The enzyme is highly specific for cyanidin 3-O-glucosides and UDP-alpha-D-glucuronate. Involved in the production of glucuronosylated anthocyanins that are the origin of the red coloration of flowers of Bellis perennis .
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The expected taxonomic range for this enzyme is: Bellis perennis
The enzyme is highly specific for cyanidin 3-O-glucosides and UDP-alpha-D-glucuronate. Involved in the production of glucuronosylated anthocyanins that are the origin of the red coloration of flowers of Bellis perennis [1].
highly specific with respect to the sugar donor UDP-GlcUA. Activity with other activated sugars such as UDP-Glc, UDP-Gal, and UDP-Xyl is very low. Wild-type enzyme activity toward delphinidin-3-O-glucoside is only 5% to 10% of the activity with cyanidin 3-O-beta-D-glucoside. A few specific amino acid residues as well as the overall size and shape of the acceptor pocket define substrate specificity
both cyanidin-3-O-6''-malonylglucoside and cyanidin 3-O-glucoside are good substrates, suggesting that these anthocyanins may serve as physiological glucuronosyl acceptors in the production of glucuronosylated anthocyanins that are the origin of the red coloration of flowers of Bellis perennis
50% of the activity with cyanidin-3-O-glucoside. The enzyme is highly specific for cyanidin 3-O-glucosides and UDP-D-glucuronate. The relative activities for UDP-D-glucose and UDP-D-galactose are less than 0.1% of the activity for UDP-D-glucuronate. The enzyme shows low activity with delphinidin 3-O-glucoside and is shows no or negligible activity towards pelargonidin 3-O-glucoside,cyanidin 3-O-3'',6''-O-dimalonylglucoside, pelargonidin 3,5-O-diglucoside, pelargonidin 3-O-6''-O-malonylglucoside-5-O-glucoside, quercetin 3-O-glucoside, quercetin 3-O-6''-O-malonylglucoside, daidzin, genistin, daidzin, genistin, 7-O-6''-O-malonylglucosides of daidzein and genistein, cyanidin, quercetin, daidzein, genistein, p-nitrophenyl beta-D-glucopyranoside
both cyanidin-3-O-(6'-O-malonyl-beta-D-glucoside) and cyanidin 3-O-glucoside are good substrates, suggesting that these anthocyanins may serve as physiological glucuronosyl acceptors in the production of glucuronosylated anthocyanins that are the origin of the red coloration of flowers of Bellis perennis
50% of the activity with cyanidin-3-O-glucoside. The enzyme is highly specific for cyanidin 3-O-glucosides and UDP-D-glucuronate. The relative activities for UDP-D-glucose and UDP-D-galactose are less than 0.1% of the activity for UDP-D-glucuronate. The enzyme shows low activity with delphinidin 3-O-glucoside and it shows no or negligible activity towards pelargonidin 3-O-glucoside,cyanidin 3-O-3'',6''-O-dimalonylglucoside, pelargonidin 3,5-O-diglucoside, pelargonidin 3-O-6''-O-malonylglucoside-5-O-glucoside, quercetin 3-O-glucoside, quercetin 3-O-6''-O-malonylglucoside, daidzin, genistin, daidzin, genistin, 7-O-6''-O-malonylglucosides of daidzein and genistein, cyanidin, quercetin, daidzein, genistein, p-nitrophenyl beta-D-glucopyranoside
both cyanidin-3-O-6''-malonylglucoside and cyanidin 3-O-glucoside are good substrates, suggesting that these anthocyanins may serve as physiological glucuronosyl acceptors in the production of glucuronosylated anthocyanins that are the origin of the red coloration of flowers of Bellis perennis
both cyanidin-3-O-(6'-O-malonyl-beta-D-glucoside) and cyanidin 3-O-glucoside are good substrates, suggesting that these anthocyanins may serve as physiological glucuronosyl acceptors in the production of glucuronosylated anthocyanins that are the origin of the red coloration of flowers of Bellis perennis
0.1 mM, complete inhibition. The observed enzyme inhibition by Cu2+ and Hg2+ may not solely be attributed to their effects on the enzyme itself because these heavy metal ions are known to destroy substrate anthocyanins
0.1 mM, complete inhibition. The observed enzyme inhibition by Cu2+ and Hg2+ may not solely be attributed to their effects on the enzyme itself because these heavy metal ions are known to destroy substrate anthocyanins
no inhibition by 1 mM uridine, 1 mM glucose or 1 mM sodium malonate. The enzyme retains full activity after incubation with 1 mM diethyl pyxrocarbonate at pH 7.0, 20°C for 20 min
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
BpUGAT cDNA is expressed under the control of the GAL1 promoter in the Saccharomyces cerevisiae YPH499 cells as a soluble, catalytically active protein
UDP-glucuronic acid:anthocyanin glucuronosyltransferase from red daisy (Bellis perennis) flowers. Enzymology and phylogenetics of a novel glucuronosyltransferase involved in flower pigment biosynthesis
Catalytic key amino acids and UDP-sugar donor specificity of a plant glucuronosyltransferase, UGT94B1: molecular modeling substantiated by site-specific mutagenesis and biochemical analyses