Information on EC 3.2.1.31 - beta-glucuronidase

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The expected taxonomic range for this enzyme is: Bacteria, Eukaryota, Archaea

EC NUMBER
COMMENTARY
3.2.1.31
-
RECOMMENDED NAME
GeneOntology No.
beta-glucuronidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
a beta-D-glucuronoside + H2O = D-glucuronate + an alcohol
show the reaction diagram
-
-
-
-
a beta-D-glucuronoside + H2O = D-glucuronate + an alcohol
show the reaction diagram
reaction mechanism, active site with catalytic nucleophile E576, residue E383 is also involved in catalysis
Q9X0F2
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
exoglycosidic
-
PATHWAY
KEGG Link
MetaCyc Link
beta-D-glucuronide and D-glucuronate degradation
-
luteolin triglucuronide degradation
-
Pentose and glucuronate interconversions
-
Starch and sucrose metabolism
-
Glycosaminoglycan degradation
-
Porphyrin and chlorophyll metabolism
-
Flavone and flavonol biosynthesis
-
Drug metabolism - other enzymes
-
Metabolic pathways
-
SYSTEMATIC NAME
IUBMB Comments
beta-D-glucuronoside glucuronosohydrolase
-
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
baicalin-beta-D-glucuronidase
-
-
baicalinase
Scutellaria baicalensis Georg
-
-
-
beta-D-glucuronidase
A7XS03
-
Beta-D-glucuronoside glucuronosohydrolase
-
-
-
-
Beta-G1
-
-
-
-
beta-Gluc
-
-
beta-glucuronidase
-
-
beta-glucuronidase
Agrobacterium sp. GV3101
-
-
-
beta-glucuronidase
-
fusion product with stachyose synthetase, EC 2.4.1.67
beta-glucuronidase
-
-
beta-glucuronidase
-
-
beta-glucuronidase A
-
-
BLG
-
-
exo-beta-D-glucuronidase
-
-
-
-
exo-beta-glucuronidase
-
-
GlcAase
Q7SFB0
-
glucuronidase, beta-glucuronide glucuronohydrolase
-
-
-
-
GUS
-
-
-
-
GUS
Lactobacillus brevis RO1
-
-
-
GUS
Lentinula edodes LD 106
-
-
-
GUS
Scutellaria baicalensis Georg
-
-
-
GUS
-
-
Gus2
-
isoform
GusA
Lactobacillus gasseri ADH, Lactobacillus gasseri ATCC33323
Q9AHJ8
-
-
GusA
Q9AFA2
isoform
GusA
Q9AFA2
isoform
-
GusB
Q97UI1
-
-
hGUSB
-
-
sGUS
Scutellaria baicalensis Georgi
Q9LRC8
-
-
UidA
P05804
isoform
ketodase
-
-
-
-
additional information
-
the enzyme belongs to glycosyl hydrolase family 2 with three conserved domains
additional information
Lactobacillus brevis RO1
-
the enzyme belongs to glycosyl hydrolase family 2 with three conserved domains
-
additional information
Q2PBR7
the enzyme belongs to the glycosyl hydrolases family 2
CAS REGISTRY NUMBER
COMMENTARY
9001-45-0
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain GV3101
-
-
Manually annotated by BRENDA team
Agrobacterium sp. GV3101
strain GV3101
-
-
Manually annotated by BRENDA team
ecotype Columbia
-
-
Manually annotated by BRENDA team
isoform Gus2
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
gene gusA
-
-
Manually annotated by BRENDA team
isoform UidA
UniProt
Manually annotated by BRENDA team
strain K12
-
-
Manually annotated by BRENDA team
Escherichia coli HGU-3
HGU-3
-
-
Manually annotated by BRENDA team
Escherichia coli K12
strain K12
-
-
Manually annotated by BRENDA team
snail
-
-
Manually annotated by BRENDA team
male adults
-
-
Manually annotated by BRENDA team
Indian major carp
-
-
Manually annotated by BRENDA team
Indian major carp, matured and healthy male fish
-
-
Manually annotated by BRENDA team
strain RO1
-
-
Manually annotated by BRENDA team
Lactobacillus brevis RO1
strain RO1
-
-
Manually annotated by BRENDA team
strain ADH
SwissProt
Manually annotated by BRENDA team
strain ATCC33323
SwissProt
Manually annotated by BRENDA team
strain ADH
SwissProt
Manually annotated by BRENDA team
Lactobacillus gasseri ATCC33323
strain ATCC33323
SwissProt
Manually annotated by BRENDA team
strain LD 106
-
-
Manually annotated by BRENDA team
Lentinula edodes LD 106
strain LD 106
-
-
Manually annotated by BRENDA team
cultivar Georgia
-
-
Manually annotated by BRENDA team
marine mollusc
-
-
Manually annotated by BRENDA team
distribution in
-
-
Manually annotated by BRENDA team
methods of enzyme determination
-
-
Manually annotated by BRENDA team
overview
-
-
Manually annotated by BRENDA team
adult male C57BL/6 mice
-
-
Manually annotated by BRENDA team
female BALB/c mice
-
-
Manually annotated by BRENDA team
no activity in Escherichia adecarboxylata
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia blattae
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia fergusonii
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia hermannii
-
-
-
Manually annotated by BRENDA team
no activity in Escherichia vulneris
-
-
-
Manually annotated by BRENDA team
2 different exo-beta-glucuronidases: a beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide and a beta-glucuronidase acting on chondroitin
-
-
Manually annotated by BRENDA team
cultivar Pusa Basmati
-
-
Manually annotated by BRENDA team
male Wistar rats
-
-
Manually annotated by BRENDA team
strain E1, isolated from human intestinal microflora, gene uidA
SwissProt
Manually annotated by BRENDA team
strain E1, isolated from human intestinal microflora, gene uidA
SwissProt
Manually annotated by BRENDA team
strain Georgi
SwissProt
Manually annotated by BRENDA team
strain Georgi
-
-
Manually annotated by BRENDA team
Scutellaria baicalensis Georgi
strain Georgi
SwissProt
Manually annotated by BRENDA team
Scutellaria baicalensis Georgi
strain Georgi
-
-
Manually annotated by BRENDA team
subspecies Streptococcus equi zooepidemicus
-
-
Manually annotated by BRENDA team
part of the normal flora of the respiratory and urogenital tracts of equines
UniProt
Manually annotated by BRENDA team
strain LJ-22, isolated from human intestinal microflora, two isozymes I and II
-
-
Manually annotated by BRENDA team
Streptococcus sp. LJ-22
strain LJ-22, isolated from human intestinal microflora, two isozymes I and II
-
-
Manually annotated by BRENDA team
strain MSB8, gene TM1062
SwissProt
Manually annotated by BRENDA team
cultivar Sathi
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
malfunction
-
beta-glucuronidase, an acid hydrolase that deconjugates glucuronides, may increase cancer risk
physiological function
-
beta-glucuronidase forms a complex with esterase 22 in the liver, both esterase Es22 and Gus play a role in liver retinoid metabolism
physiological function
-
beta-glucuronidase, an acid hydrolase that deconjugates glucuronides, may increase cancer risk
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(4GlcAbeta1-3GalNAc(4-OSO3-)beta1-)2 + H2O
D-glucuronate + ?
show the reaction diagram
-
no activity with enzyme acting on chondroitin, 142% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide
-
-
?
(4GlcAbeta1-3GalNAc(4-OSO3-)beta1-)3 + H2O
D-glucuronate + ?
show the reaction diagram
-
no activity with enzyme acting on chondroitin, 63% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide
-
-
?
(4GlcAbeta1-3GalNAc(6-OSO3-)beta1-)2 + H2O
D-glucuronate + ?
show the reaction diagram
-
no activity with enzyme acting on chondroitin, 50% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide
-
-
?
(4GlcAbeta1-3GalNAc(6-OSO3-)beta1-)3 + H2O
D-glucuronate + ?
show the reaction diagram
-
no activity with enzyme acting on chondroitin, 33% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide
-
-
?
(4GlcAbeta1-3GalNAcbeta1-)2 + H2O
D-glucuronate + ?
show the reaction diagram
-
66% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on chondroitin, 90% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide
-
-
?
(4GlcAbeta1-3GalNAcbeta1-)3 + H2O
D-glucuronate + ?
show the reaction diagram
-
56% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on chondroitin, 71% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide
-
-
?
(4GlcAbeta1-3GlcNAcbeta1-)3 + H2O
D-glucuronate + ?
show the reaction diagram
-
81% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on chondroitin, 73% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide
-
-
?
1-deoxy-1-(6-thiopurinyl)-beta-D-glucopyranoside + H2O
6-mercaptopurine + D-glucopyranose
show the reaction diagram
-
-
-
-
-
1-deoxy-1-(6-thiopurinyl)-beta-D-glucopyranosiduronamide + H2O
6-mercaptopurine + 1-deoxy-D-glucopyranosiduronamide
show the reaction diagram
-
-
-
-
-
4-Me-beta-GlcA-(1-6)-beta-Gal-(1-6)-beta-Gal-(1-3)-Gal + H2O
?
show the reaction diagram
-
rate of hydrolysis is 106% of the with p-nitrophenyl-beta-D-glucuronide
-
-
?
4-Me-beta-GlcA-(1-6)-beta-Gal-(1-6)-Gal + H2O
?
show the reaction diagram
-
rate of hydrolysis is 117% of the with p-nitrophenyl-beta-D-glucuronide
-
-
?
4-Me-beta-GlcA-(1-6)-Gal + H2O
?
show the reaction diagram
-
rate of hydrolysis is 62% of the with p-nitrophenyl-beta-D-glucuronide
-
-
?
4-methyl-beta-GlcA(1-6)beta-Gal(1-6)Gal + H2O
4-methyl-D-glucuronate + beta-Gal(1-6)Gal
show the reaction diagram
-, Q7SFB0
-
4.8% of the activity with 4-nitrophenyl beta-D-glucuronic acid
-
?
4-methyl-beta-GlcA(1-6)beta-Gal(1-6)Gal + H2O
4-methyl-D-glucuronate + beta-Gal(1-6)Gal
show the reaction diagram
-
-
42.6% of the activity with 4-nitrophenyl beta-D-glucuronic acid
-
?
4-methylumbelliferyl beta-D-glucuronide
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
Q97UI1
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
show the reaction diagram
Lentinula edodes LD 106
-
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferol + D-glucuronate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-galactosiduronide + H2O
4-nitrophenol + beta-D-galactosiduronic acid
show the reaction diagram
Q9X0F2, -
32% of the activity with 4-nitrophenyl beta-D-glucuronide
-
-
?
