Information on EC 2.4.1.240 - flavonol-3-O-glycoside glucosyltransferase

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The expected taxonomic range for this enzyme is: Pisum sativum

EC NUMBER
COMMENTARY hide
2.4.1.240
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RECOMMENDED NAME
GeneOntology No.
flavonol-3-O-glycoside glucosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucose + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside = UDP + a flavonol 3-O-beta-D-glucosyl-(1->2)-beta-D-glucosyl-(1->2)-beta-D-glucoside
show the reaction diagram
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
transfer of glycosyl group
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Flavone and flavonol biosynthesis
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kaempferol triglucoside biosynthesis
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quercetin triglucoside biosynthesis
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SYSTEMATIC NAME
IUBMB Comments
UDP-glucose:flavonol-3-O-beta-D-glucosyl-(1->2)-beta-D-glucoside 2'''-O-beta-D-glucosyltransferase
One of three specific glucosyltransferases in pea (Pisum sativum) thatsuccessively add a beta-D-glucosyl group first to O-3 of kaempferol, and then to O-2 of the previously added glucosyl group giving the 3-O-sophoroside and then the 3-O-sophorotrioside (see also EC 2.4.1.91 flavonol 3-O-glucosyltransferase, and EC 2.4.1.239 flavonol-3-O-glucoside glucosyltransferase).
CAS REGISTRY NUMBER
COMMENTARY hide
50812-18-5
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ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
var. Alaska
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-
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
TDP-glucose + a flavonol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
TDP + a flavonol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram
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3fold lower rate than with UDP-glucose as glucosyl donor
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-
?
UDP-glucose + a flavonol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
UDP + a flavonol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram
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highly specific enzyme, specific for flavonol-3-O-diglucosides, 3fold higher rate than with TDP-glucose as glucosyl donor
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-
?
UDP-glucose + kaempferol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
UDP + kaempferol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram
UDP-glucose + myricetin 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
UDP + myricetin 3-O-beta-D-glucosyl-(1-2)-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram
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32% of the activity with kaempferol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
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-
?
UDP-glucose + quercetin 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
UDP + quercetin 3-O-beta-D-glucosyl-(1-2)-beta-D-glucosyl-(1-2)-beta-D-glucoside
show the reaction diagram
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
additional information
?
-
COFACTOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
additional information
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no cofactor requirement
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
-
not activated by divalent cations, 0.1-10 mM
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
UDP
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product inhibition, 0.25 mM, 50% inhibition
additional information
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not inhibited by divalent cations, 0.1-10 mM, EDTA, EGTA, no substrate inhibition
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.008
kaempferol 3-O-beta-D-glucosyl-(1-2)-beta-D-glucoside
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pH 7.3, 30C
0.8
UDP-glucose
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pH 7.3, 30C
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
additional information
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.3
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assay at
7.6
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in 0.2 M Tris-HCl buffer, two pH optima, equally active in 0.2 M Tris-HCl and 0.2 M glycine-NaOH buffer
8.3
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in 0.2 M glycine-NaOH buffer, two pH optima, equally active in 0.2 M Tris-HCl and 0.2 M glycine-NaOH buffer
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
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young leaf tissues have much higher levels of glucosyltransferase activity than the petioles and internodes
Manually annotated by BRENDA team
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-15C or room temperature, partially purified enzyme, 36 h, 80% loss of activity
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4C, 2 weeks, stable
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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
30.7fold, separation of three distinct flavonol:glucosyltransferases
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