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Information on EC 2.4.1.254 - cyanidin-3-O-glucoside 2''-O-glucuronosyltransferase and Organism(s) Bellis perennis and UniProt Accession Q5NTH0
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EC Tree
2.4.1.254 cyanidin-3-O-glucoside 2''-O-glucuronosyltransferaseIUBMB Comments
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 taxonomic range for the selected organisms is: Bellis perennis
The expected taxonomic range for this enzyme is: Bellis perennis
The expected taxonomic range for this enzyme is: Bellis perennis
Reaction Schemes
Synonyms
bpugat, bpugt94b1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
UDP-glucuronic acid:anthocyanidin 3-glucoside 2'-O-beta-glucuronosyltransferase
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PATHWAY SOURCE
PATHWAYS
SYSTEMATIC NAME
IUBMB Comments
UDP-D-glucuronate:cyanidin-3-O-beta-D-glucoside 2-O-beta-glucuronosyltransferase
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].
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-D-glucuronate + cyanidin 3-O-beta-D-glucoside
UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
UDP-D-glucuronate + cyanidin-3-O-(6-O-malonyl-beta-D-glucoside)
UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl-6-O-malonyl-beta-D-glucoside)
UDP-beta-D-glucuronate + cyanidin 3-O-beta-D-glucoside
UDP + cyanidin 3-O-beta-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
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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
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-
?
UDP-D-glucuronate + cyanidin 3-O-beta-D-glucoside
UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
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
-
-
?
UDP-D-glucuronate + cyanidin 3-O-beta-D-glucoside
UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
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
-
-
?
UDP-D-glucuronate + cyanidin-3-O-(6-O-malonyl-beta-D-glucoside)
UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl-6-O-malonyl-beta-D-glucoside)
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
-
-
?
UDP-D-glucuronate + cyanidin-3-O-(6-O-malonyl-beta-D-glucoside)
UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl-6-O-malonyl-beta-D-glucoside)
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
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-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
UDP-D-glucuronate + cyanidin 3-O-beta-D-glucoside
UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
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
-
-
?
UDP-D-glucuronate + cyanidin-3-O-(6-O-malonyl-beta-D-glucoside)
UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl-6-O-malonyl-beta-D-glucoside)
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
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-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Cu2+
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
Hg2+
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
additional information
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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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.085
cyanidin 3-O-beta-D-glucoside
pH 7.0, cosubstrate: UDP-D-glucuronate, native enzyme
0.211
cyanidin 3-O-beta-D-glucoside
pH 7.0, cosubstrate: UDP-D-glucuronate, recombinant enzyme
0.019
cyanidin-3-O-(6-O-malonyl-beta-D-glucoside)
pH 7.0, native enzyme
0.032
cyanidin-3-O-(6-O-malonyl-beta-D-glucoside)
pH 7.0, recombinant enzyme
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
relative kcat-values for wild-type enzyme and mutant enzymes
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34
UDP-D-glucuronate
pH 7.0, cosubstrate: cyanidin-3-O-(6'-O-malonyl-beta-D-glucoside), native enzyme
35
UDP-D-glucuronate
pH 7.0, cosubstrate: cyanidin-3-O-(6'-O-malonyl-beta-D-glucoside), recombinant enzyme
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
additional information
-
relative kcat/KM values for wild-type enzyme and mutant enzymes
-
6.6
cyanidin-3-O-(6-O-malonyl-beta-D-glucoside)
pH 7.0, recombinant enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
open red flowers, transcripts of BpUGAT can be specifically detected in red petals
transcripts of BpUGAT can be specifically detected in red petals, consistent with the role of the enzyme in pigment biosynthesis
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
role of the enzyme in the production of glucuronosylated anthocyanins that are the origin of the red coloration of flowers of Bellis perennis
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). UGAT_BELPE
438
0
49645
Swiss-Prot
Secretory Pathway (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
monomer
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D152A
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mutation decreases the activity with cyanidin 3-O-beta-D-glucoside to less than 15% of wild type
N123A
-
mutation decreases the activity with cyanidin 3-O-beta-D-glucoside to less than 15% of wild type
R25G
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mutant enzyme exhibits only 0.5% to 2.5% of wild-type activity with UDP-D-glucuronate, but shows a 3fold increase in activity with UDP-D-glucose
R25K
-
mutant enzyme exhibits only 0.5% to 2.5% of wild-type activity with UDP-D-glucuronate, but shows a 3fold increase in activity with UDP-D-glucose
R25S
-
mutant enzyme exhibits only 0.5% to 2.5% of wild-type activity with UDP-D-glucuronate, but shows a 3fold increase in activity with UDP-D-glucose
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sawada, S.; Suzuki, H.; Ichimaida, F.; Yamaguchi, M.A.; Iwashita, T.; Fukui, Y.; Hemmi, H.; Nishino, T.; Nakayama, T.
UDP-glucuronic acid:anthocyanin glucuronosyltransferase from red daisy (Bellis perennis) flowers. Enzymology and phylogenetics of a novel glucuronosyltransferase involved in flower pigment biosynthesis
J. Biol. Chem.
280
899-906
2005
Bellis perennis (Q5NTH0)
Osmani, S.A.; Bak, S.; Imberty, A.; Olsen, C.E.; Moller, B.L.
Catalytic key amino acids and UDP-sugar donor specificity of a plant glucuronosyltransferase, UGT94B1: molecular modeling substantiated by site-specific mutagenesis and biochemical analyses
Plant Physiol.
148
1295-1308
2008
Bellis perennis
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