4-nitrophenyl beta-D-glucopyranosiduronic acid + 4-nitrophenyl beta-D-glucopyranosiduronic acid
4-nitrophenol + 4-nitrophenyl 3-O-beta-D-glucopyranuronosyl-beta-D-glucopyranosiduronic acid + 4-nitrophenyl 2-O-beta-D-glucopyranuronosyl-beta-D-glucopyranosiduronic acid
show the reaction diagram
-
-
-
-
-
4-nitrophenyl beta-D-glucopyranosiduronic acid + 4-nitrophenyl beta-D-glucopyranosiduronic acid
4-nitrophenol + 4-nitrophenyl 3-O-beta-D-glucopyranuronosyl-beta-D-glucopyranosiduronic acid + 4-nitrophenyl 2-O-beta-D-glucopyranuronosyl-beta-D-glucopyranosiduronic acid
show the reaction diagram
-
the enzyme shows transglucuronidation activity: when sodium (p-nitrophenyl beta-D-glucopyranoside)uronate is used as an acceptor and as a donor, sodium (sodium beta-D-glucopyranosyluronate)-(1-3)-(p-nitrophenyl beta-D-glucopyranosid)uronate and sodium (sodium beta-D-glucopyranosyluronate)-(1-2)-(p-nitrophenyl beta-D-glucopyranosid)uronate are obtained in yields of 18% and 15% respectively
-
-
-
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
-
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
Q7SFB0
-
-
-
-
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
Q9X0F2, -
low activity
-
-
?
4-nitrophenyl beta-D-glucuronic acid + H2O
4-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucuronic acid + H2O
4-nitrophenol + D-glucuronic acid
show the reaction diagram
Q7SFB0
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronate
show the reaction diagram
Scutellaria baicalensis, Scutellaria baicalensis Georgi
-
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
show the reaction diagram
[Ruminococcus] gnavus
-
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
show the reaction diagram
Q9X0F2, -
best substrate
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
show the reaction diagram
[Ruminococcus] gnavus E1
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
show the reaction diagram
-
preferred substrate
-
-
?
4-nitrophenyl D-glucuronide + H2O
4-nitrophenol + D-glucuronate
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
Q9AHJ8
-
-
-
?
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
Lactobacillus gasseri ATCC33323
Q9AHJ8
-
-
-
?
4-nitrophenyl-beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
show the reaction diagram
Lactobacillus brevis, Lactobacillus brevis RO1
-
-
-
-
?
4-phenolphthaleinyl beta-D-glucuronide + H2O
4-phenolphthalein + beta-D-glucuronic acid
show the reaction diagram
-
-
-
-
?
5-bromo-4-chloro-3-indoyl-beta-D-glucuronide + H2O
5-bromo-4-chloro-3-indole beta-D-glucuronate
show the reaction diagram
-
-
-
-
?
alpha-L-arabinosidase-treated-arabinogalactan-protein + H2O
?
show the reaction diagram
-
-
-
-
?
ammonium 1-deoxy-1-(6-thiopurinyl)-beta-D-glucopyranosidurate + H2O
6-mercaptopurine + ammonium 1-deoxy-(6-thiopurinyl)-beta-D-glucopyranosiduronate
show the reaction diagram
-
-
-
-
-
androstendione-enol-beta-D-glucuronide + H2O
?
show the reaction diagram
-
-
-
-
-
apigenin 7,4'-diglucuronide + H2O
apigenin 7-O-glucuronide + glucuronic acid
show the reaction diagram
-
-
-
-
-
baicalein 7-O-beta-D-glucuronide + H2O
baicalein + beta-D-glucuronic acid
show the reaction diagram
Q9LRC8, -
-
-
-
?
baicalein 7-O-beta-D-glucuronide + H2O
baicalein + beta-D-glucuronic acid
show the reaction diagram
Scutellaria baicalensis Georgi
Q9LRC8
-
-
-
?
baicalin + H2O
baicalein + D-glucuronate
show the reaction diagram
Q9LRC8, -
-
-
-
-
baicalin + H2O
baicalein + D-glucuronate
show the reaction diagram
-
-
-
-
?
baicalin + H2O
baicalein + D-glucuronate
show the reaction diagram
Scutellaria baicalensis Georg
-
-
-
-
?
baicalin + H2O
baicalein + D-glucuronate
show the reaction diagram
Scutellaria baicalensis Georgi
-
-
-
-
?
baicalin + H2O
baicalein + beta-D-glucuronic acid
show the reaction diagram
-
-, best substrate
-
-
?
baicalin + H2O
baicalein + beta-D-glucuronate
show the reaction diagram
-
-
-
-
?
baicalin + H2O
baicalein + beta-D-glucuronate
show the reaction diagram
-
a major flavonoid derived from the root of Scutellaria baicalensis
productivity of 73%
-
?
baicalin + H2O
baicalein + beta-D-glucuronate
show the reaction diagram
Lactobacillus brevis RO1
-
-
-
-
?
beta-GlcA(1-6)beta-Gal(1-6)Gal + H2O
D-glucuronate + beta-Gal(1-6)Gal
show the reaction diagram
-, Q7SFB0
-
67.4% of the activity with 4-nitrophenyl beta-D-glucuronic acid
-
?
beta-GlcA(1-6)betaGal(1-6)Gal + H2O
D-glucuronate + beta-Gal(1-6)Gal
show the reaction diagram
-
-
94.6% of the activity with 4-nitrophenyl beta-D-glucuronic acid
-
?
beta-GlcA-(1-3)-Gal + H2O
?
show the reaction diagram
-
rate of hydrolysis is 2% of the with p-nitrophenyl-beta-D-glucuronide
-
-
?
beta-GlcA-(1-6)-beta-Gal-(1-6)-Gal + H2O
beta-Gal-(1-6)-Gal + beta-D-glucuronic acid
show the reaction diagram
-
rate of hydrolysis is 67% of the with p-nitrophenyl-beta-D-glucuronide
-
-
?
beta-GlcA-(1-6)-Gal + H2O
D-galactose + beta-D-glucuronic acid
show the reaction diagram
-
rate of hydrolysis is 76% of the with p-nitrophenyl-beta-D-glucuronide
-
-
?
bilirubin diglucuronide + H2O
bilirubin + D-glucuronate
show the reaction diagram
Escherichia coli, Escherichia coli HGU-3
-
-
-
-
?
carboxyumbelliferyl-beta-D-glucuronide + H2O
carboxyumbelliferone + beta-D-glucuronate
show the reaction diagram
-
-
-
-
?
chondroitin + H2O
D-glucuronate + ?
show the reaction diagram
-
MW 3500 Da: 23% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on chondroitin, 41% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide. MW 8000 Da: 11% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on chondroitin, 28% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide. MW 15000 Da: 6% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on chondroitin, 9% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide
-
-
?
daidzein 7-O-beta-D-glucuronide + H2O
daidzein + D-glucuronate
show the reaction diagram
-
-
-
-
?
dermatan sulfate + H2O
?
show the reaction diagram
-
-
-
-
-
equol 7-O-beta-D-glucuronide + H2O
equol + D-glucuronate
show the reaction diagram
-
-
-
-
?
GlcA-beta(1-6)Gal + H2O
D-glucuronate + D-galactopyranose
show the reaction diagram
-, Q7SFB0
49.9% of the activity with 4-nitrophenyl beta-D-glucuronic acid
-
-
?
GlcAbeta(1-6)Gal + H2O
D-glucuronate + D-galactopyranose
show the reaction diagram
-
85.7% of the activity with 4-nitrophenyl beta-D-glucuronic acid
-
-
?
GlcAbeta1-3GalNAc(4-OSO3-) + H2O
D-glucuronate + N-acetylamino-beta-D-galactopyranose 4-sulfate
show the reaction diagram
-
no activity with enzyme acting on chondroitin, 4% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide
-
-
?
glucuronic acid 1-phosphate + H2O
glucuronic acid + phosphate
show the reaction diagram
-
-
-
-
-
glycyrrhizin + H2O
18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide + beta-D-glucuronic acid
show the reaction diagram
A7XS03, -
-
-
-
?
glycyrrhizin + H2O
18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide + beta-D-glucuronic acid
show the reaction diagram
Streptococcus sp., Streptococcus sp. LJ-22
-
specific substrate of isozymes I and II
-
-
?
heparan sulfate + H2O
?
show the reaction diagram
-
-
-
-
-
kaempferol 3-O-beta-D-glucuronide + H2O
kaempferol + D-glucuronate
show the reaction diagram
-
-
-
-
?
luteolin 3'-O-beta-glucuronide + H2O
luteolin + D-glucuronate
show the reaction diagram
Scutellaria baicalensis, Scutellaria baicalensis Georgi
-
-
-
-
?
luteolin 7-O-glucuronide + H2O
?
show the reaction diagram
-
-
-
-
-
luteolin 7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide] + H2O
?
show the reaction diagram
-
-
-
-
-
luteolin 7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide]-4'-O-glucuronide + H2O
?
show the reaction diagram
-
-
-
-
-
luteolin triglucuronide + H2O
?
show the reaction diagram
-
-
-
-
-
naphthol AS-BI-D-glucuronide + H2O
?
show the reaction diagram
-
-
-
-
-
o-nitrophenyl-beta-D-glucuronide + H2O
o-nitrophenol + D-glucuronic acid
show the reaction diagram
Escherichia coli, Escherichia coli K12
-
-
-
-
?
oestrone 3-glucuronide + H2O
?
show the reaction diagram
-
-
-
-
-
oroxylin 7-O-beta-D-glucuronide + H2O
oroxylin + D-glucuronate
show the reaction diagram
Scutellaria baicalensis, Scutellaria baicalensis Georgi
-
-
-
-
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronate
show the reaction diagram
Escherichia coli, Escherichia coli HGU-3
-
-
-
-
?
p-nitrophenyl-beta-D-glucuronide + H2O
D-glucuronate + ?
show the reaction diagram
-
1% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on chondroitin, 192% of the activity with (4GlcAbeta1-3GlcNAc1-)2 with the enzyme acting on p-nitrophenyl-beta-D-glucuronide
-
-
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + beta-D-glucuronic acid
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + beta-D-glucuronic acid
show the reaction diagram
-, Q9AHJ8
-
-
-
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + beta-D-glucuronic acid
show the reaction diagram
Q9AHJ8
-
-
-
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
show the reaction diagram
Escherichia coli, Escherichia coli K12
-
-
-
-
?
phenolphthalein beta-D-glucuronide + H2O
phenolphthalein + beta-D-glucuronate
show the reaction diagram
-
determination of specific activity in betaG-expressing tumour CT26 cells using radio-labeled substrate
-
-
?
phenolphthalein-beta-D-glucuronic acid + H2O
phenolphthalein + D-glucuronic acid
show the reaction diagram
-
-
-
-
ir
phenolphthalein-beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
phenolphthalein-beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
show the reaction diagram
-
-
-
-
?
phenolphthalein-beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
phenolphthalein-beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
show the reaction diagram
-
-
-
-
-
quercetin 3-O-beta-D-glucuronide + H2O
quercetin + D-glucuronate
show the reaction diagram
-
-
-
-
?
quercetin 7-O-beta-D-glucuronide + H2O
quercetin + D-glucuronate
show the reaction diagram
-
-
-
-
?
quercetin-4'-O-glucuronide + H2O
quercetin + D-glucuronate
show the reaction diagram
-
-
-
-
?
