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Literature summary for 2.4.1.254 extracted from

  • 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 (2005), J. Biol. Chem., 280, 899-906.
    View publication on PubMed

Cloned(Commentary)

Cloned (Comment) Organism
BpUGAT cDNA is expressed under the control of the GAL1 promoter in the Saccharomyces cerevisiae YPH499 cells as a soluble, catalytically active protein Bellis perennis

Inhibitors

Inhibitors Comment Organism Structure
Ca2+ 0.1 mM, 43% inhibition Bellis perennis
Cd2+ 0.1 mM, 51% inhibition Bellis perennis
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 Bellis perennis
Fe2+ 0.1 mM, 64% inhibition Bellis perennis
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 Bellis perennis
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 Bellis perennis
NEM 5 mM, pH 7.0, 20°C, 20 min, complete inactivation Bellis perennis
UDP 1 mM, complete inhibition Bellis perennis
UMP 1 mM, 64% inhibition Bellis perennis
UTP 1 mM, 91% inhibition Bellis perennis

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
0.019
-
cyanidin-3-O-(6-O-malonyl-beta-D-glucoside) pH 7.0, native enzyme Bellis perennis
0.032
-
cyanidin-3-O-(6-O-malonyl-beta-D-glucoside) pH 7.0, recombinant enzyme Bellis perennis
0.085
-
cyanidin 3-O-beta-D-glucoside pH 7.0, cosubstrate: UDP-D-glucuronate, native enzyme Bellis perennis
0.211
-
cyanidin 3-O-beta-D-glucoside pH 7.0, cosubstrate: UDP-D-glucuronate, recombinant enzyme Bellis perennis
0.476
-
UDP-D-glucuronate pH 7.0, native enzyme Bellis perennis
0.497
-
UDP-D-glucuronate pH 7.0, recombinant enzyme Bellis perennis

Molecular Weight [Da]

Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
49000
-
1 * 49000, SDS-PAGE Bellis perennis
49645
-
1 * 49645, calculated from sequence Bellis perennis
54000
-
gel filtration Bellis perennis

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
UDP-D-glucuronate + cyanidin 3-O-beta-D-glucoside Bellis perennis 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 + cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
-
?
UDP-D-glucuronate + cyanidin-3-O-(6-O-malonyl-beta-D-glucoside) 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 UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl-6-O-malonyl-beta-D-glucoside)
-
?

Organism

Organism UniProt Comment Textmining
Bellis perennis Q5NTH0
-
-

Purification (Commentary)

Purification (Comment) Organism
-
Bellis perennis

Source Tissue

Source Tissue Comment Organism Textmining
flower open red flowers, transcripts of BpUGAT can be specifically detected in red petals Bellis perennis
-
petal transcripts of BpUGAT can be specifically detected in red petals, consistent with the role of the enzyme in pigment biosynthesis Bellis perennis
-

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.0288
-
-
Bellis perennis

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
UDP-D-glucuronate + cyanidin 3-O-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 Bellis perennis UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
-
?
UDP-D-glucuronate + cyanidin 3-O-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 Bellis perennis UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl)-beta-D-glucoside
-
?
UDP-D-glucuronate + cyanidin-3-O-(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 Bellis perennis UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl-6-O-malonyl-beta-D-glucoside)
-
?
UDP-D-glucuronate + cyanidin-3-O-(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 Bellis perennis UDP + cyanidin 3-O-(2-O-beta-D-glucuronosyl-6-O-malonyl-beta-D-glucoside)
-
?

Subunits

Subunits Comment Organism
monomer 1 * 49000, SDS-PAGE Bellis perennis
monomer 1 * 49645, calculated from sequence Bellis perennis

Synonyms

Synonyms Comment Organism
BpUGAT
-
Bellis perennis
UDP-glucuronic acid:anthocyanidin 3-glucoside 2'-O-beta-glucuronosyltransferase
-
Bellis perennis
UDP-glucuronic acid:anthocyanin glucuronosyltransferase
-
Bellis perennis

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
35
-
-
Bellis perennis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
35
-
stable up to Bellis perennis

Turnover Number [1/s]

Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
34
-
UDP-D-glucuronate pH 7.0, cosubstrate: cyanidin-3-O-(6'-O-malonyl-beta-D-glucoside), native enzyme Bellis perennis
35
-
UDP-D-glucuronate pH 7.0, cosubstrate: cyanidin-3-O-(6'-O-malonyl-beta-D-glucoside), recombinant enzyme Bellis perennis

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
8
-
at 30°C Bellis perennis

pH Range

pH Minimum pH Maximum Comment Organism
6.5 8.5 active over pH-range 6.5-8.5 Bellis perennis

pH Stability

pH Stability pH Stability Maximum Comment Organism
7.5
-
20°C, native enzyme is stable for 17 h Bellis perennis

General Information

General Information Comment Organism
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 Bellis perennis

kcat/KM [mM/s]

kcat/KM Value [1/mMs-1] kcat/KM Value Maximum [1/mMs-1] Substrate Comment Organism Structure
4.5
-
cyanidin-3-O-(6-O-malonyl-beta-D-glucoside) pH 7.0, native enzyme Bellis perennis
6.6
-
cyanidin-3-O-(6-O-malonyl-beta-D-glucoside) pH 7.0, recombinant enzyme Bellis perennis
70.4
-
UDP-D-glucuronate pH 7.0, recombinant enzyme Bellis perennis
71.4
-
UDP-D-glucuronate pH 7.0, native enzyme Bellis perennis