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Information on EC 3.2.1.167 - baicalin-beta-D-glucuronidase for references in articles please use BRENDA:EC3.2.1.167Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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baicalin-beta-D-glucuronidase
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baicalin + H2O = baicalein + D-glucuronate
-
-
-
-
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baicalein degradation (hydrogen peroxide detoxification)
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-
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5,6,7-trihydroxyflavone-7-O-beta-D-glucupyranosiduronate glucuronosylhydrolase
The enzyme also hydrolyses wogonin 7-O-beta-D-glucuronide and oroxylin 7-O-beta-D-glucuronide with lower efficiency [4]. Neglegible activity with p-nitrophenyl-beta-D-glucuronide [2].
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baicalin-beta-D-glucuronidase
baicalin-beta-D-glucuronidase
-
-
baicalin-beta-D-glucuronidase
-
-
-
baicalinase
-
-
beta-glucuronidase
-
-
GUS
-
-
LcGUS30
-
-
sGUS
-
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-
-
brenda
subsp. coagulans
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-
brenda
Georg
-
-
brenda
Georgi
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-
brenda
Bge
-
-
brenda
Bge
-
-
brenda
strain RO1
UniProt
brenda
subsp. coagulans
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-
brenda
Georg
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-
brenda
Georgi
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-
brenda
protein sequence homology shows no significant similarity to the family 2 beta-glucuronidases
SwissProt
brenda
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evolution
-
the enzyme belongs to the glycoside hydrolase family 30, GH30, subfamily 3
evolution
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the enzyme belongs to the glycoside hydrolase family 30, GH30, subfamily 3
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4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronate
5,6,7-trihydroxyflavone-7-beta-D-glucuronide + H2O
5,6,7-trihydroxyflavone + D-glucuronate
-
-
-
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + H2O
5,6,7-trihydroxyflavone + D-glucuronate
-
i.e. baicalin
i.e. baicalein
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + H2O
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + D-glucuronate
5,7-dihydroxy-6-methoxyflavone-7-O-beta-D-glucoronate + H2O
5,7-dihydroxy-6-methoxyflavone + D-glucuronate
-
i.e. oroxylin 7-O-beta-D-glucuronide, i.e. 5-hydroxy-6-methoxy-4-oxo-2-phenyl-4H-chromen-7-yl beta-D-glucopyranosiduronic acid
-
-
?
5,7-dihydroxy-8-methoxyflavone-7-O-beta-D-glucoronate + H2O
5,7-dihydroxy-8-methoxyflavone + D-glucuronate
baicalin + H2O
baicalein + D-glucuronate
estrone 3-(beta-D-glucuronide) + H2O
estrone + D-glucuronate
wogonoside + H2O
?
-
-
-
-
?
wogonoside + H2O
wogonin + ?
0.125 mM of wogonoside is completely transformed into wogonin within 3 h at 37°C, pH 5.0
-
-
?
additional information
?
-
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronate
-
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronate
-
-
-
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + H2O
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + D-glucuronate
-
i.e. baicalin
i.e. baicalein
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + H2O
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + D-glucuronate
i.e. baicalin. The enzyme shows more than 20fold higher activity for baicalein 7-O-beta-D-glucuronide as compared with luteolin 3'-O-beta-D-glucuronide
i.e. baicalein
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + H2O
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + D-glucuronate
-
i.e. baicalin
i.e. baicalein
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + H2O
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + D-glucuronate
-
i.e. baicalin. The enzyme shows more than 20fold higher activity for baicalein 7-O-beta-D-glucuronide as compared with luteolin 3'-O-beta-D-glucuronide
i.e. baicalein
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + H2O
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + D-glucuronate
-
i.e. baicalin. No activity with p-nitrophenyl-beta-D-glucoside. Activity with p-nitrophenyl-beta-D-glucuronide is about 4% of the activity with 5,6-dihydroxy-4-oxo-2-phenyl-4H-chromen-7-yl beta-D-glucopyranosiduronic acid (baicalin), activity with p-phenolphthalein-beta-D-glucuronide is 9.5% of the activity with 5,6-dihydroxy-4-oxo-2-phenyl-4H-chromen-7-yl beta-D-glucopyranosiduronic acid (baicalin)
i.e. baicalein
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + H2O
5,6,7-trihydroxyflavone-7-O-beta-D-glucoronate + D-glucuronate
-
i.e. baicalin. No activity with p-nitrophenyl-beta-D-glucoside. Activity with p-nitrophenyl-beta-D-glucuronide is about 4% of the activity with 5,6-dihydroxy-4-oxo-2-phenyl-4H-chromen-7-yl beta-D-glucopyranosiduronic acid (baicalin), activity with p-phenolphthalein-beta-D-glucuronide is 9.5% of the activity with 5,6-dihydroxy-4-oxo-2-phenyl-4H-chromen-7-yl beta-D-glucopyranosiduronic acid (baicalin)
i.e. baicalein
-
?
