Literature summary extracted from
Shao, H.; He, X.; Achnine, L.; Blount, J.W.; Dixon, R.A.; Wang, X.
Crystal structures of a multifunctional triterpene/flavonoid glycosyltransferase from Medicago truncatula (2005), Plant Cell, 17, 3141-3154.
Cloned(Commentary)
EC Number |
Cloned (Comment) |
Organism |
---|
2.4.1.91 |
expression of His-tagged wild-type and mutant enzymes in Escherichia coli strain BL21(DE3), selenomethionine-labeled enzyme in Escherichia coli strain B834(DE3) |
Medicago truncatula |
Crystallization (Commentary)
EC Number |
Crystallization (Comment) |
Organism |
---|
2.4.1.91 |
wild-type and selenomethionine-labeled enzyme in complex with UDP and UDP-glucose, hanging drop vapour diffusion method, 5 mg/ml protein is mixed with 5 mM UDP-galactose and 5 mM quercetin at a 2:1 v/v ratio, mixed with an equal volume of reservoir solution containing 40% w/v PEG 3350, 0.2 M ammonium acetate, and 0.1 M sodium citrate, pH 5.6, equilibration over the reservoir solution at 20°C, 2-5 days, X-ray diffraction structure determination and analysis at 2.0-2.6 A resolution, molecular docking |
Medicago truncatula |
Protein Variants
EC Number |
Protein Variants |
Comment |
Organism |
---|
2.4.1.91 |
D121A |
site-directed mutagenesis, inactive mutant |
Medicago truncatula |
2.4.1.91 |
D121N |
site-directed mutagenesis, inactive mutant |
Medicago truncatula |
2.4.1.91 |
E381A |
site-directed mutagenesis, inactive mutant |
Medicago truncatula |
2.4.1.91 |
H22A |
site-directed mutagenesis, inactive mutant |
Medicago truncatula |
Natural Substrates/ Products (Substrates)
EC Number |
Natural Substrates |
Organism |
Comment (Nat. Sub.) |
Natural Products |
Comment (Nat. Pro.) |
Rev. |
Reac. |
---|
2.4.1.91 |
UDP-alpha-D-glucose + quercetin |
Medicago truncatula |
- |
UDP + quercetin 3-O-beta-D-glucoside |
- |
? |
|
Organism
EC Number |
Organism |
UniProt |
Comment |
Textmining |
---|
2.4.1.91 |
Medicago truncatula |
Q5IFH7 |
- |
- |
Purification (Commentary)
EC Number |
Purification (Comment) |
Organism |
---|
2.4.1.91 |
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli strain BL21(DE3) by nickel affinity chromatography, anion exchange chromatography, and gel filtration |
Medicago truncatula |
Reaction
EC Number |
Reaction |
Comment |
Organism |
Reaction ID |
---|
2.4.1.91 |
UDP-glucose + a flavonol = UDP + a flavonol 3-O-beta-D-glucoside |
His22 acts as the catalytic base, and Asp121 is a key residue that may assist deprotonation of the acceptor by forming an electron transfer chain with the catalytic base, both residues, as well as Glu381, are essential in donor substrate binding and enzyme activity, acceptor substrate binding site structure |
Medicago truncatula |
|
Substrates and Products (Substrate)
EC Number |
Substrates |
Comment Substrates |
Organism |
Products |
Comment (Products) |
Rev. |
Reac. |
---|
2.4.1.91 |
UDP-alpha-D-glucose + quercetin |
- |
Medicago truncatula |
UDP + quercetin 3-O-beta-D-glucoside |
- |
? |
|
Subunits
EC Number |
Subunits |
Comment |
Organism |
---|
2.4.1.91 |
More |
the structure of UGT71G1 consists of two N- and C-terminal domains with similar Rossmann-type folds and belongs to the GT-B fold, the N-terminal domain contains a central seven-stranded parallel beta sheets flanked by eight alpha helices on both sides and a small two stranded beta sheets, the C-terminal domain contains a six stranded beta sheet flanked by eight alpha helices, the two domains pack very tightly and form a deep cleft with a UDP molecule bound, structure comparisons, overview |
Medicago truncatula |
Synonyms
EC Number |
Synonyms |
Comment |
Organism |
---|
2.4.1.91 |
More |
the enzyme belongs to the UGT superfamily |
Medicago truncatula |
2.4.1.91 |
UDP flavonoid/triterpene GT |
- |
Medicago truncatula |
2.4.1.91 |
UGT71G1 |
- |
Medicago truncatula |