Information on EC 2.4.1.B71 - flavonol-3-O-glucuronosyltransferase

Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
Specify your search results
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: Vitis vinifera

EC NUMBER
COMMENTARY hide
2.4.1.B71
-
RECOMMENDED NAME
GeneOntology No.
flavonol-3-O-glucuronosyltransferase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-glucuronate + a flavonol = UDP + a flavonol 3-O-beta-D-glucuronoside
show the reaction diagram
-
-
-
-
SYSTEMATIC NAME
IUBMB Comments
UDP-glucuronic acid:flavonol-3-O-glucuronosyltransferase
-
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
physiological function
-
the enzyme catalyzes the 3-O-specific glucuronosylation of flavonols using UDP-glucuronic acid as a sugar donor to produce flavonol 3-O-glucosides, which are important bioactive phytochemicals
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-glucuronate + a flavonol
UDP + a flavonol 3-O-beta-D-glucuronoside
show the reaction diagram
-
-
-
-
?
additional information
?
-
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-glucuronate + a flavonol
UDP + a flavonol 3-O-beta-D-glucuronoside
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
UDP-sugar-dependent glycosyltransferases use a catalytic mechanism that inverts the anomeric configuration of a transferred sugar
-
-
-
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
?
-
x * 49700, SDS-PAGE
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
purified recombinant His-tagged enzyme, sitting-drop vapour-diffusion method, mixing of 0.001 ml of 0.7 mg/ml protein in 20 mM Tris–HCl, pH 8.0, 150 mM NaCl, 1 mM dithiothreitol, with 0.001 ml of reservoir solution containing 0.1 M MES–NaOH, pH 6.3, 14% w/v PEG 4000, 1 M NaCl, 0.2 M MgCl2, 5mM UDP-glucose, and equilibration against 0.06 ml reservoir solution, 2 days, 20°C, soaking of crystals in 0.1 M MES-NaOH, pH 6.3, 17% w/v PEG 4000, 1 M NaCl, 0.2 M MgCl2, 20mM UDP-glucose, 2 mM quercetin, 20% ethylene glycol, X-ray diffraction structure determination and analysis at 2.2 A resolution
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme to homogeneity from Escherichia coli strain BL21 Star (DE3) by nickel affinity chromatography, ultrafiltration, and gel filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His-tagged enzyme in Escherichia coli strain BL21 Star (DE3)
-