retinyl-beta-glucuronide + H2O
retinol + D-glucuronide
show the reaction diagram
-
-
-
-
?
sodium (p-nitrophenyl beta-D-glucopyranoside)uronate + p-nitrophenyl alpha-D-galactopyranoside
p-nitrophenyl (sodium beta-D-glucopyranosyluronate)-(1-4)-alpha-D-galactopyranoside + p-nitrophenyl (sodium beta-D-glucopyranosyluronate)-(1-2)-alpha-D-galactopyranoside
show the reaction diagram
-
the enzyme shows transglucuronidation activity: when (p-nitrophenyl beta-D-glucopyranoside)uronate is used as a donor and p-nitrophenyl alpha-D-galactopyranoside is used as an acceptor, p-nitrophenyl (sodium beta-D-glucopyranosyluronate)-(1-4)-alpha-D-galactopyranoside and p-nitrophenyl (sodium beta-D-glucopyranosyluronate)-(1-2)-alpha-D-galactopyranoside are synthesized in yields of 16% and 21% respectively
-
-
-
wogonin + H2O
wogonin aglycon + beta-D-glucuronate
show the reaction diagram
Lactobacillus brevis, Lactobacillus brevis RO1
-
-
-
-
?
wogonin 7-O-beta-D-glucuronide + H2O
wogonin + D-glucuronate
show the reaction diagram
-
-
-
-
?
wogonin glucuronide + H2O
wogonin + D-glucuronate
show the reaction diagram
Scutellaria baicalensis, Scutellaria baicalensis Georg
-
-
-
-
?
methylumbelliferyl-beta-D-glucuronide + H2O
methylumbelliferone + beta-D-glucuronate
show the reaction diagram
-
-
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
transfer of beta-glucuronosyl residues from aryl and alicyclic glucuronides to aliphatic alcohols and glycerols
-
-
-
additional information
?
-
-
transglycosylation activity
-
-
-
additional information
?
-
-
role in physiology, in tissues, in body fluids
-
-
-
additional information
?
-
-
activity is inducible by Met-Gly
-
-
-
additional information
?
-
-
activity is not inducible by Met-Gly
-
-
-
additional information
?
-
-
activity is slightly inducible by Met-Gly
-
-
-
additional information
?
-
Q9LRC8, -
the enzyme is involved in the initiation of H2O2 metabolism
-
-
-
additional information
?
-
-
the potent beta-glucuronidase activity caused by the glucuronic acid conjugates from xenobiotics and endogenous compounds is a prime factor in the etiology of colon cancer
-
-
-
additional information
?
-
-
when beta-glucuronidase producing bacteria infect the bile, the pH of the bile becomes raised, the high pH and bile induce the enzyme, and then bilirubin gallstones can be easily formed
-
-
-
additional information
?
-
-
no activity with baicalein 7-O-beta-D-glucoside
-
-
-
additional information
?
-
-
no activity with enzyme acting on chondroitin: N-acetylhyalobiuronic acid, N-acetylchondrosine, (4GlcAbeta1-3GalNAc(4-OSO3-)beta1-)3, (4GlcAbeta1-3GalNAc(4-OSO3-)beta1-)2, GlcAbeta1-3galNAc(4-OSO3-), (4GlcAbeta1-3GalNAc(6-OSO3-)beta1-)3, (4GlcAbeta1-3GalNAc(6-OSO3-)beta1-)2. No activity with enzyme acting on p-nitrophenyl-beta-D-glucuronide: N-acetylhyalobiuronic acid, N-acetylchondrosine
-
-
-
additional information
?
-
-
no hydrolysis of glycyrrhizin, luteolin-7-O-D-glucoside and apigenin-7-O-D-glucoside
-
-
-
additional information
?
-
-
the enzyme is involved in glycosaminoglycan metabolism, exoglucuronidase
-
-
-
additional information
?
-
-
no activity of isozymes I and II with 4-nitrophenyl beta-D-glucuronide, baicalin, and 18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide
-
-
-
additional information
?
-
-
no activity with 4-nitrophenyl beta-D-glucoside
-
-
-
additional information
?
-
-
substrate specificity with flavonoids and phytoestrogens of crude and purified enzyme from digestive juice, overview
-
-
-
additional information
?
-
-
enzyme additionally catalyzes the transglycosylation of glucuronic acid residues from 4-nitrophenyl beta-D-glucuronic acid to various monosaccharide acceptors such as glucose, galactose, and xylose
-
-
-
additional information
?
-
Q7SFB0
enzyme additionally catalyzes the transglycosylation of glucuronic acid residues from 4-nitrophenyl beta-D-glucuronic acid to various monosaccharide acceptors such as glucose, galactose, and xylose
-
-
-
additional information
?
-
-
the beta-glucuronidase forms a complex with esterase 22 in the liver. Gus colocalizes with Es22 at the endoplasmic reticulum but does not affect its retinoyl ester hydrolase activity
-
-
-
additional information
?
-
Escherichia coli HGU-3
-
when beta-glucuronidase producing bacteria infect the bile, the pH of the bile becomes raised, the high pH and bile induce the enzyme, and then bilirubin gallstones can be easily formed
-
-
-
additional information
?
-
Scutellaria baicalensis Georg
-
no hydrolysis of glycyrrhizin, luteolin-7-O-D-glucoside and apigenin-7-O-D-glucoside
-
-
-
additional information
?
-
Scutellaria baicalensis Georgi
-
no activity with baicalein 7-O-beta-D-glucoside
-
-
-
additional information
?
-
Scutellaria baicalensis Georgi
Q9LRC8
the enzyme is involved in the initiation of H2O2 metabolism
-
-
-
additional information
?
-
Streptococcus sp. LJ-22
-
no activity of isozymes I and II with 4-nitrophenyl beta-D-glucuronide, baicalin, and 18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
baicalin + H2O
baicalein + beta-D-glucuronic acid
show the reaction diagram
-
-
-
-
?
dermatan sulfate + H2O
?
show the reaction diagram
-
-
-
-
-
heparan sulfate + H2O
?
show the reaction diagram
-
-
-
-
-
oestrone 3-glucuronide + H2O
?
show the reaction diagram
-
-
-
-
-
retinyl-beta-glucuronide + H2O
retinol + D-glucuronide
show the reaction diagram
-
-
-
-
?
luteolin triglucuronide + H2O
?
show the reaction diagram
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
role in physiology, in tissues, in body fluids
-
-
-
additional information
?
-
-
activity is inducible by Met-Gly
-
-
-
additional information
?
-
-
activity is not inducible by Met-Gly
-
-
-
additional information
?
-
-
activity is slightly inducible by Met-Gly
-
-
-
additional information
?
-
Q9LRC8, -
the enzyme is involved in the initiation of H2O2 metabolism
-
-
-
additional information
?
-
-
the potent beta-glucuronidase activity caused by the glucuronic acid conjugates from xenobiotics and endogenous compounds is a prime factor in the etiology of colon cancer
-
-
-
additional information
?
-
-
when beta-glucuronidase producing bacteria infect the bile, the pH of the bile becomes raised, the high pH and bile induce the enzyme, and then bilirubin gallstones can be easily formed
-
-
-
additional information
?
-
-
the enzyme is involved in glycosaminoglycan metabolism
-
-
-
additional information
?
-
-
the beta-glucuronidase forms a complex with esterase 22 in the liver. Gus colocalizes with Es22 at the endoplasmic reticulum but does not affect its retinoyl ester hydrolase activity
-
-
-
additional information
?
-
Escherichia coli HGU-3
-
when beta-glucuronidase producing bacteria infect the bile, the pH of the bile becomes raised, the high pH and bile induce the enzyme, and then bilirubin gallstones can be easily formed
-
-
-
additional information
?