5,7-dihydroxy-8-methoxyflavone-7-O-beta-D-glucoronate + H2O
5,7-dihydroxy-8-methoxyflavone + D-glucuronate
-
i.e. wogonin 7-O-beta-D-glucuronide, i.e. 5-hydroxy-8-methoxy-4-oxo-2-phenyl-4H-chromen-7-yl beta-D-glucopyranosiduronic acid
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-
?
5,7-dihydroxy-8-methoxyflavone-7-O-beta-D-glucoronate + H2O
5,7-dihydroxy-8-methoxyflavone + D-glucuronate
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i.e. wogonin 7-O-beta-D-glucuronide
-
-
?
5,7-dihydroxy-8-methoxyflavone-7-O-beta-D-glucoronate + H2O
5,7-dihydroxy-8-methoxyflavone + D-glucuronate
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i.e. wogonin 7-O-beta-D-glucuronide
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-
?
baicalin + H2O
baicalein + D-glucuronate
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-
-
-
?
baicalin + H2O
baicalein + D-glucuronate
0.15 mM of baicalin is completely transformed into baicalein within 3 h at 37°C, pH 5.0
-
-
?
baicalin + H2O
baicalein + D-glucuronate
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the enzyme prefers baicalin rather than estrone 3-(beta-D-glucuronide), one of the human endogenous steroid hormones
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-
?
baicalin + H2O
baicalein + D-glucuronate
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the enzyme is strictly glycon-specific but not aglycon-specific
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-
?
baicalin + H2O
baicalein + D-glucuronate
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the enzyme prefers baicalin rather than estrone 3-(beta-D-glucuronide), one of the human endogenous steroid hormones
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-
?
baicalin + H2O
baicalein + D-glucuronate
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the enzyme is strictly glycon-specific but not aglycon-specific
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-
?
estrone 3-(beta-D-glucuronide) + H2O
estrone + D-glucuronate
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-
-
?
estrone 3-(beta-D-glucuronide) + H2O
estrone + D-glucuronate
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-
-
?
additional information
?
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substrate specificity, the enzyme is inactive with other 4-nitrophenyl glycosides, overview
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additional information
?
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substrate specificity, the enzyme is inactive with other 4-nitrophenyl glycosides, overview
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additional information
?
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no activity with 5,6-dihydroxy-4-oxo-2-phenyl-4H-chromen-7-yl beta-D-glucoside, 4-nitrophenyl beta-D-glucuronide and luteolin 3'-O-beta-D-glucuronide
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additional information
?
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the enzyme is not able to cleave the bond between the two glucuronic acid moieties in glycyrrhizin (glycyrrhetic acid 3-O-D-diglucuronide), the enzyme is not capable of hydrolyzing glucosides, luteolin-7-glucoside and apigenin-7-O-glucoside
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additional information
?
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the enzyme is not able to cleave the bond between the two glucuronic acid moieties in glycyrrhizin (glycyrrhetic acid 3-O-D-diglucuronide), the enzyme is not capable of hydrolyzing glucosides, luteolin-7-glucoside and apigenin-7-O-glucoside
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-
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baicalin + H2O
baicalein + D-glucuronate
baicalin + H2O
baicalein + D-glucuronate
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the enzyme prefers baicalin rather than estrone 3-(beta-D-glucuronide), one of the human endogenous steroid hormones
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-
?
baicalin + H2O
baicalein + D-glucuronate
-
the enzyme prefers baicalin rather than estrone 3-(beta-D-glucuronide), one of the human endogenous steroid hormones
-
-
?
