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Information on EC 2.3.1.71 - glycine N-benzoyltransferase and Organism(s) Bos taurus and UniProt Accession Q2KIR7

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EC Tree
IUBMB Comments
Not identical with EC 2.3.1.13, glycine N-acyltransferase or EC 2.3.1.68, glutamine N-acyltransferase
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This record set is specific for:
Bos taurus
UNIPROT: Q2KIR7
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The taxonomic range for the selected organisms is: Bos taurus
The enzyme appears in selected viruses and cellular organisms
Reaction Schemes
Synonyms
benzoyl-coa:glycine n-acyltransferase, aralkyl-coa:glycine n-acyltransferase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
aralkyl-CoA:glycine N-acyltransferase
-
-
-
-
benzoyl CoA-amino acid N-acyltransferase
-
-
-
-
benzoyl-CoA:glycine N-acyltransferase
-
-
-
-
benzoyltransferase, glycine
-
-
-
-
glycine N-acyltransferase
-
-
-
-
GNAT
-
-
-
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
benzoyl-CoA + glycine = CoA + hippurate
show the reaction diagram
residue Glu226 functions to deprotonate glycine, facilitating nucleophilic attack on the acyl-CoA substrate
benzoyl-CoA + glycine = CoA + hippurate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
benzoyl-CoA:glycine N-benzoyltransferase
Not identical with EC 2.3.1.13, glycine N-acyltransferase or EC 2.3.1.68, glutamine N-acyltransferase
CAS REGISTRY NUMBER
COMMENTARY hide
71567-07-2
-
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
benzoyl-CoA + glycine
CoA + N-benzoylglycine
show the reaction diagram
-
-
-
?
3-methylcrotonyl-CoA + glycine
CoA + N-3-methylcrotonylglycine
show the reaction diagram
acetyl-CoA + glycine
CoA + N-acetylglycine
show the reaction diagram
benzoyl-CoA + alanine
CoA + N-benzoylalanine
show the reaction diagram
-
0.23% of the activity with Gly
-
?
benzoyl-CoA + glutaminic acid
CoA + N-benzoylglutamic acid
show the reaction diagram
-
0.06% of the activity with Gly
-
-
?
benzoyl-CoA + glycine
CoA + N-benzoylglycine
show the reaction diagram
benzoyl-CoA + L-asparagine
CoA + N-benzoylasparagine
show the reaction diagram
benzoyl-CoA + L-glutamine
CoA + N-benzoylglutamine
show the reaction diagram
benzoyl-CoA + serine
CoA + N-benzoylserine
show the reaction diagram
-
0.03% of the activity with Gly
-
-
?
heptanoyl-CoA + glycine
CoA + N-heptanoylglycine
show the reaction diagram
-
3.9% of the activity with benzoyl-CoA
-
?
isobutyryl-CoA + glycine
CoA + N-isobutyrylglycine
show the reaction diagram
isovaleryl-CoA + glycine
CoA + N-isovalerylglycine
show the reaction diagram
methylmalonyl-CoA + glycine
CoA + N-methylmalonylglycine
show the reaction diagram
-
-
-
-
?
n-butyryl-CoA + glycine
CoA + N-butyrylglycine
show the reaction diagram
naphthylacetyl-CoA + glycine
CoA + N-naphthylacetylglycine
show the reaction diagram
-
-
-
-
?
phenylacetyl-CoA + glycine
CoA + N-phenylacetylglycine
show the reaction diagram
-
-
-
-
?
propionyl-CoA + glycine
CoA + N-propionylglycine
show the reaction diagram
salicyl-CoA + glycine
CoA + salicyluric acid
show the reaction diagram
tiglyl-CoA + glycine
CoA + N-tiglylglycine
show the reaction diagram
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
3'-dephospho-CoA
-
-
benzoylalanine
-
-
benzoylasparagine
-
-
benzoylglutamic acid
-
-
benzoylglycine
-
-
benzoylserine
-
-
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
hippuric acid
indolacetyl-CoA
-
-
Li+
-
110 mM
Na+
-
110 mM
p-hydroxymercuribenzoate
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1 mM, 24°C, 90% inhibition after 40 min
phenylacetyl-CoA
-
-
potassium phosphate
-
-
Rb+
-
110 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.016 - 0.018
benzoyl-CoA
0.0016 - 0.007
glycine
1573
Ala
-
-
129
Asn
-
-
13 - 998
benzoyl-CoA
130
butyryl-CoA
-
-
353
Gln
-
-
1148
Glu
-
-
6 - 6.2
Gly
2 - 79
glycine
170
L-asparagine
-
-
130
L-glutamine
-
-
360
methylmalonyl-CoA
-
-
7.6
salicyl-CoA
-
reaction with salicylyl-CoA
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
55.2
benzoylalanine
-
with variable Gly concentration
8.6
benzoylasparagine
-
with variable Gly concentration
11.8
benzoylglutamic acid
-
with variable Gly concentration
0.2
benzoylglycine
-
with variable Gly concentration
8.2
benzoylserine
-
with variable Gly concentration
0.03 - 0.075
hippuric acid
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5 - 8.5
wild-type
8.4 - 8.6
-
-
additional information
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
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
GLYAT_BOVIN
295
0
33907
Swiss-Prot
other Location (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
32400
-
sucrose density gradient centrifugation
33000
-
1 * 33000, SDS-PAGE
33500
-
gel filtration
33800
-
gel filtration
34000
36000
-
x * 36000, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 36000, SDS-PAGE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E226Q
about 3fold increase in Km value for lgycine
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70°C, enzyme retains more than half of its activity after several months
-
4°C, 3 weeks, enzyme retains about 80% of its initial activity
-
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Manually annotated by BRENDA team
Webster, L.T.
Benzoyl-CoA: amino acid and phenylacetyl-CoA: amino acid N-acyltransferases
Methods Enzymol.
77
301-308
1981
Bos taurus
Manually annotated by BRENDA team
Van der Westhuizen, F.H.; Pretorius, P.J.; Erasmus, E.
The utilization of alanine, glutamic acid, and serine as amino acid substrates for glycine N-acyltransferase
J. Biochem. Mol. Toxicol.
14
102-109
2000
Bos taurus, Homo sapiens
Manually annotated by BRENDA team
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
Manually annotated by BRENDA team
Kelley, M.; Vessey, D.A.
Isolation and characterization of mitochondrial acyl-CoA: glycine N-acyltransferases from kidney
J. Biochem. Toxicol.
8
63-69
1993
Bos taurus
Manually annotated by BRENDA team
Badenhorst, C.P.; Jooste, M.; van Dijk, A.A.
Enzymatic characterization and elucidation of the catalytic mechanism of a recombinant bovine glycine N-acyltransferase
Drug Metab. Dispos.
40
346-352
2012
Bos taurus (Q2KIR7)
Manually annotated by BRENDA team