-
Scutellaria baicalensis Georgi
Q9LRC8
the enzyme is involved in the initiation of H2O2 metabolism
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ca2+
-
-
Ca2+
-
activates 7% at 100 mM
Ca2+
A7XS03, -
activity enhanced
Fe2+
A7XS03, -
activity enhanced
K+
A7XS03, -
activity enhanced
Mg2+
-
-
Mg2+
-
activates 26% at 100 mM
Mg2+
-
activates
Mg2+
A7XS03, -
activity enhanced
Na+
A7XS03, -
activity enhanced
NaCl
-
-
NaCl
-
below 0.075 M the activity of beta-glucuronidase acting on chondroitin is increased with increasing NaCl concentrations.The activity of beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide is decreased with increasing NaCl concentrations, and 0.4 M NaCl produces 50% inhibition
Mn2+
A7XS03, -
activity enhanced
additional information
-
Na+, K+, Mg2+, Mn2+, and Ca2+ increase the activity but with no significance
additional information
A7XS03, -
the catalytic activity of recombinant PGUS expressed under low-shear modeled microgravity is less affected by metal ions and EDTA as compared with that of normal gravity
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1,4-D-glucarolactone
-
specific reversible inhibition
2-deoxy-2-fluoro-beta-D-glucosyluronic acid fluoride
Q9X0F2
inactivation the recombinant His6-tagged enzyme
4-chloromercuriphenylsulfonic acid
-
inhibition of isozymes I and II
Ag+
-
0.3 mM, 20-25% inhibition
ascorbic acid
-
-
ascorbic acid
-
-
azide
-
50 mM, 70% loss of activity of wild-type enzyme and mutant enzyme E451A. 50 mM-0.5 M, stimulation of mutant enzyme E451A. 1 mM, inhibition of wild-type enzyme and mutant enzyme E451A
Ca2+
-
0.3 mM, 15% inhibition
CaCl2
-
2 mM, 14.8% inhibition
Citric acid
-
-
Cu2+
-
0.3 mM, 20-25% inhibition
Cu2+
-
inhibition of isozymes I and II
Cu2+
-
inhibits 29% at 100 mM
D-glucaric acid 1,4-lactone
-
5 mM, 30% inhibition
D-glucaro-1,4-lactone
-
-
D-glucose
-
10 mM, about 15% inhibition
D-glucuronate
-
IC50: 7.5 mM, competitive
D-glucuronic acid
-
10 mM, about 15% inhibition
D-saccharic acid 1,4-lactone
-
-
D-saccharic acid 1,4-lactone
-
-
D-saccharic acid 1,4-lactone
-
-
D-saccharic acid 1,4-lactone
-
-
D-saccharic acid 1,4-lactone
Q9X0F2
competitive, protects the enzyme against inactivation by 2-deoxy-2-fluoro-beta-D-glucosyluronic acid fluoride
D-saccharic acid 1,4-lactone
-
-
D-saccharic acid 1,4-lactone monohydrate
-
a betaG-specific inhibitor
D-saccharic acid-1,4-lactone
-
-
delta-D-glucuronolactone
-
-
estradiol 3-glucuronide
-
-
Fe2+
-
inhibits 29% at 1 mM, 71% at 100 mM
FeCl2
-
2 mM,33.1% inhibition
glucuronic acid
-
-
glucuronic acid
-
-
glucuronic acid
-
-
glycyrrhizin
-
IC50: 0.08 mM, competitive
glycyrrhizin
-
-
Hg2+
-
reversed by EDTA
Hg2+
-
reversed by EDTA
Hg2+
-
1 mM, 37C, 10 min, 23% inhibition
Inhibitor
-
heat stable, competetive, in plasma
-
Inhibitor
-
from endogenous tissue
-
methanol
-
concentration: 15%, 10-20% inhibition
MgCl2
-
2 mM, 24.8% inhibition
NaCl
-
between 0.075 and 0.25 M, the activity is decreased with increasing NaCl concentration. Above 0.25 M, the enzyme shows no activity. The activity of beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide is decreased with increasing NaCl concentrations, and 0.4 M NaCl produces 50% inhibition
NEM
-
IC50: 0.09 mM
NiCl2
-
2 mM, 52% inhibition
p-chloromercuribenzoate
-
-
p-Chloromercuriphenylsulfonic acid
-
IC50: 0.04 mM
p-nitrophenol
-
IC50: 0.3 mM, competitive
paracetamol glucuronide
-
-
Phenolic and alcoholic glucuronides
-
-
-
Potassium saccharate
-
-
S-saccharic acid 1,4-lactone
-
inhibits enzyme in several patients with colon cancer in addition to the healthy controls
saccharic acid 1,4-lactone
-, Q9AHJ8
80% inhibition by 0.5 mM, 88% inhibition by 1.0 mM
saccharic acid 1,4-lactone
-
IC50: 0.09 mM, competitive
saccharo-1,4-lactone
-
-
saccharo-1,4-lactone
-
complete inhibition of liver enzyme
silybin
-
IC50: 1 mM, non-competitive
Sodium desoxycholate
-
-
TLCK
-
IC50: 0.3 mM
Zn2+
-
inhibits 7% at 100 mM
MnCl2
-
2 mM, 31.9% inhibition
additional information
-
Mg2+ shows no effect
-
additional information
-
lower beta-glucuronidase activity is significantly associated with higher intakes of calcium, iron, and magnesium. Several dietary and nondietary factors are associated with beta-glucuronidase activity. The botanical families Cruciferae, Rutaceae, Compositae, Roseaceae, and Umbelliferae might decrease the enzyme activity when being part of the diet
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
abscisic acid
-
1.49fold increased enzyme activity after application of 100 micromo/l abscisic acid for 6 h
azide
-
50 mM-0.5 M, stimulation of mutant enzyme E451A
Bovine serum albumin
-
activation
-
Bovine serum albumin
-
activation
-
chlorpyrifos-methyl
-
-
Dichlorvos
-
-
ethyleneglycol
-
activation
fenitrothion
-
-
pectin-protein complex
-
adsorption of beta-glucuronidase on biopolymers is studied by the retention of the enzyme on the membrane of a concentrator with a pore diameter of 300 kDa and by native PAGE. Pectin-protein complexes (fractions PPC/CP and PPC/C) are established to increase the activity of beta-glucuronidase by 50 and 100%, respectively. There is a positive correlation between the increase of beta-glucuronidase activity in the presence of carbohydrates and enzyme adsorption on the polymers. The activity of the enzyme in the gel after electrophoresis of the PPC/+ beta-glucuronidase mixture is inversely proportional to the concentration of PPC/C in the mixture
-
Plasma serum
-
acivation
-
propetamphos
-
-
salicylic acid
-
44.6% increase of enzyme activity after treatment with 1 mmol/l salicylic acid for 5 h
lactose
-
uncompetitive activator
additional information
-
85.2% increased activity in response to 250 mmol/l NaCl for 8 h; increased expression and 1.87fold enzyme activity at dehydratation
-
additional information
-
higher beta-glucuronidase activity is significantly associated with being male, over 30 years old, non-Caucasian, overweighted, and exhibiting higher intakes of gamma-tocopherol. Several dietary and nondietary factors are associated with beta-glucuronidase activity
-
additional information
-
organophosphorous insecticides lead to several fold increased plasma enzyme activity, overview
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.49
-
1-Deoxy-1-(6-thiopurinyl)-beta-D-glucopyranoside
-
-
9.25
-
1-Deoxy-1-(6-thiopurinyl)-beta-D-glucopyranosiduronamide
-
-
1.4
-
4-Me-beta-GlcA-(1-6)-beta-Gal-(1-6)-beta-Gal-(1-3)-Gal
-
pH 4.6, 37C
1.9
-
4-Me-beta-GlcA-(1-6)-beta-Gal-(1-6)-Gal
-
pH 4.6, 37C
3.6
-
4-Me-beta-GlcA-(1-6)-Gal
-
pH 4.6, 37C
0.54
-
4-methylumbelliferyl beta-D-glucuronide
Q97UI1
pH 6.5, 75C
0.58
-
4-methylumbelliferyl beta-D-glucuronide
Q97UI1
pH 6.5, 65C
0.041
1.3
4-methylumbelliferyl-beta-D-glucuronide
-
-
0.041
1.3
4-methylumbelliferyl-beta-D-glucuronide
-
-
1.04
-
4-methylumbelliferyl-beta-D-glucuronide
-
enzyme from kidney
1.2
-
4-methylumbelliferyl-beta-D-glucuronide
-
37C, pH 5.0, mutant enzyme E540A
1.3
-
4-methylumbelliferyl-beta-D-glucuronide
-
pH 5, 37C
1.32
-
4-methylumbelliferyl-beta-D-glucuronide
-
enzyme from liver
1.33
-
4-methylumbelliferyl-beta-D-glucuronide
-
37C, pH 4.0-5.0, mutant enzyme E451A
1.67
-
4-methylumbelliferyl-beta-D-glucuronide
-
37C, mutant enzyme Y540A
2.76
-
4-methylumbelliferyl-beta-D-glucuronide
-
37C, pH 4.5, wild-type enzyme
3.06
-
4-nitrophenyl beta-D-galactosiduronide
Q9X0F2
pH 6.5, 75C, recombinant His6-tagged enzyme
0.0304
-
4-nitrophenyl beta-D-glucoside
-
-
0.0383
-
4-nitrophenyl beta-D-glucoside
-, Q7SFB0
-
145
-
4-nitrophenyl beta-D-glucoside
Q9X0F2
pH 6.5, 75C, recombinant His6-tagged enzyme
0.152
-
4-nitrophenyl beta-D-glucuronide
Q9X0F2
pH 6.5, 75C, recombinant His6-tagged enzyme
0.36
-
4-nitrophenyl beta-D-glucuronide
-
wild-type enzyme
167.5
-
4-nitrophenyl beta-D-glucuronide
-
28C, pH 6.5
0.2
-
4-nitrophenyl beta-D-xylopyranoside
-
wild-type enzyme
0.208
-
4-nitrophenyl-beta-D-glucuronide
-
wild type enzyme
0.414
-
4-nitrophenyl-beta-D-glucuronide
-
mutant enzyme Q493R/T509A/M532T/N550S/G559S/N566S
1.4
-
4-nitrophenyl-beta-D-glucuronide
-
pH 7.2, 37C
0.132
-
Ammonium 1-deoxy-1-(6-thiopurinyl)-beta-D-glucopyranosidurate
-
-
0.0097
-
baicalein 7-O-beta-D-glucuronide
Q9LRC8, -
pH 6.5, 28C, mutant enzyme E329A
0.0103
-
baicalein 7-O-beta-D-glucuronide
Q9LRC8, -
pH 6.5, 28C, mutant enzyme E212A
0.0121
-
baicalein 7-O-beta-D-glucuronide
Q9LRC8, -
pH 6.5, 28C, wild-type enzyme
0.027
-
baicalein 7-O-beta-D-glucuronide
Q9LRC8, -
pH 6.5, 28C, mutant enzyme Y281A
0.01
-
Baicalin
-
28C, pH 6.5
0.038
-
Baicalin
-
pH 4.7, 30C
0.53
-
beta-GlcA-(1-6)-beta-Gal-(1-6)-Gal
-
pH 4.6, 37C
0.71
-
beta-GlcA-(1-6)-Gal
-
pH 4.6, 37C
0.91
-
carboxyumbelliferyl-beta-D-glucuronide
-
pH 6.5, 38C, Vmax: 0.041 mM/min
-
6.3
-
Chondroitin
-
pH 5.0, 37C
0.272
-
daidzein 7-O-beta-D-glucuronide
-
pH 7.2, 37C
0.266
-
equol 7-O-beta-D-glucuronide
-
pH 7.2, 37C
0.2
-
estriol-3-glucuronide
-
estriol-16-alpha-glucuronide
0.378
-
GlcAbeta(1-6)Gal
-, Q7SFB0
-
0.422
-
GlcAbeta(1-6)Gal
-
-
1.72
-
glycyrrhizin
A7XS03, -
pH 5, 55C, low-shear modeled microgravity
7.72
-
glycyrrhizin
A7XS03, -
pH 5, 55C, normal gravity
0.025
-
kaempferol 3-O-beta-D-glucuronide
-
pH 7.2, 37C
0.009
-
luteolin 3'-O-beta-glucuronide
-
28C, pH 6.5
0.007
-
luteolin 7-O-diglucuronide 4'-O-glucuronide
-
-
0.02
-
oestrone-3-glucuronide
-
-
0.04
-
oroxylin-7-O-beta-D-glucuronide
-
28C, pH 6.5
0.13
2.9
p-nitrophenyl-beta-D-glucuronide
-
-
0.13
2.9
p-nitrophenyl-beta-D-glucuronide
-
-
0.13
2.9
p-nitrophenyl-beta-D-glucuronide
-
-
0.13
2.9
p-nitrophenyl-beta-D-glucuronide
-
-
0.13
2.9
p-nitrophenyl-beta-D-glucuronide
-
-
0.13
2.9
p-nitrophenyl-beta-D-glucuronide
-
-
0.22
-
p-nitrophenyl-beta-D-glucuronide
-
pH 7.0, 37C
0.23
-
p-nitrophenyl-beta-D-glucuronide
-
pH 4.6, 37C
0.018
3.08
phenolphthalein glucuronide
-
dependency on form of enzyme
0.018
3.08
phenolphthalein glucuronide
-
-
0.018
3.08
phenolphthalein glucuronide
-
dependency on pH
2.907
-
phenolphthalein-beta-D-glucuronic acid
-
pH 5.0, 52C
0.048
-
quercetin 4'-O-beta-D-glucuronide
-
pH 7.2, 37C
0.237
-
quercetin 7-O-beta-D-glucuronide
-
pH 7.2, 37C
0.167
-
quercetin-3-O-beta-D-glucuronide
-
pH 7.2, 37C
0.03
-
wogonin 7-O-beta-D-glucuronide
-
28C, pH 6.5
0.065
-
methylumbelliferyl-beta-D-glucuronide
-
pH 6.5, 38C, Vmax: 0.026 mM/min
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
-
-
additional information
-
additional information
Q9X0F2
kinetics of mutant enzymes, overview
-
additional information
-
additional information
-
kinetics of mutant enzymes, overview
-
additional information
-
additional information
-
-
-
additional information
-
additional information
