Literature summary for 2.4.1.91 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)

Cloned (Comment)	Organism
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)

Crystallization (Comment)	Organism
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

Crystallization (Comment)

Organism

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

Protein Variants	Comment	Organism
D121A	site-directed mutagenesis, inactive mutant	Medicago truncatula
D121N	site-directed mutagenesis, inactive mutant	Medicago truncatula
E381A	site-directed mutagenesis, inactive mutant	Medicago truncatula
H22A	site-directed mutagenesis, inactive mutant	Medicago truncatula

Natural Substrates/ Products (Substrates)

Natural Substrates	Organism	Comment (Nat. Sub.)	Natural Products	Comment (Nat. Pro.)	Rev.	Reac.
UDP-alpha-D-glucose + quercetin	Medicago truncatula	-	UDP + quercetin 3-O-beta-D-glucoside	-	?

Organism

Organism	UniProt	Comment	Textmining
Medicago truncatula	Q5IFH7	-	-

Purification (Commentary)

Purification (Comment)	Organism
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

Reaction	Comment	Organism	Reaction ID
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	a

Substrates and Products (Substrate)

Substrates	Comment Substrates	Organism	Products	Comment (Products)	Rev.	Reac.
UDP-alpha-D-glucose + quercetin	-	Medicago truncatula	UDP + quercetin 3-O-beta-D-glucoside	-	?

Subunits

Subunits	Comment	Organism
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

Synonyms	Comment	Organism
More	the enzyme belongs to the UGT superfamily	Medicago truncatula
UDP flavonoid/triterpene GT	-	Medicago truncatula
UGT71G1	-	Medicago truncatula