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Information on EC 3.2.1.31 - beta-glucuronidase
for references in articles please use BRENDA:EC3.2.1.31
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EC Tree 3 Hydrolases
3.2 Glycosylases
3.2.1 Glycosidases, i.e. enzymes that hydrolyse O- and S-glycosyl compounds
3.2.1.31 beta-glucuronidase
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
- 3.2.1.31
- lysosomal
- urine
- urinary
- neutrophil
- bile
- leukocyte
- granule
- lysozyme
-
polymorphonuclear
- hydrolases
-
protoplasts
- mucopolysaccharidosis
- agrobacterium
- cathepsins
-
cytochemical
- biliary
- tumefaciens
- cauliflower
-
n-acetyl-beta-d-glucosaminidase
- beta-n-acetylglucosaminidase
- alpha-mannosidase
-
degranulation
- glycosaminoglycans
-
sulfatase
-
glucuronic
-
azurophilic
- beta-hexosaminidase
- nitroreductase
- nptii
- hygromycin
- zymosan
- alpha-galactosidase
-
bombard
-
calli
- glycosidases
-
agrobacterium-mediated
-
deconjugation
- neomycin
-
unconjugated
- beta-d-galactosidase
- arylsulphatase
- fmlp
- diagnostics
- alpha-l-fucosidase
- synthesis
-
coliforms
- medicine
- biotechnology
-
alpha-naphthyl
- toxicology
- pomatia
- analysis
- hexosaminidase
-
crevicular
- 1,2-dimethylhydrazine
- drug development
- nutrition
- molecular biology
- alpha-l-iduronidase
showSynonyms
beta-glucuronidase, beta-d-glucuronidase, betag, beta-gluc, beta-glucuronidase a, hgusb, exo-beta-glucuronidase, tmgusi, exo-beta-d-glucuronidase, ketodase, more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
B-GUS
beta-D-glucuronidase
Beta-D-glucuronoside glucuronosohydrolase
-
-
-
-
Beta-G1
-
-
-
-
beta-glucuronidase
betaG
BfGUS
exo-beta-D-glucuronidase
-
-
-
-
FAEPRAA2165_01145
GlcAase
glucuronidase, beta-glucuronide glucuronohydrolase
-
-
-
-
GUS
GusA
GusB
ketodase
-
-
-
-
lacZ
PGUS
TM1062
UidA
additional information
beta-glucuronidase
-
fusion product with stachyose synthetase, EC 2.4.1.67
GUS
-
-
-
-
additional information
-
the enzyme belongs to glycosyl hydrolase family 2 with three conserved domains
additional information
-
the enzyme belongs to glycosyl hydrolase family 2 with three conserved domains
-
additional information
the enzyme belongs to the glycosyl hydrolases family 2
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a beta-D-glucuronoside + H2O = D-glucuronate + an alcohol
-
-
-
-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
-
-
exoglycosidic
-
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PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
MetaCyc
beta-D-glucuronide and D-glucuronate degradation, luteolin triglucuronide degradation
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SYSTEMATIC NAME
IUBMB Comments
beta-D-glucuronoside glucuronosohydrolase
-
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CAS REGISTRY NUMBER
COMMENTARY
9001-45-0
-
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(1S)-1-(chloromethyl)-3-([5-[2-(dimethylamino)ethoxy]-1H-indol-2-yl]carbonyl)-2,3-dihydro-1H-benzo[e]indol-5-yl beta-D-glucopyranosiduronic acid + H2O
D-glucuronate + [(1S)-1-(chloromethyl)-5-hydroxy-1,2-dihydro-3H-benzo[e]indol-3-yl][5-[2-(dimethylamino)ethoxy]-1H-indol-2-yl]methanone
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Substrates: -
Products: -
Products: -
?
(1S,3S)-3,12-dihydroxy-3-(hydroxyacetyl)-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 2,3,6-trideoxy-3-{[({2-[({[4-(beta-D-glucopyranuronosyloxy)-3-nitrobenzyl]oxy}carbonyl)amino]-5-({[(2-{[4-({[(pyridin-3-ylmethoxy)carbonyl]amino}methyl)benzoyl]amino}phenyl)carbamoyl]oxy}methyl)benzyl}oxy)carbonyl]amino}-alpha-D-lyxo-hexopyranoside + H2O
D-glucuronate + (1S,3S)-3,12-dihydroxy-3-(hydroxyacetyl)-10-methoxy-6,11-dioxo-1,2,3,4,6,11-hexahydrotetracen-1-yl 2,3,6-trideoxy-3-[({[2-({[(4-hydroxy-3-nitrobenzyl)oxy]carbonyl}amino)-5-({[(2-{[4-({[(pyridin-3-ylmethoxy)carbonyl]amino}methyl)benzoyl]amino}phenyl)carbamoyl]oxy}methyl)benzyl]oxy}carbonyl)amino]-alpha-D-lyxo-hexopyranoside
-
Substrates: -
Products: -
Products: -
?