-
kinetics
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.004
-
4-methylumbelliferyl-beta-D-glucuronide
-
37C, pH 5.0, mutant enzyme E540A
0.015
-
4-methylumbelliferyl-beta-D-glucuronide
-
37C, pH 4.0-5.0, mutant enzyme E451A
0.2
-
4-methylumbelliferyl-beta-D-glucuronide
-
37C, mutant enzyme Y540A
276
-
4-methylumbelliferyl-beta-D-glucuronide
-
37C, pH 4.5, wild-type enzyme
443
-
4-nitrophenyl beta-D-galactosiduronide
Q9X0F2
pH 6.5, 75C, recombinant His6-tagged enzyme
9
-
4-nitrophenyl beta-D-glucoside
Q9X0F2
pH 6.5, 75C, recombinant His6-tagged enzyme
0.001
-
4-nitrophenyl beta-D-glucuronide
-
wild-type enzyme
29
-
4-nitrophenyl beta-D-glucuronide
Q9X0F2
pH 6.5, 65C, recombinant His6-tagged enzyme
68
-
4-nitrophenyl beta-D-glucuronide
Q9X0F2
pH 6.5, 75C, recombinant His6-tagged enzyme
68
-
4-nitrophenyl beta-D-xylopyranoside
-
wild-type enzyme
0.67
-
4-nitrophenyl-beta-D-glucuronide
-
pH 7.2, 37C
1100
-
4-nitrophenyl-beta-D-glucuronide
-
mutant enzyme Q493R/T509A/M532T/N550S/G559S/N566S
1500
-
4-nitrophenyl-beta-D-glucuronide
-
wild type enzyme
200
-
4-nitrophenyl-beta-glucuronide
-
-
0.011
-
baicalein 7-O-beta-D-glucuronide
Q9LRC8, -
pH 6.5, 28C, mutant enzyme E329A
0.135
-
baicalein 7-O-beta-D-glucuronide
Q9LRC8, -
pH 6.5, 28C, mutant enzyme E212A
0.77
-
baicalein 7-O-beta-D-glucuronide
Q9LRC8, -
pH 6.5, 28C, mutant enzyme Y281A
639
-
baicalein 7-O-beta-D-glucuronide
Q9LRC8, -
pH 6.5, 28C, wild-type enzyme
1.07
-
daidzein 7-O-beta-D-glucuronide
-
pH 7.2, 37C
0.35
-
equol 7-O-beta-D-glucuronide
-
pH 7.2, 37C
23.3
-
glycyrrhizin
A7XS03, -
pH 5, 55C, low-shear modeled microgravity
27.84
-
glycyrrhizin
A7XS03, -
pH 5, 55C, normal gravity
0.65
-
kaempferol 3-O-beta-D-glucuronide
-
pH 7.2, 37C
0.26
-
quercetin 4'-O-beta-D-glucuronide
-
pH 7.2, 37C
1.65
-
quercetin 7-O-beta-D-glucuronide
-
pH 7.2, 37C
1.9
-
quercetin-3-O-beta-D-glucuronide
-
pH 7.2, 37C
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
3.61
-
glycyrrhizin
A7XS03, -
pH 5, 55C, normal gravity
4646
13.55
-
glycyrrhizin
A7XS03, -
pH 5, 55C, low-shear modeled microgravity
4646
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.024
-
D-saccharic acid 1,4-lactone
Q9X0F2
pH 6.5, 75C, recombinant His6-tagged enzyme
0.9
-
estradiol 3-glucuronide
-
enzyme from liver
1.2
-
estradiol 3-glucuronide
-
enzyme from kidney
0.47
-
glycyrrhizin
-
enzyme from liver
1.6
-
paracetamol glucuronide
-
enzyme from liver
2
-
paracetamol glucuronide
-
enzyme from kidney
0.57
-
glycyrrhizin
-
enzyme from kidney
additional information
-
additional information
Q9X0F2
-
-
IC50 VALUE [mM]
IC50 VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
7.5
-
D-glucuronate
-
IC50: 7.5 mM, competitive
0.08
-
glycyrrhizin
-
IC50: 0.08 mM, competitive
0.09
-
NEM
-
IC50: 0.09 mM
0.04
-
p-Chloromercuriphenylsulfonic acid
-
IC50: 0.04 mM
0.3
-
p-nitrophenol
-
IC50: 0.3 mM, competitive
0.09
-
saccharic acid 1,4-lactone
-
IC50: 0.09 mM, competitive
1
-
silybin
-
IC50: 1 mM, non-competitive
0.3
-
TLCK
-
IC50: 0.3 mM
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.000144
-
-
at pH 7.0 and 37C
0.08
-
Q6W7J7, -
activity in crude cell extract from cell after growth for 9 h, activity-growth curve
0.127
-
-
beta-glucuronidase acting on chondroitin
0.137
-
-
purified isozyme I
0.19
-
-
purified isozyme II
9.37
-
-
purified enzyme, substrate 4-nitrophenyl beta-D-glucuronide
17.78
-
-
-
22.6
-
-
reaction with p-nitrophenyl-beta-D-glucuronide
23
-
-
pH 5.0, 45C
29.3
-
-
reaction with beta-GlcA-(1-6)-Gal
29.3
-
-, Q7SFB0
pH 6.0, 37C
30.6
-
-
pH 4.0, 37C
31.33
-
-
-
117
-
-
purified recombinant enzyme, at pH 7.0 and 37C
160
-
-
purified recombinant enzyme, at pH 5.6 and 37C
173.4
-
-
activity with wogonin 7-O-beta-D-glucuronide
270
-
-
purified recombinant enzyme, at pH 7.0 and 52C
1284
-
-
purified recombinant enzyme
additional information
-
-
-
additional information
-
-
assay method
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
assay method
additional information
-
-
-
additional information
-
-
-
additional information
-
-
activities of crude and purified enzyme from digestive juice
additional information
-
-
-
additional information
-
-
the specific activity of the wild type and mutant enzyme Q493R/T509A/M532T/N550S/G559S/N566S are approximately 142.9 and 43.1 units/mg at 37C and pH 6.5
additional information
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.6
-
-
form III
3
-
-
substrate 4-methylumbelliferyl-beta-D-glucuronide
3
-
-
reaction with beta-GlcA-(1-6)-Gal and p-nitrophenyl-beta-D-glucuronide
3.2
-
-
form II
3.4
-
-
form I
3.4
-
-
form II
3.8
-
-
-
4
4.4
-
acetate buffer
4
5
-
mutant enzyme E451A
4.1
-
-
form II
4.3
-
-
-
4.3
-
-
-
4.4
-
-
form I
4.4
-
-
-
4.5
6.5
Q97UI1
highly active in the pH-range 4.5-6.5
4.5
-
-
beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide
4.5
-
-
wild-type enzyme
4.6
-
-
assay at
4.7
-
-
-
4.7
-
-
-
4.7
-
-
Na-citrate buffer
5
-
-
beta-glucuronidase acting on chondroitin
5
-
-
mutant enzyme E540A
5
-
-
liver enzyme
5
-
-
kidney enzyme
5
-
-
recombinant enzyme
5.4
-
-
citrate buffer
6
-
-, Q9AHJ8
-
6
-
-
activity with wogonin 7-O-beta-D-glucuronide
6
-
-, Q7SFB0
activity gradually decreases below
6.5
-
Q9X0F2
-
6.5
-
-
purified isozyme II
6.5
-
Q97UI1
assay at
6.8
-
-
soluble and immobilized
6.8
-
Q6W7J7, -
assay at
7
-
-
purified isozyme I
7
-
-
assay at
7
-
-
free and encapsulated enzyme
7.6
-
-
assay at
8
-
-
assay at, recombinant RFP-tagged enzyme
additional information
-
-
comparison of values for different substrates and organisms
additional information
-
-
comparison of values for different substrates and organisms
additional information
-
-
comparison of values for different substrates and organisms
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2.1
5.8
-
half maximal activity
3
5
-
pH 3.0: about 50% of maximal activity, pH 5.0: about 70% of maximal activity, beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide
3
6.5
-
pH profile, liver enzyme
3
7
-
pH profile, kidney enzyme
4
5.5
-
pH 4.0: about 45% of maximal activity, pH 5.5: about 90% of maximal activity, pH 6.0: no activity, beta-glucuronidase acting on chondroitin
4
7
-, Q9AHJ8
pH 4.0: about 50% of maximal activity, pH 7.0: 25% of maximal activity
4
9
-
pH profile
4
-
-
70% activity
4.5
7.5
Q9X0F2
-
5
8.5
-
pH 5.0: about 45% of maximal activity, pH 8.5: about 50% of maximal activity
6
7
Q9AHJ8
activity is limited in neutral pH ranges of 6-7
6
-
-
90% activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
37
-
Q6W7J7, -
assay at
37
-
-
assay at
37
-
-
assay at, recombinant RFP-tagged enzyme
37
-
-
recombinant enzyme
37
-
-
assay at
37
-
-
assay at
37
-
-
assay at
45
-
-
activity at 44.5C is higher than at 25C and at 35C
45
-
-
wild type enzyme
45
-
Q7SFB0
-
52
-
-
liver enzyme
52
-
-
kidney enzyme
56
-
-
-
60
-
-
-
60
-
-
free and encapsulated enzyme
65
-
-, Q9AHJ8
-
65
-
-
mutant enzymes Q493R/T509A/M532T/N550S/G559S/N566S
70
-
-
-
75
-
Q97UI1
assay at
additional information
-
-
assay carried out at room temperature
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
30
45
A7XS03, -
-
30
70
-
temperature profile
37
100
Q97UI1
37C: about 40% of maximal activity, 100C: about 50% of maximal activity
37
75
-, Q9AHJ8
37C: about 60% of maximal activity, 75C: about 90% of maximal activity
38
70
-
inactive at 80C, temperature profile, liver enzyme
38
70
-
temperature profile, inactive above 70C, kidney enzyme
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4.9
-
-
chromatofocusing
4.9
-
-
chromatofocusing
5
-
-
isoelectric focusing, pH-range: 3.5-10
5.1
-
-
calculated
5.5
-
Q9LRC8, -
isoelectric focusing
5.5
-
-
isoelectric focusing
6.8
-
-, Q7SFB0
calculated
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
Scutellaria baicalensis Georgi
-
;
-
Manually annotated by BRENDA team
-
Pectinex Ultra SP-L, Lot No. G 770
Manually annotated by BRENDA team
Agrobacterium sp. GV3101
-
-
-
Manually annotated by BRENDA team
-
the enzyme is present during embryogenesis
Manually annotated by BRENDA team
-
the enzyme is present during embryogenesis
Manually annotated by BRENDA team
-
of patients with colon cancer and healthy controls
Manually annotated by BRENDA team
-
expresses only the lysosomal form of the enzyme
Manually annotated by BRENDA team
Agrobacterium sp. GV3101
-
-
-
Manually annotated by BRENDA team
-
high varability in the expression
Manually annotated by BRENDA team
Agrobacterium sp. GV3101
-
-
-
Manually annotated by BRENDA team
-
chronic myelogenous
Manually annotated by BRENDA team
-
high varability in the expression
Manually annotated by BRENDA team
Lentinula edodes LD 106
-
-
-
Manually annotated by BRENDA team
Agrobacterium sp. GV3101
-
-
-
Manually annotated by BRENDA team
Scutellaria baicalensis Georg
-
-
-
Manually annotated by BRENDA team
Agrobacterium sp. GV3101
-
-
-
Manually annotated by BRENDA team
-
activity in round spermatids is detected in multivesicular bodies and acrosomal vesicles, activity in elongated spermatids is detected in sickle-shaped acrosome and in the residual body
Manually annotated by BRENDA team
-
activity in lysosome-like bodies
Manually annotated by BRENDA team
-
activity in acrosome and in cytoplasmic droplets
Manually annotated by BRENDA team
additional information
-
from armadillo liver infected with Mycobacterium leprae
Manually annotated by BRENDA team
additional information
-
distribution in tissues and organs; nearly all mammalian tissues and body fluids
Manually annotated by BRENDA team
additional information
-
nearly all mammalian tissues and body fluids
Manually annotated by BRENDA team
additional information
Q6W7J7, -
activity during cell growth
Manually annotated by BRENDA team
additional information
-
beta-glucuronidase is a lysosomal enzyme that increases in the tissues of animals in response to xenobiotics entering the body
Manually annotated by BRENDA team
additional information
-
CT26/betaG cell, colon carcinoma CT26 cells expressing beta-G
Manually annotated by BRENDA team
additional information
-
activity during cell growth
-
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
activity in acrosome and in cytoplasmic droplets. Activity in round spermatids is detected in acrosomal vesicles, activity in elongated spermatids is detected in sickle-shaped acrosome
-
Manually annotated by BRENDA team
-
activity in acrosome and in cytoplasmic droplets
Manually annotated by BRENDA team
-
the beta-glucuronidase forms a complex with esterase 22 in the liver. Gus colocalizes with Es22 at the endoplasmic reticulum but does not affect its RE hydrolase activity
