Information on EC 2.4.1.254 - cyanidin-3-O-glucoside 2''-O-glucuronosyltransferase

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The expected taxonomic range for this enzyme is: Bellis perennis

EC NUMBER
COMMENTARY hide
2.4.1.254
-
RECOMMENDED NAME
GeneOntology No.
cyanidin-3-O-glucoside 2''-O-glucuronosyltransferase
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
UDP-alpha-D-glucuronate + cyanidin 3-O-beta-D-glucoside = UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
show the reaction diagram
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-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
Anthocyanin biosynthesis
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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].
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
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
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
UDP-beta-D-glucuronate + cyanidin 3-O-beta-D-glucoside
UDP + cyanidin 3-O-beta-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
show the reaction diagram
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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
show the reaction diagram
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)
show the reaction diagram
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-D-glucuronate + cyanidin 3-O-beta-D-glucoside
UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
show the reaction diagram
Q5NTH0
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
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-
?
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)
show the reaction diagram
Q5NTH0
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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-
?
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
Ca2+
0.1 mM, 43% inhibition
Cd2+
0.1 mM, 51% inhibition
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
Fe2+
0.1 mM, 64% inhibition
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
NEM
5 mM, pH 7.0, 20°C, 20 min, complete inactivation
UDP
1 mM, complete inhibition
UMP
1 mM, 64% inhibition
UTP
1 mM, 91% inhibition
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 hide
LITERATURE
IMAGE
0.085 - 0.211
cyanidin 3-O-beta-D-glucoside
0.8
cyanidin 3-O-beta-glucoside
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pH 7.5, 30°C, wild-type enzyme
0.019 - 0.032
cyanidin-3-O-(6-O-malonyl-beta-D-glucoside)
1 - 7
UDP-beta-D-glucuronate
0.476 - 0.497
UDP-D-glucuronate
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
34 - 35
UDP-D-glucuronate
additional information
additional information
Bellis perennis
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relative kcat-values for wild-type enzyme and mutant enzymes
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.5 - 6.6
cyanidin-3-O-(6-O-malonyl-beta-D-glucoside)
40064
70.4 - 71.4
UDP-D-glucuronate
465
additional information
additional information
Bellis perennis
-
relative kcat/KM values for wild-type enzyme and mutant enzymes
2
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
-
assay at
pH RANGE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.5 - 8.5
active over pH-range 6.5-8.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
30
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assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
open red flowers, transcripts of BpUGAT can be specifically detected in red petals
Manually annotated by BRENDA team
transcripts of BpUGAT can be specifically detected in red petals, consistent with the role of the enzyme in pigment biosynthesis
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
49000
1 * 49000, SDS-PAGE
49645
1 * 49645, calculated from sequence
54000
gel filtration
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
monomer
1 * 49000, SDS-PAGE; 1 * 49645, calculated from sequence
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
7.5
20°C, native enzyme is stable for 17 h
704415
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
35
stable up to
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
expression in Escherichia coli
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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
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
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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
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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
R25S
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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