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additional information
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Ca2+ and Zn2+ have no significant effect on enzyme activity
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Ag+
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0.3 mM, 20-25% inhibition
D-glucose
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10 mM, 15% inhibition
D-glucuronate
-
10 mM, 15% inhibition
Fe3+
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10 mM: 50% inhibition
additional information
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2-mercaptoethanol has no influence on activity up to 10 mM
-
Ca2+
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the free enzyme activity decreases rapidly and is even totally lost when the Ca2+ concentration is higher than 5 mM
Ca2+
-
0.3 mM, about 15% inhibition
Cu2+
-
0.3 mM, 20-25% inhibition
Cu2+
-
10 mM: 14% inhibition
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Mg2+
-
50 mM, 1.2 fold activation
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0.154 - 0.156
4-nitrophenyl beta-D-glucuronide
0.0097 - 0.038
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
0.19 - 0.36
5,6,7-trihydroxyflavone-7-beta-D-glucuronide
0.0391
5,7-dihydroxy-6-methoxyflavone-7-O-beta-D-glucoronate
-
pH 6.5, 28°C
0.0307
5,7-dihydroxy-8-methoxyflavone-7-O-beta-D-glucoronate
-
pH 6.5, 28°C
2.02
wogonoside
-
recombinant His-tagged enzyme, pH 5.0, 37°C
0.154
4-nitrophenyl beta-D-glucuronide
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native enzyme, pH 5.0, 37°C
0.156
4-nitrophenyl beta-D-glucuronide
-
recombinant His-tagged enzyme, pH 5.0, 37°C
0.0097
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, mutant enzyme E329A
0.0098
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
-
pH 6.5, 28°C
0.0103
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, mutant enzyme E212A
0.0121
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, wild-type enzyme
0.027
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, mutant enzyme Y281A
0.038
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
-
-
0.19
5,6,7-trihydroxyflavone-7-beta-D-glucuronide
-
free enzyme, at pH 7.0 and 37°C
0.36
5,6,7-trihydroxyflavone-7-beta-D-glucuronide
-
calcium alginate-encapsulated enzyme, at pH 7.0 and 37°C
1.5 - 2
Baicalin
-
native enzyme, pH 5.0, 37°C
1.74
Baicalin
-
recombinant His-tagged enzyme, pH 5.0, 37°C
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31.8 - 53.7
4-nitrophenyl beta-D-glucuronide
0.011 - 639
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
6.37
wogonoside
-
recombinant His-tagged enzyme, pH 5.0, 37°C
31.8
4-nitrophenyl beta-D-glucuronide
-
recombinant His-tagged enzyme, pH 5.0, 37°C
53.7
4-nitrophenyl beta-D-glucuronide
-
native enzyme, pH 5.0, 37°C
0.011
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, mutant enzyme E329A
0.135
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, mutant enzyme E212A
0.77
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, mutant enzyme Y281A
639
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, wild-type enzyme
18.5
Baicalin
-
recombinant His-tagged enzyme, pH 5.0, 37°C
21.3
Baicalin
-
native enzyme, pH 5.0, 37°C
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204 - 348
4-nitrophenyl beta-D-glucuronide
4.2 - 52810
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
2.58
estrone 3-(beta-D-glucuronide)
-
recombinant His-tagged enzyme, pH 5.0, 37°C
3.15
wogonoside
-
recombinant His-tagged enzyme, pH 5.0, 37°C
204
4-nitrophenyl beta-D-glucuronide
-
recombinant His-tagged enzyme, pH 5.0, 37°C
348
4-nitrophenyl beta-D-glucuronide
-
native enzyme, pH 5.0, 37°C
4.2
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, mutant enzyme E329A
13.1
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, mutant enzyme E212A
28.5
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, mutant enzyme Y281A
52810
5,6,7-trihydroxyflavone 7-O-beta-D-glucoronate
pH 6.5, 28°C, wild-type enzyme
10.6
Baicalin
-
recombinant His-tagged enzyme, pH 5.0, 37°C
14
Baicalin
-
native enzyme, pH 5.0, 37°C
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1.284
at 37°C and pH 5.0, using 4-nitrophenyl-beta-D-glucuronide as substrate
7.57
-
purified native enzyme, pH 5.0, 37°C, substrate baicalin
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4.7
-
in 50 mM Na-citrate buffer
5
-
7
-
for GUS free or encapsulated in biomimetic alginate/protamine/silica capsules
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3 - 7
-
pH 3.0: about 50% of maximal activity, pH 7.0: about 65% of maximal activity
3.5 - 7
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activity range, profile overview
4.5
-
activity completely disappeares below pH 4.5
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28
assay at
37
-
optimal temperature for the conversion of baicalin to baicalein
60
-
for GUS free or encapsulated in biomimetic alginate/protamine/silica capsules
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20 - 80
-
activity range, profile overview
40 - 70
-
40°C: about 60% of maximal activity, 70°C: about 50% of maximal activity
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4.8
-
isoelectric focusing
5.5
-
isoelectric focusing
5.52
calculated from sequence
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-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
-
brenda
-
-
brenda
-
-
-
brenda
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-
brenda
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55000
-
4 * 55000, SDS-PAGE
56027
x * 56027, calculated from sequence
58400
-
x * 58400, SDS-PAGE
60000
-
x * 60000, native enzyme, SDS-PAGE
71000
recombinant enzyme, SDS-PAGE
200000 - 220000
-
gel filtration
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?