Manually annotated by BRENDA team
-
wild-type enzyme
-
Manually annotated by BRENDA team
-
digestive juice, composition of the digestive juice containing enzyme and phytoestrogen compounds, overview
-
Manually annotated by BRENDA team
-
recombinant enzyme in BHK cells
Manually annotated by BRENDA team
B0FN51
beta-glucuronidase is present in every compartment of the digestive cell endo-lysosomal compartment and appears to be not necessarily membrane-bound. Enzyme is released to the digestive alveolar lumen in secretory lysosomes produced by basophilic cells and endocytosed by digestive cells
Manually annotated by BRENDA team
additional information
-
subcellular distribution
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670)
Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670)
Acidobacterium capsulatum (strain ATCC 51196 / DSM 11244 / JCM 7670)
Clostridium perfringens (strain 13 / Type A)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Escherichia coli (strain K12)
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
Streptococcus agalactiae serotype V (strain ATCC BAA-611 / 2603 V/R)
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
55000
-
-
gel filtration
66800
-
Q97UI1
-
70000
-
-
gel filtration, SDS-PAGE
71000
-
-
gel filtration
113500
-
-
sedimentation equilibrium centrifugation of form I
130000
-
-
gel filtration, beta-glucuronidase acting on chondroitin
140000
-
-
isozymes I and II, gel filtration
160000
-
-
SDS-PAGE
180000
-
-
-
200000
220000
-
gel filtration
230000
-
-
gel filtration
250000
310000
-
gel filtration
250000
310000
-
gel filtration
250000
310000
-
gel filtration
250000
310000
-
Littorina littorea, gel filtration
250000
310000
-
gel filtration; sedimention equilibrium centrifugation
250000
310000
-
mouse, gel filtration
250000
310000
-
sedimentation equilibrium centrifugation
250000
310000
-
gel electrophoresis
250000
310000
-
mouse, gel filtration
250000
310000
-
sedimentation equilibrium centrifugation
250000
310000
-
gradient polyacrylamide electrophoresis
250000
310000
-
gel electrophoresis; sedimentation equilibrium centrifugation
250000
310000
-
rabbit, sucrose density gradient centrifugation
280000
300000
-
gel filtration, beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide
290000
-
-
gel filtration
300000
-
-
SDS-PAGE
390000
-
-
wild-type enzyme, gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 75000, SDS-PAGE, beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide
?
Q9LRC8, -
x * 55000, SDS-PAGE
?
-
x * 78000, SDS-PAGE
?
Q9X0F2
x * 66000, recombinant His6-tagged enzyme, SDS-PAGE
?
-
x * 58400, SDS-PAGE
?
-
x * 56682, calculated, mature protein, x * 85700, SDS-PAGE
?
-, Q7SFB0
x * 58123, calculated, mature protein, x * 90100, SDS-PAGE
?
-
x * 71000, recombinant enzyme, SDS-PAGE
?
Lactobacillus brevis RO1
-
x * 71000, recombinant enzyme, SDS-PAGE
-
?
Scutellaria baicalensis Georgi
-
x * 55000, SDS-PAGE
-
dimer
-
2 * 79000, intracellular human beta-glucuronidase in transfected BHK cells, SDS-PAGE
dimer
-
2 * 67000, isozymes I and II, SDS-PAGE
dimer
-
2 * 90000
dimer
Streptococcus sp. LJ-22
-
2 * 67000, isozymes I and II, SDS-PAGE
-
homotetramer
-
4 * 75000, SDS-PAGE
monomer
-
1 * 68000, SDS-PAGE
tetramer
-
4 * 70000-80000, man, 2 identical 2 non-identical chains; SDS-PAGE
tetramer
-
SDS-PAGE
tetramer
-
mouse, SDS-PAGE
tetramer
-
rat, SDS-PAGE
tetramer
-
4 * 83000, the enzyme consists of two disulfide-linked dimers, wild-type enzyme and secreted recombinant enzyme, SDS-PAGE
tetramer
-
4 * 72000, SDS-PAGE
tetramer
-
4 * 55000, SDS-PAGE
tetramer
Escherichia coli HGU-3
-
4 * 72000, SDS-PAGE
-
tetramer
Scutellaria baicalensis Georg, Scutellaria baicalensis Georgi
-
4 * 55000, SDS-PAGE
-
monomer
-
1 * 55000, SDS-PAGE
additional information
-
the enzyme is composed of three components of 18000, 64000 and 80000 Da
additional information
-
beta-glucuronidase acting on chondroitin yields several protein bands on SDS-PAGE, no protein band with a MW of 75000 Da
additional information
Q2PBR7
domain organization, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
glycoprotein
-
sequence contains 12 putative glycosylation sites. Treatment with endoglycanase F reduces the molecular mass to 55000 Da
proteolytic modification
-
sequence contains a putative signal sequence, calculated molecular mass of immature protein is 58859
glycoprotein
-
-
glycoprotein
-
carbohydrate composition
glycoprotein
-
-
glycoprotein
-
glycosylated at Asn173 and Asn420 with high mannose-type oligosaccharides
phosphoprotein
-
both the placental 80000 Da and 64000 Da peptides, though not the 18000 Da one, are apparently phosphorylated, whereas the enzyme of leukemic cells is poorly phosphorylated
proteolytic modification
-
human beta-glucuronidase remains intracellular in BHK cells after synthesis undergoes a proteolytic processing event, i.e. a reduction in mass of 3000-4000 Da
proteolytic modification
-
the 80000 Da form is a protein from which a 22000 amino-acid-N-terminal signal peptide has been removed. A second cleavage occurs between the 159th and 160th amino acid to produce the 64000 Da and 18000 Da polypeptides. Thus the 18000 Da polypeptide of 137 amino acids represents the N-terminal part of the 80000 Da precursor
glycoprotein
-
-
glycoprotein
-, Q7SFB0
sequence contains 12 putative glycosylation sites
proteolytic modification
-, Q7SFB0
sequence contains a putative signal sequence, calculated molecular mass of immature protein is 60235
glycoprotein
-
oligosaccharide structure
glycoprotein
-
-
glycoprotein
-
carbohydrate composition
glycoprotein
-
analysis by hydrazinolysis and labeling, 80% N-glycosylation, analysis of oligosaccharides components of the microsomal enzyme, mainly branched bi- and triantennary complex type glycans, 20% O-glycosylation with major species being Galbeta(1,3)GalNAc, detailed overview
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
3D model shows catalytic resiudes E396, E508, and Y471in loop regions
Q9AFA2
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
1
7
-
stable
2
9
-
4C, 24 h, stable
4
11
-
-
4.2
7
-
form III
4.5
9
-
37C, 3 h, stable
5
7
-
form I
5
8
-
80 min, purified recombinant enzyme, 37C, completely stable
5
-
-
inactivation
5.4
7
-
form II
6
9
-, Q7SFB0
stable
6.5
-
-
inactivation
7
-
-
or 7.8, stable at, depending on buffer
8
-
-
stable at
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
-20
-
-
inactivation
37
-
-
presence of oestrone-3-glucuronide, 45 min
37
-
-
80 min, purified recombinant enzyme, pH 5.0-8.0, completely stable
37
-
-
enzyme encapsulated in biomimetic alginate/protamine/silica capsules, no loss of activity after 11 days, 90% remaining activity after 26 days
40
-
-
10 min
50
-
-
more stable in neutral buffers
50
-
-
depending on buffer
50
-
-
inactivation above
50
-
-
30 min, 50% loss of activity
50
-
Q7SFB0
30 min, 50% loss of activity
50
-
-
purified recombinant enzyme, half-life is over 2 h
55
-
-
denaturation above
55
-
-
depending on pH, substrate protects against inactivation
55
-
-
30 min, form I: inactivation, form II: stable
55
-
-
10 min, inactivation at pH 5.0, not at pH 7.0
60
-
-
form I: 60 min, form II: 5 min
60
-
-
pH 4.6, 20 min, stable
60
-
-
purified recombinant enzyme, half-life is 1 h
65
-
-
retains 90% of initial activity after 3 h at 65C
65
-
Q97UI1
4.5 d, 1.1% loss of activity
68
-
-
pH 6, stable for up to 3 h
68
-
-
pH 7.5, 75 mM NaCL and 5 mg/ml bovine serum albumin, 2 h: less than 40% inactivation of wild-type enzyme, mutant enzyme Y504A is as stable as the wild-type enzyme, mutant enzyme E540A is inactivated at a faster rate than the wild-type enzyme, mutant enzyme E541A is completely inactivated within 30 min
70
-
-
absence of substrate, 10 min, inactivation
70
-
-
stable at
70
-
-
lysosomal form: 60 min, 80% activity, plasma enzyme: 15 min, 0% activity
70
-
-
30 min, stable up to
70
-
-
the wild type enzyme loses its activity completely after 10 min at 70C
70
-
Q97UI1
10 h, enzyme retains full activity
71
-
-
30 min, pH 5.0, 80% activity, 30 min, pH 8.0, 20% activity
75
-
-
pH 4.6, 20 min, complete inactivation
80
-
-
inactivation
80
-
Q97UI1
10 h, enzyme retains full activity
85
-
Q9X0F2
recombinant His6-tagged enzyme, half-life is 3 h
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
freezing, inactivation due to dissociation
-
freezing/thawing, no inactivation
-
the enzyme acting on chondroitin is less stable than enzyme acting on p-nitrophenylphosphate
-
bovine serum albumin, stabilization
-
sodium acetate buffer, inactivation
-
ORGANIC SOLVENT
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
effect of solvents on soluble and immobilized enzyme
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-20C, form I: unstable, form II: 6 months, both forms stable in whole flies
-
4C, immobilized enzyme, 1 year, 40% activity
-
4C, at least 1 month
-
-20C or 4C, 0.02 M sodium acetate buffer, pH 5.2, 0.15 M NaCl, 1 mg/ml protein, several months, sucrose prevents aggregation
-
-20C, enzyme acting on chondroitin retains high level of activity for at least 1 month
-
-20C, neutral pH, 50% glycerol
-
0-4C, Tris-HCl buffer, pH 8.0, more than 1 month
-
4C, 2 weeks, 90% activity, or -20C, 50% glycerol
-
-20C, 10 mM NaH2PO4/Na2HPO4, 1 mM 2-mercaptoethanol, pH 7.0, 50% glycerol, more than two months with loss of activity of 10-20%
-
4C, 10 mM NaH2PO4/Na2HPO4, 1 mM 2-mercaptoethanol, pH 7.0, complete loss of activity after 2 weeks
-
-20C, 50% glycerol, at least 2 months
-
0C, 0.2 M potassium phosphate buffer, pH 8.0, 3 days, unstable at -20C or 4C or in sodium acetate buffer pH 4.0
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
lactamyl-Sepharose column chromatography
-
2 forms, partial
-
nickel chelate affinity chromatography
-
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography to homogeneity
-
native enzyme from digestive juice by ion exchange chromatography on a resin containing a polymeric sorbent
-
Blue Sepharose FF column chromatography, phenyl-Sepharose high-Sub FF column chromatography, DEAE-Sephacel column chromatography
-
recombinant GUS from Escherichia coli strain GMS407
-
DEAE Sepharose Fast Flow column chromatography and polyethyleneimine gel filtration
-
2 different exo-beta-glucuronidases: a beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide and a beta-glucuronidase acting on chondroitin
-
native enzyme from eggs, by ammonium sulfate fractionation, anion exchange chromatography, and heparin affinity chromatography
-
from liver microsomes by calcium precipitation, immunoaffinity chromatography, preparative PAGE, gel filtration, and anion exchange chromatography to homogeneity
