Information on EC 2.3.1.13 - glycine N-acyltransferase

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The expected taxonomic range for this enzyme is: Eutheria

EC NUMBER
COMMENTARY
2.3.1.13
-
RECOMMENDED NAME
GeneOntology No.
glycine N-acyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
acyl-CoA + glycine = CoA + N-acylglycine
show the reaction diagram
sequential reaction mechanism, acyl-CoA substrate adds to the enzyme first, glycine adds before CoA leaves and the peptide product dissociates last
-
acyl-CoA + glycine = CoA + N-acylglycine
show the reaction diagram
residue Glu226 functions to deprotonate glycine, facilitating nucleophilic attack on the acyl-CoA substrate
-, Q2KIR7
acyl-CoA + glycine = CoA + N-acylglycine
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
KEGG Link
MetaCyc Link
Phenylalanine metabolism
-
SYSTEMATIC NAME
IUBMB Comments
acyl-CoA:glycine N-acyltransferase
The CoA derivatives of a number of aliphatic and aromatic acids, but not phenylacetyl-CoA or (indol-3-yl)acetyl-CoA, can act as donor. Not identical with EC 2.3.1.68 glutamine N-acyltransferase or EC 2.3.1.71 glycine N-benzoyltransferase.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
acyltransferase, glycine
-
-
-
-
GlyAT
Q6IB77
-
GLYATL1
Q969I3
-
GLYATL2
Q8WU03
-
glycine acyltransferase
-
-
-
-
glycine N-acyltransferase
Q6IB77
-
glycine-N-acylase
-
-
-
-
glycine-N-acyltransferase
Q969I3
-
CAS REGISTRY NUMBER
COMMENTARY
9029-95-2
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
isoform Glyat
UniProt
Manually annotated by BRENDA team
isoform Glyatl2
UniProt
Manually annotated by BRENDA team
New Zealand white rabbits
-
-
Manually annotated by BRENDA team
Sprague-Dawley rats
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
Q6IB77
5 novel single nucleotide polymorphisms of the GlyAT gene, including a polymorphism resulting in an amino acid change of Arg131His, in Japanese individuals are identified. The allelic frequency of this polymorphism in Japanese is 0.005, and none possessed this single nucleotide polymorphism among 31 caucasian individuals. Three genetic polymorphisms, 7527 T to A, 21289G to A and 21364A to G, cause the amino acid changes
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
-
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
-
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
-
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
-
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
-
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
the CoA derivatives of a number of aliphatic and aromatic acids, e.g. benzoyl-CoA and butyryl-CoA can act as acyl donor
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
the CoA derivatives of a number of aliphatic and aromatic acids, e.g. benzoyl-CoA and butyryl-CoA can act as acyl donor
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
the CoA derivatives of a number of aliphatic and aromatic acids, e.g. benzoyl-CoA and butyryl-CoA can act as acyl donor
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
phenylacetyl-CoA acts as acyl donor
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
salicyl-CoA acts as acyl donor
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
phenylacetyl-CoA or indoleacetyl-CoA can not act as acyl donor
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
phenylacetyl-CoA or indoleacetyl-CoA can not act as acyl donor
-
?
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
enzyme is believed to catalyze the formation of both the straight-chain and branched-chain acylglycines from the corresponding acyl-CoA esters
-
?
acyl-CoA + L-asparagine
?
show the reaction diagram
-
-
-
-
?
acyl-CoA + L-glutamine
?
show the reaction diagram
-
-
-
-
?
arachidonoyl-CoA + glycine
CoA + N-arachidonoylglycine
show the reaction diagram
Q8WU03
-
-
-
?
benzoyl-CoA + glycine
CoA + N-benzoylglycine
show the reaction diagram
-
-
-
?
benzoyl-CoA + glycine
CoA + N-benzoylglycine
show the reaction diagram
-
-
-
?
benzoyl-CoA + glycine
CoA + N-benzoylglycine
show the reaction diagram
-
-
-
?
benzoyl-CoA + glycine
CoA + N-benzoylglycine
show the reaction diagram
-, Q2KIR7
-
-
-
?
benzoyl-CoA + glycine
CoA + N-benzoylglycine
show the reaction diagram
Q6IB77
best substrates are benzoyl-CoA as an acyl donor and glycine as acyl acceptor
-
-
?
benzoyl-CoA + L-alanine
CoA + N-benzoyl-L-alanine
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + L-asparagine
CoA + N-benzoyl-L-asparagine
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + L-glutamic acid
CoA + N-benzoyl-L-glutamic acid
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + L-glutamine
CoA + N-benzoyl-L-glutamine
show the reaction diagram
-
-
-
-
?
benzoyl-CoA + L-glutamine
CoA + N-benzoyl-L-glutamine
show the reaction diagram
Q6IB77
24% of the rate with glycine and benzoyl-CoA
-
-
?
