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Information on EC 3.2.1.167 - baicalin-beta-D-glucuronidase
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3.2.1.167 baicalin-beta-D-glucuronidaseIUBMB Comments
The enzyme also hydrolyses wogonin 7-O-beta-D-glucuronide and oroxylin 7-O-beta-D-glucuronide with lower efficiency . Neglegible activity with p-nitrophenyl-beta-D-glucuronide .
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Word Map
- 3.2.1.167
-
3.2.1.31
- beta-glucuronidase
- lysosomal
- beta-d-glucuronide
-
glucuronosohydrolase
- mucopolysaccharidosis
-
3.1.6.1
- synthesis
- alpha-l-fucosidase
-
preputial
The expected taxonomic range for this enzyme is: Bacteria, Eukaryota
Synonyms
baicalin-beta-D-glucuronidase, baicalinase, beta-glucuronidase, EC 3.2.1.31, GUS, HP-GUS, LcGUS30, sGUS, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
baicalin-beta-D-glucuronidase
baicalinase
beta-glucuronidase
GUS
LcGUS30
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
baicalin + H2O = baicalein + D-glucuronate
-
-
-
-
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PATHWAY SOURCE
PATHWAYS
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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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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-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferol + D-glucuronate
-
-
-
?
4-phenolphthaleinyl beta-D-glucuronide + H2O
4-phenolphthalein + 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-glucuronate + H2O
5,6,7-trihydroxyflavone + D-glucuronate
5,7-dihydroxy-6-methoxyflavone-7-O-beta-D-glucuronate + H2O
5,7-dihydroxy-6-methoxyflavone + D-glucuronate
5,7-dihydroxy-8-methoxyflavone-7-O-beta-D-glucuronate + 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 + beta-D-glucuronic acid
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
-
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronate
-
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronate
Levilactobacillus brevis FERM BP-4693
-
-
-
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucuronate + H2O
5,6,7-trihydroxyflavone + D-glucuronate
-
i.e. baicalin
i.e. baicalein
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucuronate + H2O
5,6,7-trihydroxyflavone + 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-glucuronate + H2O
5,6,7-trihydroxyflavone + D-glucuronate
-
i.e. baicalin
i.e. baicalein
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucuronate + H2O
5,6,7-trihydroxyflavone + D-glucuronate
-
i.e. baicalin
i.e. baicalein
-
?
5,6,7-trihydroxyflavone-7-O-beta-D-glucuronate + H2O
5,6,7-trihydroxyflavone + 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-glucuronate + H2O
5,6,7-trihydroxyflavone + 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-6-methoxyflavone-7-O-beta-D-glucuronate + 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-6-methoxyflavone-7-O-beta-D-glucuronate + 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-glucuronate + 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-glucuronate + 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-glucuronate + 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-glucuronate + 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-glucuronate + H2O
5,7-dihydroxy-8-methoxyflavone + D-glucuronate
-
i.e. wogonin 7-O-beta-D-glucuronide
-
-
?
baicalin + H2O
baicalein + beta-D-glucuronic acid
-
best substrate
-
-
?
baicalin + H2O
baicalein + D-glucuronate
-
baicalein 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
Levilactobacillus brevis FERM BP-4693
-
the enzyme prefers baicalin rather than estrone 3-(beta-D-glucuronide), one of the human endogenous steroid hormones
-
-
?
baicalin + H2O
baicalein + D-glucuronate
Levilactobacillus brevis FERM BP-4693
-
the enzyme is strictly glycon-specific but not aglycon-specific
-
-
?
estrone 3-(beta-D-glucuronide) + H2O
estrone + D-glucuronate
-
-
-
-
?
estrone 3-(beta-D-glucuronide) + H2O
estrone + D-glucuronate
Levilactobacillus brevis FERM BP-4693
-
-
-
-
?
additional information
?