-
native enzyme 7.2fold from roots, by ammonium sulfate fractionation and anion exchange chromatography to homogeneity
-
partial
-
native isozymes I and II to homogeneity by ammonium sulfate fractionation, hydrophobic interaction, ion exchange, and hydroxyapatite chromatographies, and glycyrrhizin affinity chromatography
-
recombinant His6-tagged enzyme from Escherichia coli strain GMS407 by metal affinity chromatography to homogeneity
Q9X0F2
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in transgenic Arabidopsis
-
expression in Pichia pastoris
-
expressed in 3T3 fibroblasts and EJ carcinoma cells
-
expressed in Escherichia coli DH5alpha cells
-
gene gusA, expression of His-tagged wild-type and mutant enzymes in Escherichia coli
-
mutants expressed in Escherichia coli DH5alpha cells
-
over-expressed in wheat plants
-
recombinant expression of His-tagged GusA in Escherichia coli strain TOP10 and BL21, stable expression of GusA in Gardia lamblia strain WB C6 trophozoites, under control of the promoter from the glutamate dehydrogenase, gdh, gene, for establishing a system to test enzyme susceptibility to the anti-giardial drugs nitazoxanide and metronidazole, overview
-
expressed in 3T3 fibroblasts and EJ carcinoma cells
-
expression vectors pMCG-GLUC and pMCG-dGLUC containing cDNA coding for human beta-glucuronidase and a C-terminal-truncated form of beta-glucuronidase respectively are transfected into BHK cells. The stable clones B702 expressing wild-type and B688 expressing mutant beta-glucuronidase. In the mutant enzyme a stop codon is introduced after the CAC/His-637 codon, thereby eliminating 14 amino acids from the C-terminus
-
wild-type and mutant enzymes expressed COS cells and GUSB-deficient fibroblasts from the SV40 late promoter in vector pJC119
-
GUS, DNA and amino acid sequence determination, analysis and comparison, overexpression of the His-tagged enzyme in Escherichia coli strain GMS407
-
expressed in Escherichia coli
Q9AHJ8
GusA is expressed from the cloned gusA gene by a constitutive promoter in Lactobacillus gasseri ATCC 33323 and by a regulated promoter in Escherichia coli
-, Q9AHJ8
expressed in Escherichia coli
-
expressed in 3T3 fibroblasts and EJ carcinoma cells
-
expression of red fluorescent protein, RFP, fusion Gus in COS-7 cells, coexpression with GFP-tagged esterase 22
-
expression in Pichia pastoris
-, Q7SFB0
expressed in Escherichia coli strain JM109
-
beta-D-glucuronidase gene derived from Penicillium purpurogenum Li-3 is expressed in Pichia pastoris GS115 in two different environments of low-shear modeled microgravity (LSMMG) and normal gravity (NG)
A7XS03, -
gene uidA, DNA and amino acid sequence determination and analysis, genetic organization, expression analysis, expression in Escherichia coli strain TG1 mutant with inactivated endogenous enzyme activity, complementation of enzyme-deficient Escherichia coli strain
Q6W7J7, -
expression in Escherichia coli, sGUS does not belong to the family 2 beta-glucuronidases, sGUS and heparanase belong to the same family
Q9LRC8, -
expressed in Escherichia coli strain Origami B(DE3)
-
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree
Q2PBR7
expression in Escherichia coli. Although Escherichia coli possesses an endogenous beta-glucuronidase activity, a short treatment at 80C of the crude extract causes the precipitation of most Escherichia coli protein, resulting in an enrichment of the Sulfolobus beta-glucuronidase
Q97UI1
gene TM1062, DNA and amino acid sequence determination and analysis, expression of His6-tagged enzyme in Escherichia coli strain GMS407
Q9X0F2
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression confined to the vascular system of cotyledon, in small developing leaves expression in leaf trichomes, beginning expression in veins of distal part of the lamina with leaves becoming larger, in mature flowering plants grwon on pot soil expression in vascular tissue of leaves, green sepals and siliques
-
enhanced expression when grown on agar plates supplemented with 4% sucrose under high light growth conditions
-
beta-glucuronidase is a lysosomal enzyme that increases in the tissues of animals in response to xenobiotics entering the body
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
mut-1
-
base-substituted mutant, less induction of enzyme activity
mut-1
Agrobacterium sp. GV3101
-
base-substituted mutant, less induction of enzyme activity
-
D531E/S557V/N566S/G601S
-
saturation mutagenesis, mutant 1.13, altered substrate specificity compared to the wild-type enzyme
Q493R/T509A/M532T/N550S/G559S/N566S
-
mutant showing improved thermostability retaining 75% of its activity when heated at 80C for 10 min
S193N/G466A/Q951R
-
212% increased activity compared to the wild type enzyme
S193N/T266A/Q267R/Q626R
-
167% increased activity compared to the wild type enzyme
S193N/V411A/D448G
-
172% increased activity compared to the wild type enzyme
S22N/G81S/K257E/T509A/S557P/N566S/K568Q/Q598R/stop604W
-
saturation mutagenesis, mutant 1.15, altered substrate specificity compared to the wild-type enzyme
S557I/N566A/K568R/A580V
-
saturation mutagenesis, mutant 1.16, altered substrate specificity compared to the wild-type enzyme
S557Q/N566K/K568S/Q598stop
-
saturation mutagenesis, mutant 1.2, altered substrate specificity compared to the wild-type enzyme
T266A/Q267R/Q626R
-
137% increased activity compared to the wild type enzyme
V473A/S557P/N566S/K568Q
-
saturation mutagenesis, mutant 4.7, altered substrate specificity compared to the wild-type enzyme
L527I/M543I
Escherichia coli K12
-
158% increased activity compared to the wild type enzyme
-
S193N/G466A/Q951R
Escherichia coli K12
-
212% increased activity compared to the wild type enzyme
-
S193N/T266A/Q267R/Q626R
Escherichia coli K12
-
167% increased activity compared to the wild type enzyme
-
S193N/V411A/D448G
Escherichia coli K12
-
172% increased activity compared to the wild type enzyme
-
T266A/Q267R/Q626R
Escherichia coli K12
-
137% increased activity compared to the wild type enzyme
-
D207A
-
4.9% of the wild-type activity is expressed in COS cells
E451A
-
0.6% of the wild-type activity is expressed in COS cells, tetrameric enzyme, ratio of turnover number to KM-value is decreased 9100fold as compared to wild-type enzyme. Mutant enzyme E541A is inactivated at a faster rate than the wild-type enzyme, and is completely inactivated within 30 min. 50 mM azide causes 70% loss of activity of wild-type enzyme and mutant enzyme E451A. 50 mM-0.5 M stimulates mutant enzyme E451A. 1 mM inhibits wild-type enzyme and mutant enzyme E451A
E451Q
-
5.9% of the wild-type activity is expressed in COS cells
E515A
-
no activity is expressed in COS cells
E540A
-
no activity is expressed in COS cells, tetrameric enzyme, ratio of turnover number to KM-value is decreased 33000 fold as compared to wild-type enzyme, optimal pH is 5.0 instead of 4.5 for the wild-type enzyme. Mutant enzyme is inactivated at a faster rate than the wild-type enzyme at 68C
E540D
-
no activity is expressed in COS cells
Y504A
-
1.4% of the wild-type activity is expressed in COS cells, tetrameric enzyme, the ratio of turnover number to KM-value is decreased 830fold as compared to wild-type enzyme. Mutant enzyme is as stable as the wild-type enzyme at 68C
Y504F
-
2.3% of the wild-type activity is expressed in COS cells
Y504H
-
0.6% of the wild-type activity is expressed in COS cells
Y508A
-
no activity is expressed in COS cells
D524G
Q9AHJ8
mutant shows increased activity in neutral pH ranges
D573A
Q9AHJ8
mutant shows increased activity in neutral pH ranges
D524G
Lactobacillus gasseri ATCC33323
-
mutant shows increased activity in neutral pH ranges
-
D573A
Lactobacillus gasseri ATCC33323
-
mutant shows increased activity in neutral pH ranges
-
E194A
Q9LRC8, -
beta-glucuronidase activity is 86% of the wild-type activity
E212A
Q9LRC8, -
beta-glucuronidase activity is 1.2% of the wild-type activity. The ratio of turnover number to KM-value is 0.025% of the wild-type ratio
E225A
Q9LRC8, -
beta-glucuronidase activity is 94% of the wild-type activity
E272A
Q9LRC8, -
beta-glucuronidase activity is 70% of the wild-type activity
E329A
Q9LRC8, -
beta-glucuronidase activity is 0.3% of the wild-type activity. The ratio of turnover number to KM-value is 0.008% of the wild-type ratio
Y281A
Q9LRC8, -
the ratio of turnover number to KM-value is 0.025% of the wild-type ratio
E194A
Scutellaria baicalensis Georgi
-
beta-glucuronidase activity is 86% of the wild-type activity
-
E212A
Scutellaria baicalensis Georgi
-
beta-glucuronidase activity is 1.2% of the wild-type activity. The ratio of turnover number to KM-value is 0.025% of the wild-type ratio
-
E225A
Scutellaria baicalensis Georgi
-
beta-glucuronidase activity is 94% of the wild-type activity
-
E272A
Scutellaria baicalensis Georgi
-
beta-glucuronidase activity is 70% of the wild-type activity
-
Y281A
Scutellaria baicalensis Georgi
-
the ratio of turnover number to KM-value is 0.025% of the wild-type ratio
-
E383A
Q9X0F2
site-directed mutagenesis, the mutant enzyme shows reduced activity and similar thermal stability at 85C compared to the wild-type enzyme
E383Q
Q9X0F2
site-directed mutagenesis, the mutant enzyme shows reduced activity and thermal stability at 85C compared to the wild-type enzyme
E476A
Q9X0F2
site-directed mutagenesis, the mutant enzyme shows increased thermal stability at 85C compared to the wild-type enzyme
additional information
-
fusion gene of beta-glucuronidase with promoter gene of 9-cis-epoxycarotenoid dioxygenase, EC 1.13.11.51
mut-2
-
base-substituted mutant, less induction of enzyme activity
additional information
Agrobacterium sp. GV3101
-
fusion gene of beta-glucuronidase with promoter gene of 9-cis-epoxycarotenoid dioxygenase, EC 1.13.11.51
-
mut-2
Agrobacterium sp. GV3101
-
base-substituted mutant, less induction of enzyme activity
-
additional information
-
arabinogalactan protein isloated from a GUS2 knock-out insertion line shows higher glucuronic acid content than wild-type. A transgenic line overexpressing the gene shows markedly lower glucuronic acid content in arabinogalactan proteins and displays increased hipocotyl and root lengths, while the knock-out line displays reduced hipocotyl and root lengths compared with wild-type
L527I/M543I
-
158% increased activity compared to the wild type enzyme
additional information
-
