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Enzyme Nomenclature
Information on EC 3.2.1.167 - baicalin-beta-D-glucuronidase
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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
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EC NUMBER 
COMMENTARY 
3.2.1.167
-
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RECOMMENDED NAME
GeneOntology No.
baicalin-beta-D-glucuronidase
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
baicalin + H2O = baicalein + D-glucuronate
-
-
-
-
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PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
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SYSTEMATIC NAME
IUBMB Comments
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
protein sequence homology shows no significant similarity to the family 2 beta-glucuronidases
SwissProt
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
evolution
-
the enzyme belongs to the glycoside hydrolase family 30, GH30, subfamily 3
evolution
-
the enzyme belongs to the glycoside hydrolase family 30, GH30, subfamily 3
-
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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
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
-
-
-
?
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
wogonoside + H2O
wogonin + ?
0.125 mM of wogonoside is completely transformed into wogonin within 3 h at 37°C, pH 5.0
-
-
?
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
-
-
?
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
-
-
?
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
-
-
?
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
-
the enzyme prefers baicalin rather than estrone 3-(beta-D-glucuronide), one of the human endogenous steroid hormones
-
-
?
baicalin + H2O
baicalein + D-glucuronate
-
the enzyme is strictly glycon-specific but not aglycon-specific
-
-
?
baicalin + H2O
baicalein + D-glucuronate
-
the enzyme prefers baicalin rather than estrone 3-(beta-D-glucuronide), one of the human endogenous steroid hormones
-
-
?
baicalin + H2O
baicalein + D-glucuronate
-
the enzyme is strictly glycon-specific but not aglycon-specific
-
-
?
estrone 3-(beta-D-glucuronide) + H2O
estrone + D-glucuronate
-
-
-
-
?
additional information
?
-
-
substrate specificity, the enzyme is inactive with other 4-nitrophenyl glycosides, overview
-
-
-
additional information
?
-
-
substrate specificity, the enzyme is inactive with other 4-nitrophenyl glycosides, overview
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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
-
-
-
additional information
?
-
-
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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NATURAL SUBSTRATES
NATURAL PRODUCTS
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
baicalin + H2O
baicalein + D-glucuronate
-
the enzyme prefers baicalin rather than estrone 3-(beta-D-glucuronide), one of the human endogenous steroid hormones
-
-
?
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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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
Ca2+ and Zn2+ have no significant effect on enzyme activity
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INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
additional information
-
2-mercaptoethanol has no influence on activity up to 10 mM
-
Ca2+
-
the free enzyme activity decreases rapidly and is even totally lost when the Ca2+ concentration is higher than 5 mM
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
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
0.0103
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
0.19
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
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
31.8
4-nitrophenyl beta-D-glucuronide
-
recombinant His-tagged 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
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2.58
estrone 3-(beta-D-glucuronide)
-
recombinant His-tagged enzyme, pH 5.0, 37°C
204
4-nitrophenyl beta-D-glucuronide
-
recombinant His-tagged 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
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
1.284
at 37°C and pH 5.0, using 4-nitrophenyl-beta-D-glucuronide as substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7
-
for GUS free or encapsulated in biomimetic alginate/protamine/silica capsules
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7
-
pH 3.0: about 50% of maximal activity, pH 7.0: about 65% of maximal activity
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
28
37
60
60
-
for GUS free or encapsulated in biomimetic alginate/protamine/silica capsules
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
40 - 70
-
40°C: about 60% of maximal activity, 70°C: about 50% of maximal activity
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4 - 8
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
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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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
30 - 70
50 - 60
the purified enzyme exhibits a half-life of 1 h at 60°C and more than 2 h at 50°C
70
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)
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
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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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-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, 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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Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
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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ENGINEERING
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
synthesis
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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LINKS TO OTHER DATABASES (specific for EC-Number 3.2.1.167)
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