(4GlcAbeta1-3GalNAc(4-OSO3-)beta1-)2 + H2O
D-glucuronate + ?
-
Substrates: 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
Products: -
Products: -
?
(4GlcAbeta1-3GalNAc(4-OSO3-)beta1-)3 + H2O
D-glucuronate + ?
-
Substrates: 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
Products: -
Products: -
?
(4GlcAbeta1-3GalNAc(6-OSO3-)beta1-)2 + H2O
D-glucuronate + ?
-
Substrates: 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
Products: -
Products: -
?
(4GlcAbeta1-3GalNAc(6-OSO3-)beta1-)3 + H2O
D-glucuronate + ?
-
Substrates: 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
Products: -
Products: -
?
(4GlcAbeta1-3GalNAcbeta1-)2 + H2O
D-glucuronate + ?
-
Substrates: 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
Products: -
Products: -
?
(4GlcAbeta1-3GalNAcbeta1-)3 + H2O
D-glucuronate + ?
-
Substrates: 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
Products: -
Products: -
?
(4GlcAbeta1-3GlcNAcbeta1-)3 + H2O
D-glucuronate + ?
-
Substrates: 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
Products: -
Products: -
?
1-deoxy-1-(6-thiopurinyl)-beta-D-glucopyranoside + H2O
6-mercaptopurine + D-glucopyranose
-
Substrates: -
Products: -
Products: -
?
1-deoxy-1-(6-thiopurinyl)-beta-D-glucopyranosiduronamide + H2O
6-mercaptopurine + 1-deoxy-D-glucopyranosiduronamide
-
Substrates: -
Products: -
Products: -
?
1-O-([4-[(10R,11S)-10-([[(2alpha,5beta,7beta,13alpha)-4,10-bis(acetyloxy)-2-(benzoyloxy)-7-hydroxy-9-oxo-5,20-epoxytax-11-en-13-yl]oxy]carbonyl)-4-methyl-3,8,13-trioxo-11,13-diphenyl-2,7,9-trioxa-4,12-diazatridec-1-yl]phenyl]carbamoyl)-beta-D-glucuronate + H2O
D-glucuronate + [4-[(10R,11S)-10-[[((2alpha,5beta,7beta,13alpha)-4,10-bis(acetyloxy)-2-(benzoyloxy)-7-hydroxy-9-oxo-5,20-epoxytax-11-en-13-yl]oxy]carbonyl)-4-methyl-3,8,13-trioxo-11,13-diphenyl-2,7,9-trioxa-4,12-diazatridec-1-yl]phenyl]carbamic acid
-
Substrates: -
Products: -
Products: -
?
1-O-[(2-[[4-(acetylamino)benzoyl]amino]phenyl)carbamoyl]-beta-D-glucopyranuronic acid + H2O
D-glucuronate + (2-[[4-(acetylamino)benzoyl]amino]phenyl)carbamic acid
-
Substrates: -
Products: -
Products: -
?
1-O-[(4-[[([[(1S,2R)-1-(benzoylamino)-3-[[(2alpha,5beta,7beta,13alpha)-4,10-bis(acetyloxy)-2-(benzoyloxy)-7-hydroxy-9-oxo-5,20-epoxytax-11-en-13-yl]oxy]-3-oxo-1-phenylpropan-2-yl]oxy]carbonyl)oxy]methyl]phenyl)carbamoyl]-beta-D-glucopyranuronic acid + H2O
D-glucuronate + (4-[[([[(1S,2R)-1-(benzoylamino)-3-[[(2alpha,5beta,7beta,13alpha)-4,10-bis(acetyloxy)-2-(benzoyloxy)-7-hydroxy-9-oxo-5,20-epoxytax-11-en-13-yl]oxy]-3-oxo-1-phenylpropan-2-yl]oxy]carbonyl)oxy]methyl]phenyl)carbamic acid
-
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
2-amino-4-[(10R,11S)-10-([[(2alpha,5beta,7beta,13alpha)-4,10-bis(acetyloxy)-2-(benzoyloxy)-7-hydroxy-9-oxo-5,20-epoxytax-11-en-13-yl]oxy]carbonyl)-4,7-dimethyl-3,8,13-trioxo-11,13-diphenyl-2,9-dioxa-4,7,12-triazatridec-1-yl]phenyl beta-D-glucopyranosiduronate + H2O
D-glucuronate + (2alpha,5beta,7beta,13alpha)-4,10-bis(acetyloxy)-2-(benzoyloxy)-7-hydroxy-9-oxo-5,20-epoxytax-11-en-13-yl (10R)-1-(3-amino-4-hydroxyphenyl)-10-[(S)-(benzoylamino)(phenyl)methyl]-4,7-dimethyl-3,8-dioxo-2,9-dioxa-4,7-diazaundecan-11-oate
-
Substrates: -
Products: -
Products: -
?