-
-
development of a chemically defined medium-based baicalein bioproduction process with a comparable yield compared to complex medium-based ones, detailed overview
-
-
?
additional information
?
-
-
substrate specificity, the enzyme is inactive with other 4-nitrophenyl glycosides, overview
-
-
?
additional information
?
-
Levilactobacillus brevis FERM BP-4693
-
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
?
-
domination of the glucuronide wogonoside is a characteristic feature of the hairy roots culture, while glucuronide baicalin is predominant in intact plant roots and also in the hairy roots. Alteration in contents of the main flavones in hairy roots culture of the Baikal skullcap during culturing, overview
-
-
?
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
?
-
-
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
?
-
-
no activity with 4-nitrophenyl beta-D-glucoside
-
-
?
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NATURAL SUBSTRATE
NATURAL 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
additional information
?
-
domination of the glucuronide wogonoside is a characteristic feature of the hairy roots culture, while glucuronide baicalin is predominant in intact plant roots and also in the hairy roots. Alteration in contents of the main flavones in hairy roots culture of the Baikal skullcap during culturing, overview
-
-
?
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
Levilactobacillus brevis FERM BP-4693
-
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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INHIBITOR
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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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
Alteration in glycosidases from well-differentiated colorectal adenocarcinoma of rat.
Carcinoma, Hepatocellular
Serum and host liver activities of glycosidases and sialyltransferases in animals bearing transplantable tumors.
Hydatidiform Mole
Studies of beta-glucuronidase in first-trimester placenta, term placenta and hydatidiform mole.
Hypertension
A lack of coordination in the release of urinary lysosomal and brush border enzymes following renovascular surgery.
Liver Cirrhosis
Changes in the catalytic activities of proteoglycan-degrading lysosomal enzymes in parenchymal and non-parenchymal liver cells and in serum during the development of experimental liver fibrosis.
Mastitis
Optimizing the fluorometric ?-glucuronidase assay in ruminant milk for a more precise determination of mastitis.
Mucopolysaccharidoses
Large scale analysis of the mutational landscape in ?-glucuronidase: A major player of mucopolysaccharidosis type VII.
Mucopolysaccharidosis VII
Correction of murine mucopolysaccharidosis VII by a human beta-glucuronidase transgene.
Mucopolysaccharidosis VII
Large scale analysis of the mutational landscape in ?-glucuronidase: A major player of mucopolysaccharidosis type VII.
Mucopolysaccharidosis VII
Mutations and polymorphisms in GUSB gene in mucopolysaccharidosis VII (Sly Syndrome).
Silicosis
Serum beta-N-acetylglucosaminidase and beta-glucuronidase activities in silicosis patients and in workers exposed to silica dust.
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0391
5,7-dihydroxy-6-methoxyflavone-7-O-beta-D-glucuronate
-
pH 6.5, 28°C
0.0307
5,7-dihydroxy-8-methoxyflavone-7-O-beta-D-glucuronate
-
pH 6.5, 28°C
0.154
4-nitrophenyl beta-D-glucuronide
-
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
0.0103
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
4.5
7
-
for GUS free or encapsulated in biomimetic alginate/protamine/silica capsules
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 7
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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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
protein sequence homology shows no significant similarity to the family 2 beta-glucuronidases
SwissProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
relationship between contents of principal flavones in hairy roots of Scutellaria baicalensis with the activity of the beta-glucuronidase (sGUS) enzyme during a culturing cycle, overview. The highest contents of aglycones, baicalin and wogonin is observed at the growth days 8, 14, and 71 and reach 45, 41, and 62% (based on the total weight of hairy roots of the Baikal skullcap), correspondingly. Their accumulation is accompanied by increase of the sGUS activity. The enzyme activity is characterized by significant and reasonable correlation only with the wogonin contents
brenda
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
metabolism
the central precursor metabolite of wogonin and baicalein and their glycosylated forms is chrysin
physiological function
evolution
-