butyryl-CoA + glycine
CoA + N-butyrylglycine
show the reaction diagram
-
-
-
-
-
butyryl-CoA + glycine
CoA + N-butyrylglycine
show the reaction diagram
-
19% of activity with benzoyl-coA
-
?
heptanoyl-CoA + glycine
CoA + N-heptanoylglycine
show the reaction diagram
-
3.9% of activity with benzoyl-coA
-
?
isovaleryl-CoA + glycine
CoA + N-isovalerylglycine
show the reaction diagram
-
-
-
?
octanoyl-CoA + glycine
CoA + N-octanoylglycine
show the reaction diagram
-
-
-
?
oleoyl-CoA + glycine
CoA + N-oleoyl-glycine
show the reaction diagram
Q8WU03
-
-
-
?
salicyl-CoA + glycine
CoA + N-salicylglycine
show the reaction diagram
-
-
-
?
salicyl-CoA + glycine
CoA + N-salicylglycine
show the reaction diagram
-
-
-
-
-
salicyl-CoA + glycine
CoA + N-salicylglycine
show the reaction diagram
-
15% of activity with benzoyl-coA
-
?
stearoyl-CoA + glycine
CoA + N-stearoyl-glycine
show the reaction diagram
Q8WU03
-
-
-
?
isovaleryl-CoA + glycine
CoA + N-isovalerylglycine
show the reaction diagram
-
8.4% of activity with benzoyl-coA
-
?
additional information
?
-
Q8WU03
substrates are medium- and long-chain acyl-CoAs ranging from chain-length C8:0-CoA to C18:0-CoA. Enzyme is specific for glycine as an acceptor molecule, and preferentially produces N-oleoyl glycine. No substrates: docosahexanoyl-CoA and chenodeoxycholoyl-CoA, L-alanine, l-serine
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
acyl-CoA + glycine
CoA + N-acylglycine
show the reaction diagram
-
enzyme is believed to catalyze the formation of both the straight-chain and branched-chain acylglycines from the corresponding acyl-CoA esters
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Cs+
-
K+, Rb+, Na+, Li+, Cs+ or NH4+ required for activity
K+
-
K+, Rb+, Na+, Li+, Cs+ or NH4+ required for activity
Li+
-
K+, Rb+, Na+, Li+, Cs+ or NH4+ required for activity
Na+
-
K+, Rb+, Na+, Li+, Cs+ or NH4+ required for activity
NH4+
-
K+, Rb+, Na+, Li+, Cs+ or NH4+ required for activity
Rb+
-
K+, Rb+, Na+, Li+, Cs+ or NH4+ required for activity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
5,5'-dithiobis(2-nitrobenzoate)
-
-
benzoyl-CoA
-
-
benzoylglycine
-
competitive vs. benzoyl-CoA
Butyryl-CoA
-
-
K3PO4
-
100 mM, 68% inhibition
K3PO4
-
100 mM, 43% inhibition
KCl
-
100 mM, 50% inhibition
KCl
-
100 mM, 79% inhibition
KCl
-
100 mM, 88% inhibition
N-benzoyl-L-alanine
-
competitive vs. benzoyl-CoA
N-benzoyl-L-asparagine
-
competitive vs. benzoyl-CoA
N-benzoyl-L-glutamic acid
-
competitive vs. benzoyl-CoA
N-benzoyl-L-serine
-
competitive vs. benzoyl-CoA
N-benzoylglycine
-
-
NaCl
-
100 mM, 53% inhibition; 100 mM, 57% inhibition
NaCl
-
100 mM, 57% inhibition
oleoyl-CoA
Q8WU03
slight substrate inhibition above 0.05 mM
p-chloromercuribenzoate
-
-
p-chloromercuribenzoate
-
1 mM, 90% inhibition after 40 min, 20% activity can be recovered by adding 20fold excess of dithiothreitol, benzoyl-CoA protects
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
997
-
alanine
-
acyl donor benzoyl-CoA
1573
-
alanine
-
acyl donor benzoyl-CoA
129
-
asparagine
-
acyl donor benzoyl-CoA
0.016
-
benzoyl-CoA
-, Q2KIR7
recombinant wild-type, pH 8.0, 30C; wild-type, pH 8.0, 30C
0.018
-
benzoyl-CoA
-, Q2KIR7
mutant E226Q, pH 8.0, 30C
0.02
-
benzoyl-CoA
-
cosubstrate glycine
13
-
benzoyl-CoA
-
cosubstrate glycine
15.2
-
benzoyl-CoA
-
cosubstrate alanine
22.5
-
benzoyl-CoA
-
-
41
-
benzoyl-CoA
-
cosubstrate alanine
57.9
-
benzoyl-CoA
-
-
105
-
benzoyl-CoA
-
cosubstrate glutamine
157
-
benzoyl-CoA
-
cosubstrate asparagine
160
-
benzoyl-CoA
-
cosubstrate glycine
998
-
benzoyl-CoA
-
cosubstrate glutamic acid
0.7
-
Butyryl-CoA
-
cosubstrate glycine
1150
-
glutamic acid
-
acyl donor benzoyl-CoA
353
-
glutamine
-
acyl donor benzoyl-CoA
0.0016
-
glycine
-, Q2KIR7
wild-type, pH 8.0, 30C
0.002
-
glycine
-, Q2KIR7
recombinant wild-type, pH 8.0, 30C
0.003
-
glycine
-
acyl donor salicyl-CoA
0.006
-
glycine
-
acyl donor benzoyl-CoA
0.007
-
glycine
-, Q2KIR7
mutant E226Q, pH 8.0, 30C
0.5
-