2-amino-4-[(10R,11S)-10-([[(2alpha,5beta,7beta,13alpha)-4,10-bis(acetyloxy)-2-(benzoyloxy)-7-hydroxy-9-oxo-5,20-epoxytax-11-en-13-yl]oxy]carbonyl)-4-methyl-3,8,13-trioxo-11,13-diphenyl-2,7,9-trioxa-4,12-diazatridec-1-yl]phenyl beta-D-glucopyranosiduronic acid + H2O
D-glucuronate + (2alpha,5beta,7beta,13alpha)-4,10-bis(acetyloxy)-2-(benzoyloxy)-7-hydroxy-9-oxo-5,20-epoxytax-11-en-13-yl (10R)-1-(3-amino-4-hydroxyphenyl)-10-[(S)-(benzoylamino)(phenyl)methyl]-4-methyl-3,8-dioxo-2,7,9-trioxa-4-azaundecan-11-oate
-
Substrates: -
Products: -
Products: -
?
4-([[(2-[[4-(acetylamino)benzoyl]amino]phenyl)carbamoyl]oxy]methyl)-2-nitrophenyl beta-D-glucopyranosiduronic acid + H2O
D-glucuronate + 4-hydroxy-3-nitrobenzyl (2-[[4-(acetylamino)benzoyl]amino]phenyl)carbamate
-
Substrates: -
Products: -
Products: -
?
4-([[(4S)-4-ethyl-4-hydroxy-3,14-dioxo-3,4,12,14-tetrahydro-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinolin-9-yl]oxy]methyl)-2-nitrophenyl beta-D-glucopyranosiduronic acid + H2O
D-glucuronate + (4S)-4-ethyl-4-hydroxy-9-[(4-hydroxy-3-nitrobenzyl)oxy]-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinoline-3,14(4H,12H)-dione
-
Substrates: -
Products: -
Products: -
?
4-Me-beta-GlcA-(1-6)-beta-Gal-(1-6)-beta-Gal-(1-3)-Gal + H2O
?
-
Substrates: rate of hydrolysis is 106% of the with p-nitrophenyl-beta-D-glucuronide
Products: -
Products: -
?
4-Me-beta-GlcA-(1-6)-beta-Gal-(1-6)-Gal + H2O
?
-
Substrates: rate of hydrolysis is 117% of the with p-nitrophenyl-beta-D-glucuronide
Products: -
Products: -
?
4-Me-beta-GlcA-(1-6)-Gal + H2O
?
-
Substrates: rate of hydrolysis is 62% of the with p-nitrophenyl-beta-D-glucuronide
Products: -
Products: -
?
4-methylumbelliferyl beta-D-glucuronide + H2O
4-methylumbelliferone + beta-D-glucuronic acid
4-methylumbelliferyl-beta-D-glucuronic acid + H2O
4-methylumbelliferone + beta-D-glucuronic acid
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferol + beta-D-glucuronate
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferol + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
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
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
Substrates: preferred substrate
Products: -
Products: -
?
4-nitrophenyl D-glucuronide + H2O
4-nitrophenol + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
4-[(10R,11S)-10-([[(2alpha,5beta,7beta,13alpha)-4,10-bis(acetyloxy)-2-(benzoyloxy)-7-hydroxy-9-oxo-5,20-epoxytax-11-en-13-yl]oxy]carbonyl)-4-methyl-3,8,13-trioxo-11,13-diphenyl-2,7,9-trioxa-4,12-diazatridec-1-yl]-2-nitrophenyl beta-D-glucuronate + H2O
D-glucuronate + (2alpha,5beta,7beta,13alpha)-4,10-bis(acetyloxy)-2-(benzoyloxy)-7-hydroxy-9-oxo-5,20-epoxytax-11-en-13-yl (10R)-10-[(S)-(benzoylamino)(phenyl)methyl]-1-(4-hydroxy-3-nitrophenyl)-4-methyl-3,8-dioxo-2,7,9-trioxa-4-azaundecan-11-oate
-
Substrates: -
Products: -
Products: -
?