the enzyme belongs to the glycoside hydrolase family 30, GH30, subfamily 3
evolution
Levilactobacillus brevis FERM BP-4693
-
the enzyme belongs to the glycoside hydrolase family 30, GH30, subfamily 3
physiological function
relationship between contents of principal flavones in hairy roots of Scutellaria baicalensis with the activity of the beta-glucuronidase (sGUS) enzyme during a culturing cycle. The enzyme activity is characterized by significant and reasonable correlation only with the wogonin contents. The endogenous beta-glucuronidase (sGUS), that catalyzes the cleavage of the glucuronic acid residue from the glycosylated forms of phenolic compounds
physiological function
the beta-glucuronidase enzyme is involved in the formation of the more active aglycone flavones in the mdicinal plant. The enzyme activity is characterized by significant correlation only with the wogonin contents, whereas the correlation for the baicalin is insignificant
physiological function
-
the protective effect of baicalin (the main active compound in Scutellariae radix (Huangqin)) against aminoacetophen (APAP or paracetamol)-induced hepatotoxicity is not altered through enzyme inhibition by D-saccharic acid 1.4-lactone. SAL, a beta-glucuronidase inhibitor, strongly decreased the intestinal beta-glucuronidase activity in mice, but the baicalin-provided protection against APAP-induced cytotoxicity in L-02 cells is not altered after the application of SAL, thus protection of baicalin against APAP-induced hepatotoxicity does not require the conversion into its aglycone baicalein
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). BAGLU_SCUBA
527
0
58772
Swiss-Prot
Secretory Pathway (Reliability: 1)
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
homotetramer
tetramer
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PROTEIN VARIANTS
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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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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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimethyl formamide
-
enzyme HP-GUS retains its catalytic activity in presence of 5% DMF, which is required in the biotransformation assay due to a low solubility and insolubility problem of baicalin and baicalein at reaction pH 4.5, respectively
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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
native enzyme 7.2fold from roots, by ammonium sulfate fractionation and anion exchange chromatography to homogeneity
-
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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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
increase in the glucuronidase activity due to mechanical stress (e.g. dissecting roots)
increase in the glucuronidase activity during the first weeks of cultivation followed by mechanical stress (e.g. dissecting roots)
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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
-
the enzyme can be used for biotransformation of glycone baicalin to more pharmacologically active aglycone baicalein in extracts from Scutellaria baicalensis Georgi plant roots. Development of a chemically defined medium-based baicalein bioproduction process with a comparable yield compared to complex medium-based ones, overview
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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REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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-b-D-glucuronidase hydrolyzing baicalin to baicalein from fresh roots of Scutellaria viscidula Bge
Process Biochem.
40
1911-1915
2005
Scutellaria viscidula
-
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
Levilactobacillus 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
Levilactobacillus brevis, Levilactobacillus brevis FERM BP-4693
brenda
Shi, L.; Hao, Z.; Zhang, S.; Wei, M.; Lu, B.; Wang, Z.; Ji, L.
Baicalein and baicalin alleviate acetaminophen-induced liver injury by activating Nrf2 antioxidative pathway The involvement of ERK1/2 and PKC
Biochem. Pharmacol.
150
9-23
2018
Mus musculus
brenda
Muderrisoglu, C.; Yesil-Celiktas, O.
High-yield biocatalysis of baicalein 7-O-beta-D-glucuronide to baicalein using soluble Helix pomatia-derived beta-glucuronidase in a chemically defined acidic Medium
Catal. Lett.
149
1701-1709
2019
Helix pomatia
-
brenda
Dikaya, V.S.; Solovyeva, A.I.; Sidorov, R.A.; Solovyev, P.A.; Stepanova, A.Y.
The relationship between endogenous beta-glucuronidase activity and biologically active flavones-aglycone contents in hairy roots of Baikal skullcap
Chem. Biodivers.
15
e1700409
2018
Scutellaria baicalensis (Q9LRC8)
brenda
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