-
x * 60000, native enzyme, SDS-PAGE
?
-
x * 60000, native enzyme, SDS-PAGE
-
?
x * 56027, calculated from sequence
?
-
x * 56027, calculated from sequence
-
?
-
x * 58400, SDS-PAGE
-
homotetramer
-
4 * 55000, SDS-PAGE
homotetramer
-
4 * 55000, SDS-PAGE
-
tetramer
-
4 * 55000, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
-
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3
-
purified enzyme, inactivation
731207
3.5 - 9
-
purified enzyme, stable at
731207
4
-
30 min, about 50% loss of activity
706477
5 - 8
at 37°C, the GUS remains stable for 80 min at pH values ranging from 5.0 to 8.0. Activity decreases quickly above pH 7.0
709499
5 - 5.5
-
30 min, stable
706477
6
-
30 min, about 35% loss of activity
706477
7
-
30 min, about 40% of maximal activity
706477
4 - 8
-
encapsulated enzyme retains more than 80% of activity after being incubated at pH 4.0-5.0, about 90% activity at pH 6.0, and 100% activity at pH 7.0-8.0. Free enzyme shows no activity at pH 4.0, about 30% activity at pH 6.0, about 80% activity at pH 6.0, 100% activity at pH 7.0, and about 75% activity at pH 8.0
709548
4 - 8
-
the free enzyme shows no activity at pH 4.0, about 85% relative activity at pH 5.5 and pH 6.5, 100% activity at pH 7.0, about 60% relative activity at pH 7.5, and no activity at pH 8.0 (at 37°C, reaction time 60 min)
712143
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20 - 60
-
purified enzyme, stable at
50 - 60
the purified enzyme exhibits a half-life of 1 h at 60°C and more than 2 h at 50°C
30 - 70
-
compared with the activity after being incubated at 30°C, 92% of activity retained after being incubated at 50°C for encapsulated GUS, whereas 57% of the free GUS activity retained after the same treatment. Encapsulated GUS retains about 20% activity at 60°C and is inactivated at 70°C, while free enzyme is already inactive at 60°C
30 - 70
-
the free enzyme shows about 45% relative activity at 30°C, about 65% relative activity at 40°C, about 80% relative activity at 50°C, 100% activity at 60°C, and about 75% relative activity at 70°C (at pH 7.0, reaction time 40 min)
70
-
purified enzyme, inactivation
70
-
30 min, pH 5.0, stable below
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no appreciable loss in activity is found during 10 repeated reaction cycles of GUS encapsulated in biomimetic alginate/protamine/silica capsules
-
the calcium alginate-encapsulated GUS retains up to 88% of its free-form activity with an encapsulation efficiency of 77%. Conversion of baicalin by free and calcium alginate-encapsulated GUS results in the baicalein productivities of 80% and 65%, respectively. The calcium alginate-encapsulated GUS shows no appreciable loss in activity after four repeated cycles, and 90% of its initial activity remains after 26-day storage at 4°C
-
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-20°C, 10 mM NaH2PO4/Na2HPO4 buffer, 1 mM mercaptoethanol, pH 7.0, 50% glycerol, 2 months, 10-20% loss of activity
-
4°C, 10 mM NaH2PO4/Na2HPO4 buffer, 1 mM mercaptoethanol, pH 7.0, 50% glycerol, 2 weeks, complete loss of activity
-
4°C, 30 mM Tris-HCl pH 7.0, 11 days, 26% loss of activity
-
4°C, 30 mM Tris-HCl pH 7.0, 5 days, 19% loss of activity
-
4°C, free enzyme in 30 mM Tris–HCl (pH 7.0), 11 days, about 25% loss of activity
-
4°C, free enzyme in 30 mM Tris–HCl (pH 7.0), 26 days, 96% loss of activity
-
4°C, free enzyme in 30 mM Tris–HCl (pH 7.0), 5 days, about 20% loss of activity
-
4°C, GUS encapsulated in biomimetic alginate/protamine/silica capsules in 30 mM Tris–HCl (pH 7.0), 11 days, no loss of activity
-
4°C, GUS encapsulated in biomimetic alginate/protamine/silica capsules in 30 mM Tris–HCl (pH 7.0), 26 days, 10% loss of activity
-
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Ni-NTA column chromatography
recombinant His-tagged enzyme from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography and dialysis, native enzyme 1800fold from cell-free extract by repeated anion exchange chromatography and gel filtration, followed by dialysis
-
-
-