glycine
-
acyl donor butyryl-CoA
6
-
glycine
-
acyl donor benzoyl-CoA
6.2
-
glycine
-
acyl donor benzoyl-CoA
6.4
-
glycine
-
acyl donor benzoyl-CoA
7.6
-
glycine
-
acyl donor salicyl-CoA
20
-
glycine
-
acyl donor phenylacetyl-CoA
79
-
glycine
-
acyl donor butyryl-CoA
73.3
-
isovaleryl-CoA
-
-
124
-
isovaleryl-CoA
-
-
108.6
-
Octanoyl-CoA
-
-
198
-
Octanoyl-CoA
-
-
0.0044
-
oleoyl-CoA
Q8WU03
pH not specified in the publication, temperature not specified in the publication
0.15
-
phenylacetyl-CoA
-
cosubstrate glycine
0.03
-
salicyl-CoA
-
cosubstrate glycine
35.6
-
salicyl-CoA
-
-
83.7
-
salicyl-CoA
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.9
-
N-benzoyl-L-alanine
-
-
3
-
N-benzoyl-L-asparagine
-
-
8
-
N-benzoyl-L-glutamic acid
-
-
4.1
-
N-benzoyl-L-serine
-
-
0.075
-
N-benzoylglycine
-
-
0.1
-
N-benzoylglycine
-
-
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.105
-
-
activity in 176000 g supernantant of Triton X-100 solubilized preparations
0.19
-
-
activity in liver 4 h after birth
0.7
-
-
-
2.51
-
-
activity in liver of a 7 months old child
6.38
-
-
mean activity in liver of children aged 18 months to 11 years
6.5
-
-
activity in liver of adults aged 24 to 40 years
9.7
-
-
-
10
-
-
acyl donor benzoyl-CoA
13.9
-
-
-
32
-
-
-
500
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
7.5
8.5
-, Q2KIR7
wild-type
8.4
8.6
-
-
8.8
9.5
-
kidney enzyme
additional information
-
-, Q2KIR7
for mutant E226Q, activity increases significantly when raising the pH above 8.0, while for wild-type, activity remains more or less stable up to pH 9.0
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
8
10
-
approx. 35% of maximal activity at pH 8.0, approx. 40% of maximal activity at pH 10.0, kidney enzyme
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
6.44
-
Q969I3
calculated
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
kidney enzyme is located in the matrix, probably not membrane bound
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24000
-
-
gel filtration
33000
-
-
SDS-PAGE, sucrose density gradient centrifugation
33500
-
-
gel filtration
35100
-
Q969I3
SDS-PAGE, Western blot analysis
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
monomer
-
1 * 33000, SDS-PAGE
monomer
-
1 * 33500, SDS-PAGE
monomer
-
-
monomer
-
1 * 33000, SDS-PAGE
monomer
-
1 * 30000, SDS-PAGE
monomer
-
-
monomer
-
1 * 36000, SDS-PAGE
monomer
-
27000, SDS-PAGE
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
enzyme fractions from hydroxylapatite column are inactivated by dialysis or concentration by ultracentrifugation
-
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
4C, 1-3 weeks, about 25% loss of activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
DE-52, gel filtration, chromatofocusing
-
ammonium sulfate, hydroxylapatite, Biogel P 100, Blue-dextran agarose, chromatofocusing
-
ammonium sulfate, Bio-gel P-150
-
ammonium sulfate, DEAE-Sephacel, heparin-Sepharose 4B, Biogel P 100, hydroxylapatite, Blue-Dextran agarose
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-
-, Q2KIR7
overexpression in HEK293T cells, transient expression in COS-7 cells as myc-tagged GLYATL1 fusion protein, GLYATL1 is involved in heat shock response pathway
Q969I3
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
isoform Glyat expression is suppressed in all hepatocellular carcinomas, but not in other liver diseases. Glyat repression in cancerous cells in the liver is controlled at the transcriptional level
Q6IB77
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
E226Q
-, Q2KIR7
about 3fold increase in Km value for lgycine
Arg131His
Q6IB77
polymorphism resulting in an amino acid change of Arg131His, in Japanese individuals
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
medicine
Q6IB77
isoform Glyat expression is suppressed in all hepatocellular carcinomas, but not in other liver diseases. Glyat repression in cancerous cells in the liver is controlled at the transcriptional level