Information on EC 2.4.1.91 - flavonol 3-O-glucosyltransferase and Organism(s) Vitis vinifera

for references in articles please use BRENDA:EC2.4.1.91
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This record set is specific for:
Vitis vinifera


The taxonomic range for the selected organisms is: Vitis vinifera

The enzyme appears in selected viruses and cellular organisms

EC NUMBER
COMMENTARY hide
2.4.1.91
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RECOMMENDED NAME
GeneOntology No.
flavonol 3-O-glucosyltransferase
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
hexosyl group transfer
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
daphnetin modification
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flavonol acylglucoside biosynthesis I - kaempferol derivatives
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flavonol acylglucoside biosynthesis III - quercetin derivatives
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kaempferol gentiobioside biosynthesis
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kaempferol glycoside biosynthesis (Arabidopsis)
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kaempferol triglucoside biosynthesis
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myricetin gentiobioside biosynthesis
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quercetin gentiotetraside biosynthesis
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quercetin glucoside biosynthesis (Allium)
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quercetin glycoside biosynthesis (Arabidopsis)
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quercetin triglucoside biosynthesis
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rutin biosynthesis
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Flavone and flavonol biosynthesis
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Metabolic pathways
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Biosynthesis of secondary metabolites
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:flavonol 3-O-D-glucosyltransferase
Acts on a variety of flavonols, including quercetin and quercetin 7-O-glucoside. Different from EC 2.4.1.81 (flavone 7-O-beta-glucosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
50812-18-5
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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
dTDP-glucose + quercetin
dTDP + quercetin 3-O-beta-D-glucoside
show the reaction diagram
-
-
-
-
?
dTDP-xylose + quercetin
dTDP + quercetin 3-O-beta-D-xylose
show the reaction diagram
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low activity
-
-
?
GDP-glucose + quercetin
GDP + quercetin 3-O-beta-D-glucoside
show the reaction diagram
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low activity
-
-
?
UDP-5-thio-glucose + quercetin
UDP + quercetin 3-O-5-thio-beta-D-glucoside
show the reaction diagram
-
low activity
-
-
?
UDP-alpha-D-glucose + kaempferol
UDP + kaempferol 3-O-beta-D-glucoside
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-glucose + quercetin
UDP + quercetin 3-O-beta-D-glucoside
show the reaction diagram
-
-
-
-
?
UDP-galactose + quercetin
UDP + quercetin 3-O-beta-D-galactoside
show the reaction diagram
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low activity
-
-
?
UDP-glucose + delphinidin
UDP + delphinidin 3-O-glucoside
show the reaction diagram
-
-
-
-
?
UDP-mannose + quercetin
UDP + quercetin 3-O-beta-D-mannoside
show the reaction diagram
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very low activity
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-
?
UDP-N-acetylglucose + quercetin
UDP + quercetin 3-O-N-acetylglucoside
show the reaction diagram
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low activity
-
-
?
UDP-xylose + quercetin
UDP + quercetin 3-O-beta-D-xylose
show the reaction diagram
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low activity
-
-
?
UDPglucose + a flavonol
UDP + a flavonol 3-O-D-glucoside
show the reaction diagram
UDPglucose + cyanidin
UDP + cyanidin 3-O-glucoside
show the reaction diagram
-
-
-
-
?
UDPglucose + malvidin
UDP + malvidin 3-O-glucoside
show the reaction diagram
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-
-
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?
UDPglucose + quercetin
UDP + quercetin 3-O-glucoside
show the reaction diagram
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-
-
-
?
additional information
?
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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
UDP-alpha-D-glucose + kaempferol
UDP + kaempferol 3-O-beta-D-glucoside
show the reaction diagram
-
-
-
-
?
UDP-alpha-D-glucose + quercetin
UDP + quercetin 3-O-beta-D-glucoside
show the reaction diagram
-
-
-
-
?
UDPglucose + a flavonol
UDP + a flavonol 3-O-D-glucoside
show the reaction diagram
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.03
cyanidin
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recombinant enzyme
0.016
delphinidin
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recombinant enzyme
0.042
kaempferol
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0.0357
malvidin
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recombinant enzyme
0.015 - 0.031
quercetin
1.9
UDPglucose
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recombinant enzyme
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.8
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assay at
8
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reaction with quercetin or cyanidin
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
37
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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gene expression in the red-skin sports seems to be the result of a mutation in this gene or a mutation in a regulatory gene controlling its expression
Manually annotated by BRENDA team
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant detagged enzyme bound to UDP-2-fluoroglucose and kaempferol, or with UDP and quercetin, hanging drop method, 4.8 mg/ml protein in 5 mM Tris (2-carboxyethyl) phosphine HCl, 10 mM Tris–Cl, pH 8.3, diluted 1:1 with mother liquor which contains 18–22% polyethylene glycol 10 000, 0.1M Bis-Tris propane, pH 7.0, and 0–0.5% v/v Pluronic F-68, crystals appear within 24 h, X-ray diffraction structure determination and analysis at 2.2 A resolution
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
at least three freeze-thaw cycles can be tolerated without apparent loss of activity
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 4°C, the recombinant enzyme is stable for at least 120 h
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-80°C, stable for many months
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant enzyme
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recombinant His-tagged enzyme from Escherichia coli to homogeneity, the His-tag is cleaved off
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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
gene VvGT1, expression of His-tagged enzyme in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
D374A
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site-directed mutagenesis, inactive mutant
H20A
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site-directed mutagenesis, inactive mutant
Q375H
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q375N
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Q375N/T141A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
T141A
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site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme