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 | 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 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 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 | 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 | UniProt | Comment | Textmining |
---|---|---|---|
Bellis perennis | Q5NTH0 | - |
- |
Purification (Comment) | Organism |
---|---|
- |
Bellis perennis |
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 Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
---|---|---|---|
0.0288 | - |
- |
Bellis perennis |
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 | Comment | Organism |
---|---|---|
monomer | 1 * 49000, SDS-PAGE | Bellis perennis |
monomer | 1 * 49645, calculated from sequence | Bellis perennis |
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 Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | - |
- |
Bellis perennis |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
35 | - |
stable up to | Bellis perennis |
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 Minimum | pH Optimum Maximum | Comment | Organism |
---|---|---|---|
8 | - |
at 30°C | Bellis perennis |
pH Minimum | pH Maximum | Comment | Organism |
---|---|---|---|
6.5 | 8.5 | active over pH-range 6.5-8.5 | Bellis perennis |
pH Stability | pH Stability Maximum | Comment | Organism |
---|---|---|---|
7.5 | - |
20°C, native enzyme is stable for 17 h | Bellis perennis |
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 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 |