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DNA and amino acid sequence determination and analysis, recombinant expression of His-tagged enzyme in Escherichia coli strain Rosetta 2 (DE3)
-
expressed in Escherichia coli strain GMS407 (beta-glucuronidase-deficient)
expression in Escherichia coli. Escherichia coli having pET28a/sGUS shows much higher beta-glucuronidase activity using baicalein 7-O-beta-D-glucuronide as a substrate than Escherichia coli carrying pET28a. The minor enzyme activity observed in the latter is considered to be due to endogenous beta-glucuronidase
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E194A
beta-glucuronidase activity of the mutant enzyme with baicalein 7-O-beta-D-glucuronide is 86% of wild-type activity
E212A
beta-glucuronidase activity of the mutant enzyme with baicalein 7-O-beta-D-glucuronide is 1.2% of wild-type activity
E225A
beta-glucuronidase activity of the mutant enzyme with baicalein 7-O-beta-D-glucuronide is 94% of wild-type activity
E272A
beta-glucuronidase activity of the mutant enzyme with baicalein 7-O-beta-D-glucuronide is 70% of wild-type activity
E329A
beta-glucuronidase activity of the mutant enzyme with baicalein 7-O-beta-D-glucuronide is 0.3% of wild-type activity
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synthesis
-
synthesis of baicalein (i.e. 5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one), a main active ingredient of Scutellaria sp. used in traditional Chinese medicine. It is difficult to obtain baicalein directly from skullaps because of its low content
synthesis
-
synthesis of baicalein (i.e. 5,6,7-trihydroxy-2-phenyl-4H-chromen-4-one), a main active ingredient of Scutellaria sp. used in traditional Chinese medicine. It is difficult to obtain baicalein directly from skullaps because of its low content
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BAGLU_SCUBA
527
58772
Swiss-Prot
D2DMF3_LACBR
603
69335
TrEMBL
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Ikegami, F.; Matsunae, K.; Hisamitsu, M.; Kurihara, T.; Yamamoto, T.; Murakoshi, I.
Purification and properties of a plant beta-D-glucuronidase from Scutellaria root
Biol. Pharm. Bull.
18
1531-1534
1995
Scutellaria baicalensis, Scutellaria baicalensis Georg
brenda
Sasaki, K.; Taura, F.; Shoyama, Y.; Morimoto, S.
Molecular characterization of a vovel beta-glucuronidase from Scutellaria baicalensis Georgi
J. Biol. Chem.
275
27466-27472
2000
Scutellaria baicalensis (Q9LRC8)
brenda
Morimoto, S.; Harioka, T.; Shoyama, Y.
Purification and characterization of flavone-specific beta-glucuronidase from callus cultures of Scutellaria baicalensis Georgi
Planta
195
535-540
1995
Scutellaria baicalensis, Scutellaria baicalensis Georgi
-
brenda
Zhang, C.; Zhang, Y.; Chen, J.; Liang, X.
Purification and characterization of baicalin-beta-D-glucuronidase hydrolyzing baicalin to baicalein from fresh roots of Scutellaria viscidula Bge
Proc. Biochem.
40
1911-1915
2005
Scutellaria viscidula, Scutellaria viscidula Bge
-
brenda
Kim, H.S.; Kim, J.Y.; Park, M.S.; Zheng, H.; Ji, G.E.
Cloning and expression of beta-glucuronidase from Lactobacillus brevis in E. coli and application in the bioconversion of baicalin and wogonoside
J. Microbiol. Biotechnol.
19
1650-1655
2009
Lactobacillus brevis (D2DMF3)
brenda
Zhang, Y.; Wu, H.; Li, L.; Li, J.; Jiang, Z.; Jiang, Y.; Chen, Y.
Enzymatic conversion of baicalin into baicalein by beta-glucuronidase encapsulated in biomimetic core-shell structured hybrid capsules
J. Mol. Catal. B
57
130-135
2009
Escherichia coli
-
brenda
Jiang, Z.; Zhang, Y.; Li, J.; Jiang, W.; Yang, D.; Wu, H.
Encapsulation of beta-glucuronidase in biomimetic alginate capsules for bioconversion of baicalin to baicalein
Ind. Eng. Chem. Res.
46
1883-1890
2007
Escherichia coli
-
brenda
Sakurama, H.; Kishino, S.; Uchibori, Y.; Yonejima, Y.; Ashida, H.; Kita, K.; Takahashi, S.; Ogawa, J.
beta-Glucuronidase from Lactobacillus brevis useful for baicalin hydrolysis belongs to glycoside hydrolase family 30
Appl. Microbiol. Biotechnol.
98
4021-4032
2014
Lactobacillus brevis, Lactobacillus brevis FERM BP-4693
brenda
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