Information on EC 2.3.1.71 - glycine N-benzoyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
Mark a special word or phrase in this record:
Search Reference ID:
Select one or more organisms in this record:
Show additional data
Do not include text mining results
Include (text mining) results (more...)
Include results (AMENDA + additional results, but less precise; more...)


The expected taxonomic range for this enzyme is: Eutheria

EC NUMBER
COMMENTARY hide
2.3.1.71
-
RECOMMENDED NAME
GeneOntology No.
glycine N-benzoyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
benzoyl-CoA + glycine = CoA + hippurate
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Acyl group transfer
-
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Phenylalanine metabolism
-
-
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
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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
benzoyl-CoA + glutaminic acid
CoA + N-benzoylglutamic acid
show the reaction diagram
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-benzoyl-L-glutamine
show the reaction diagram
24% of the rate with glycine and benzoyl-CoA
-
-
?
benzoyl-CoA + L-glutamine
CoA + N-benzoylglutamine
show the reaction diagram
benzoyl-CoA + serine
CoA + N-benzoylserine
show the reaction diagram
heptanoyl-CoA + glycine
CoA + N-heptanoylglycine
show the reaction diagram
indoleacetyl-CoA + glycine
CoA + N-indoleacetylglycine
show the reaction diagram
-
-
-
-
?
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
phenylacetyl-CoA + L-glutamine
CoA + N-phenylacetyl-L-glutamine
show the reaction diagram
20% of the rate with glycine and benzoyl-CoA
-
-
?
propionyl-CoA + glycine
CoA + N-propionylglycine
show the reaction diagram
salicyl-CoA + glycine
CoA + N-salicylglycine
show the reaction diagram
tiglyl-CoA + glycine
CoA + N-tiglylglycine
show the reaction diagram
additional information
?
-
-
enzyme synthesis is induced in response to cholestasis
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
enzyme synthesis is induced in response to cholestasis
-
-
-
INHIBITORS
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
-
1 mM, 24C, 90% inhibition after 40 min
phenylacetyl-CoA
-
-
potassium phosphate
-
-
Rb+
-
110 mM
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
997 - 1573
Ala
129
Asn
-
-
0.016 - 998
benzoyl-CoA
130
Butyryl-CoA
-
-
353
Gln
-
-
1148
Glu
-
-
6 - 6.4
Gly
0.0016 - 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
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
enzyme activity shows significant increase between the 1st and 7th day after common bile duct ligation
-
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30500
-
gel filtration
32400
-
sucrose density gradient centrifugation
33500
-
gel filtration
33800
-
gel filtration
34000
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-70C, enzyme retains more than half of its activity after several months
-
4C, 3 weeks, enzyme retains about 80% of its initial activity
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
partial
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
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
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E226Q
about 3fold increase in Km value for lgycine
APPLICATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
medicine
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