4-[([[(3b,22S,23R)-3-hydroxy-17,23-epoxyveratraman-28-yl]carbonyl]oxy)methyl]-2-nitrophenyl beta-D-glucopyranosiduronic acid + H2O
D-glucuronate + 4-hydroxy-3-nitrobenzyl (3b,22S,23R)-3-hydroxy-17,23-epoxyveratraman-28-carboxylate
-
Substrates: -
Products: -
Products: -
?
4-[([[(4S)-4-ethyl-4-hydroxy-3,14-dioxo-3,4,12,14-tetrahydro-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinolin-10-yl]carbamoyl]oxy)methyl]phenyl beta-D-glucopyranosiduronic acid + H2O
D-glucuronate + 4-hydroxybenzyl [(4S)-4-ethyl-4-hydroxy-3,14-dioxo-3,4,12,14-tetrahydro-1H-pyrano[3',4':6,7]indolizino[1,2-b]quinolin-10-yl]carbamate
-
Substrates: -
Products: -
Products: -
?
4-[2-[1-(2-[2-[2-(beta-D-glucopyranuronosyloxy)ethoxy]ethoxy]ethyl)-1H-1,2,3-triazol-4-yl]-1-([[(3b,22S,23R)-3-hydroxy-17,23-epoxyveratraman-28-yl]carbonyl]oxy)ethyl]-2-nitrophenyl beta-D-glucopyranosiduronic acid + H2O
D-glucuronate + 2-[2-(2-[4-[2-([[(3beta,22S,23R)-3-hydroxy-17,23-epoxyveratraman-28-yl]carbonyl]oxy)-2-(4-hydroxy-3-nitrophenyl)ethyl]-1H-1,2,3-triazol-1-yl]ethoxy)ethoxy]ethyl beta-D-glucopyranosiduronic acid
-
Substrates: -
Products: -
Products: -
?
5-bromo-4-chloro-3-indoyl-beta-D-glucuronide + H2O
5-bromo-4-chloro-1H-indol-3-ol + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
alpha-L-arabinosidase-treated-arabinogalactan-protein + H2O
?
-
Substrates: -
Products: -
Products: -
?
ammonium 1-deoxy-1-(6-thiopurinyl)-beta-D-glucopyranosidurate + H2O
6-mercaptopurine + ammonium 1-deoxy-(6-thiopurinyl)-beta-D-glucopyranosiduronate
-
Substrates: -
Products: -
Products: -
?
apigenin 7,4'-diglucuronide + H2O
apigenin 7-O-glucuronide + glucuronic acid
-
Substrates: -
Products: -
Products: -
?
beta-GlcA(1-6)beta-Gal(1-6)Gal + H2O
D-glucuronate + beta-Gal(1-6)Gal
Substrates: -
Products: 67.4% of the activity with 4-nitrophenyl beta-D-glucuronic acid
Products: 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
-
Substrates: -
Products: 94.6% of the activity with 4-nitrophenyl beta-D-glucuronic acid
Products: 94.6% of the activity with 4-nitrophenyl beta-D-glucuronic acid
?
beta-GlcA-(1-3)-Gal + H2O
?
-
Substrates: rate of hydrolysis is 2% of the with p-nitrophenyl-beta-D-glucuronide
Products: -
Products: -
?
beta-GlcA-(1-6)-beta-Gal-(1-6)-Gal + H2O
beta-Gal-(1-6)-Gal + beta-D-glucuronic acid
-
Substrates: rate of hydrolysis is 67% of the with p-nitrophenyl-beta-D-glucuronide
Products: -
Products: -
?
beta-GlcA-(1-6)-Gal + H2O
D-galactose + beta-D-glucuronic acid
-
Substrates: rate of hydrolysis is 76% of the with p-nitrophenyl-beta-D-glucuronide
Products: -
Products: -
?
carboxyumbelliferyl-beta-D-glucuronide + H2O
carboxyumbelliferone + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
chondroitin + H2O
D-glucuronate + ?
-
Substrates: 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
Products: -
Products: -
?
curcumin beta-D-glucuronide + H2O
curcumin + beta-D-glucuronic acid
Substrates: -
Products: -
Products: -
?
curcumin-beta-D-glucuronide + H2O
curcumin + beta-D-glucuronic acid
Substrates: curcumin, despite low systemic bioavailability, may be enzymatically activated (deconjugated) within GUSB-enriched bone to exert protective effects, a metabolic process that can also contribute to bone-protective effects of other highly glucuronidated dietary polyphenols
Products: -
Products: -
?
daidzein 7-O-beta-D-glucuronide + H2O
daidzein + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
equol 7-O-beta-D-glucuronide + H2O
equol + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
estriol 3-glucuronide + H2O
estriol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
GlcA-beta(1-6)Gal + H2O
D-glucuronate + D-galactopyranose
Substrates: 49.9% of the activity with 4-nitrophenyl beta-D-glucuronic acid
Products: -
Products: -
?