the enzyme is engineered as fusion with an N-terminal 76 amino acid ubiquitin-coding region. When translated in any eukaryotic cell, such ubiquitin fusions are cleaved by ubiqitin-specific proteases specifically after the C-terminus of ubiquitin, irrespective of the distal amino acid (with the exception of Pro), releasing the downstream protein with the specified amino terminus. The presence of an N-terminal uncleavable ubiquitin on GUS does not reduce activity. A version of GUS with phenylalanine at the mature N-terminus accumulates a minimum of 3fold lower than GUS with methionine at its mature N-terminus
additional information
-
rapid evolution of beta-glucuronidase specificity by saturation mutagenesis of an active site loop, DNA shuffling of point mutations, construction of diverse mutants with mutation of residues 557, 566, and 568, the mutants show increased activity with beta-D-xylopyranoside and reduced activity with beta-D-glucuronide, overview
additional information
-
encapsulation of the enzyme in biomimetic alginate/protamine/silica capsules increases the enzyme storage, recycling, pH and thermostability compared to free enzyme, overview. No appreciable loss in activity during 10 repeated reaction cycles
E540Q
-
0.3% of the wild-type activity is expressed in COS cells
additional information
-
in the mutant enzyme a stop codon is introduced after the CAC/His-637 codon, thereby eliminating 14 amino acids from the C-terminus. Thereby the last Cys at position 644 is eliminated. In the mutant, covalent linkage between two monomers is no longer observed, indicating that Cys44 is involved in intermolecular disulfide-bond formation
Renatured/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
reporter enzyme which is used for studies in higher plants because endogenous activities are low and sensitive assays are available. A version of GUS with phenylalanine at the mature N-terminus accumulates a minimum of 3fold lower than GUS with methionine at its mature N-terminus. This altered protein can be useful for promoter studies which require more rapid changes in the accumulation of the reporter protein
analysis
-
assay for beta-glucuronidase is able to distinguish Escherichia coli from other Escherichia species
analysis
-
enzymatic assay adapted to study the fate of fecal coliforms in survival experiments, and appears to be rapid and efficient way to estimate the microbiological quality of surface waters. The major advantage of the enzymtic assay is the very short time response, and thus this method offers a powerful, rapid, and efficient way to estimate the microbiological quality of bathing and fishing areas, and to monitor disinfection efficiencies
analysis
-
precise and reliable detection of Escherichia coli strains for differentiation from biochemically and ohylogenetically related bacteria. Method is based on polymerase chain reaction, in which four genes coding for lactose permease, cytochrome bd complex, beta-D-glucuronidase, and beta-D-galactosidase, serve as target DNA sequences
analysis
-
comparison of commercially available kits to assess water quality and evaluation of their ability to detect Escherichia coli. Chromocult, MI agar, Readycult, and Colilert detect beta-glucuronidase production from respectively 79.9, 79.9, 81.1, and 51.4% of the 74 Escherichia coli strains tested. These four methods detect beta-galactosidase production from respectively 85.1, 73.8, 84.1, and 84.1% of the total coliform strains tested. The high level of false-negative results for Escherichia coli recognition obtained by all four methods suggests that they may not be appropriate for identification of presumptive Escherichia coli strains
analysis
-
comparison of commercially available kits used for the simultaneous detection of coliforms and Escherichia coli from water. Membrane lactose glucuronide agar, Colilert-18, MI agar, Colitag and Chromocult agar to detect beta-D-glucuronidase activity are tested with over 1000 isolates of Escherichia coli recovered from naturally contaminated water samples. Four of the media give very similar results but membrane lactose glucuronide agar fails to detect glucuronidase activity in 15.6% of the cultures tested
biotechnology
P05804
comparison of Escherichia coli and Staphylococcus sp. RLH1 beta-glucuronidase as gene fusion markers in plant transformation experiments. The Staphylococcus enzyme shows higher catalytic activity and increased accessible surface area of active site residues compared with the Escherichia coli protein
drug development
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stable expression of GusA in Gardia lamblia strain WB C6 for establishing a system to test enzyme susceptibility to the anti-giardial drugs nitazoxanide and metronidazole, overview
medicine
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the potent beta-glucuronidase activity caused by the glucuronic acid conjugates from xenobiotics and endogenous compounds is a prime factor in the etiology of colon cancer
medicine
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when beta-glucuronidase producing bacteria infect the bile, the pH of the bile becomes raised, the high pH and bile induce the enzyme, and then bilirubin gallstones can be easily formed
molecular biology
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stable expression of GusA in Gardia lamblia strain WB C6 for establishing a system to test enzyme susceptibility to the anti-giardial drugs nitazoxanide and metronidazole, overview
molecular biology
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beta-glucuronidase is the most frequent reporter gene in plants. Beta-glucuronidase enzyme activity is not only tissue-specific but also genotype-dependent
medicine
Escherichia coli HGU-3
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when beta-glucuronidase producing bacteria infect the bile, the pH of the bile becomes raised, the high pH and bile induce the enzyme, and then bilirubin gallstones can be easily formed
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analysis
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the enzyme is useful in analysis of phytoestrogens and related compounds in human biofluids, e.g. urine
diagnostics
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the enzyme is useful in analysis of phytoestrogens and related compounds in human biofluids, e.g. urine
diagnostics
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beta-glucuronidase activity is a sensitive biomarker to assess low-level organophosphorus insecticide exposure, e.g. plasma BG activity for low-level organophosphorus-exposure compared to BChE activity, overview
medicine
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a high varability in the expression of beta-Glc in human liver and kidney. Therefore cleavage of drug glucuronides that accumulate during chronic therapy or are used as prodrugs can show a wide interindividual variability in humans, which might result in variable response to drugs
medicine
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measurement of beta-glucuronidase activity has no additive clinical value following a parathion overdose in humans
nutrition
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crossover feeding trial in healthy women and men with a diet high in selected citrus fruit, crucifers and soy and a diet devoid of fruits, vegetables, and soy. Participants of the fruit and soy diet display a signifcantly higher beta-glucuronidase activity than those with the basal diet, where the enzyme activity decreased during the diet. Response to the diet does not differ by sex
toxicology
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measurement of beta-glucuronidase activity has no additive clinical value following a parathion overdose in humans
analysis
B0FN51
in environmental toxicology, techniques used to visualise lysosomes in order to determine their responses to pollutants are the lysosomal structural changes test and the lysosomal membrane stability test are based on the histochemical application of lysosomal marker enzymes. In mussel digestive cells, the marker enzymes used are beta-glucuronidase and hexosaminidase. beta-Glucuronidase, but not hexosaminindase, histochemistry provides an appropriate marker for the lysosomal structural changes test and that, although both lysosomal marker enzymes can be employed in the lysosomal membrane stability test, different values would be obtained depending on the marker enzyme employed
toxicology
B0FN51
in environmental toxicology, techniques used to visualise lysosomes in order to determine their responses to pollutants are the lysosomal structural changes test and the lysosomal membrane stability test are based on the histochemical application of lysosomal marker enzymes. In mussel digestive cells, the marker enzymes used are beta-glucuronidase and hexosaminidase. beta-Glucuronidase, but not hexosaminindase, histochemistry provides an appropriate marker for the lysosomal structural changes test and that, although both lysosomal marker enzymes can be employed in the lysosomal membrane stability test, different values would be obtained depending on the marker enzyme employed
medicine
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after liver injury induced by ontraperitoneal injections of N-nitrosodimethylamine, a significant increase is observed in beta-glucuronidase levels in the serum, liver homogenate, and subcellular fractions, but not in the nuclear fraction, concomitant with a maximum lysosomal fragility on day 21 during the induced fibrosis
biotechnology
Q9AFA2
comparison of Escherichia coli and Staphylococcus sp. RLH1 beta-glucuronidase as gene fusion markers in plant transformation experiments. The Staphylococcus enzyme shows higher catalytic activity and increased accessible surface area of active site residues compared with the Escherichia coli protein
biotechnology
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comparison of Escherichia coli and Staphylococcus sp. RLH1 beta-glucuronidase as gene fusion markers in plant transformation experiments. The Staphylococcus enzyme shows higher catalytic activity and increased accessible surface area of active site residues compared with the Escherichia coli protein
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analysis
Q97UI1
Sulfolobus gene can be used as reporter in any thermophilic microorganism lacking an endogenous beta-glucuronidase activity
analysis
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Sulfolobus gene can be used as reporter in any thermophilic microorganism lacking an endogenous beta-glucuronidase activity
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