cations is required
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
2,4,5-trichlorophenoxyacetyl-CoA
-
competitive
2,4-dichlorophenoxyacetyl-CoA
-
competitive
5,5'-dithiobis(2-nitrobenzoate)
-
phenylacetyl-CoA partially protects phenylacetyltransferase against 5,5'-dithiobis(2-nitrobenzoate) inactivation
acylglycine
-
noncompetitive
citrate
-
40 mM, 22% residual activity
K2SO4
-
55 mM, 67% residual activity at physiological substrate concentration, 110% of initial activity at high substrate concentration
Mg2+
-
1 mM, about 10% activation, 10 mM, inihibition at physiological substrate concentration, activation at high substrate concnetration
Ni2+
-
2 mM, 28% residual activity
p-chloromercuribenzoate
-
-
Zn2+
-
1 mM, 46% residual activity
additional information
-
human enzyme is insensitive to salts
-
CoA
-
noncompetitve
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
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
KCl
-
80 mM KC1, ca. 30% inhibition, inhibition is seen at all concentrations of glutamine up to 150 mM
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
KCl
-
110 mM, 72% residual activity at physiologic substrate concentration, 195% of initial activity at high substrate concentration
phosphate
-
37 mM, 140-175% of initial activity at low and high substrate concentration
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
120
L-glutamine
-
pH 8.0, 30°C
9
glycine
-
cosubstrate phenylacetyl-CoA, pH 8.0, 30°C
1000
glycine
-
cosubstrate 2,4-dichlorophenoxyacetyl-CoA pH 8.0, 30°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.1
CoA
Bos taurus
-
pH 8.0, 30°C, assay at 3.5 mM glycine, 0.020 mM phenylacetyl-CoA and in the absence of ions
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.051
-
pH not specified in the publication, temperature not specified in the publication
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
7.5
-
isoelectric focusing
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
-
brenda
-
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
-
-
brenda
-
-
brenda
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
GLYAL_BOVIN
295
0
33684
Swiss-Prot
other Location (Reliability: 3 )
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
33500
-
1 * 33500, SDS-PAGE
38937
-
x * 38937, calculated
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
?
-
x * 38937, calculated
monomer
-
1 * 33500, SDS-PAGE
monomer
-
1 * 33000, SDS-PAGE
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
proteolytic modification
-
presence of a signal peptide of 5 kDa
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
Nandi, D.L.; Lucas, S.V.; Webster, L.T.
Benzoyl-coenzyme A:glycine N-acyltransferase and phenylacetyl-coenzyme A:glycine N-acyltransferase from bovine liver mitochondria. Purification and characterization
J. Biol. Chem.
254
7230-7237
1979
Bos taurus
brenda
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
J. Biochem. Toxicol.
5
125-135
1990
Bos taurus
brenda
Kelley, M.; Vessey, D.A.
Characterization of the acyl-CoA:amino acid N-acyltransferases from primate liver mitochondria
J. Biochem. Toxicol.
9
153-158
1994
Homo sapiens
brenda
Kelley, M.; Vessey, D.A.
Interaction of 2,4-dichlorophenoxyacetate (2,4-D) and 2,4,5-trichlorophenoxyacetate (2,4,5-T) with the acyl-CoA: amino acid N-acyltransferase enzymes of bovine liver mitochondria
Biochem. Pharmacol.
35
289-295
1986
Bos taurus
brenda
Vessey, D.A.; Lau, E.
Determination of the sequence of the arylacetyl acyl-CoA:amino acid N-acyltransferase from bovine liver mitochondria and its homology to the aralkyl acyl-CoA:amino acid N-acyltransferase
J. Biochem. Mol. Toxicol.
12
275-279
1998
Bos taurus
brenda
Select items on the left to see more content.
html completed