GlcAbeta(1-6)Gal + H2O
D-glucuronate + D-galactopyranose
-
Substrates: 85.7% of the activity with 4-nitrophenyl beta-D-glucuronic acid
Products: -
Products: -
?
GlcAbeta1-3GalNAc(4-OSO3-) + H2O
D-glucuronate + N-acetylamino-beta-D-galactopyranose 4-sulfate
-
Substrates: 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
Products: -
Products: -
?
glucuronic acid 1-phosphate + H2O
glucuronic acid + phosphate
-
Substrates: -
Products: -
Products: -
?
glycyrrhizin + H2O
18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide + beta-D-glucuronic acid
kaempferol 3-O-beta-D-glucuronide + H2O
kaempferol + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
luteolin 7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide] + H2O
?
-
Substrates: -
Products: -
Products: -
?
luteolin 7-O-[beta-D-glucuronosyl-(1->2)-beta-D-glucuronide]-4'-O-glucuronide + H2O
?
-
Substrates: -
Products: -
Products: -
?
methylumbelliferyl-beta-D-glucuronide + H2O
methylumbelliferone + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
N-([[4-(beta-D-glucopyranuronosyloxy)-3-nitrobenzyl]oxy]carbonyl)-N-methyl-L-valyl-N-[(3R,4S,5S)-1-[(2S)-2-[(1R,2R)-3-[[(1S,2R)-1-hydroxy-1-phenylpropan-2-yl]amino]-1-methoxy-2-methyl-3-oxopropyl]pyrrolidin-1-yl]-3-methoxy-5-methyl-1-oxoheptan-4-yl]-N-met + H2O
D-glucuronate + N-[[(4-hydroxy-3-nitrobenzyl)oxy]carbonyl]-N-methyl-L-valyl-N-[(3R,4S,5S)-1-[(2S)-2-[(1R,2R)-3-[[(1S,2R)-1-hydroxy-1-phenylpropan-2-yl]amino]-1-methoxy-2-methyl-3-oxopropyl]pyrrolidin-1-yl]-3-methoxy-5-methyl-1-oxoheptan-4-yl]-N-methyl-L-valinamide
-
Substrates: -
Products: -
Products: -
?
o-nitrophenyl-beta-D-glucuronide + H2O
o-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-glucuronide + H2O
D-glucuronate + ?
-
Substrates: 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
Products: -
Products: -
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
phenolphthalein beta-D-glucuronide + H2O
phenolphthalein + beta-D-glucuronate
-
Substrates: determination of specific activity in betaG-expressing tumour CT26 cells using radio-labeled substrate
Products: -
Products: -
?
phenolphthalein-beta-D-glucuronic acid + H2O
phenolphthalein + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
ir
quercetin 3-O-beta-D-glucuronide + H2O
quercetin + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
quercetin 4'-O-beta-D-glucuronide + H2O
quercetin + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
quercetin 7-O-beta-D-glucuronide + H2O
quercetin + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
quercetin-4'-O-glucuronide + H2O
quercetin + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
retinyl-beta-glucuronide + H2O
retinol + D-glucuronide
-
Substrates: -
Products: -
Products: -
?
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
-
Substrates: 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
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Bacteroides fragilis CCUG 4856
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Bacteroides fragilis Onslow
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
-
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Roseburia intestinalis DSM 14610
-
Substrates: -
Products: -
Products: -
?
4-methyl-beta-GlcA(1-6)beta-Gal(1-6)Gal + H2O
4-methyl-D-glucuronate + beta-Gal(1-6)Gal
-
Substrates: -
Products: 42.6% of the activity with 4-nitrophenyl beta-D-glucuronic acid
Products: 42.6% 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
Substrates: -
Products: 4.8% of the activity with 4-nitrophenyl beta-D-glucuronic acid
Products: 4.8% of the activity with 4-nitrophenyl beta-D-glucuronic acid
?
4-methylumbelliferyl beta-D-glucuronide + H2O
4-methylumbelliferone + beta-D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl beta-D-glucuronide + H2O
4-methylumbelliferone + beta-D-glucuronic acid
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
DQ459484
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenol beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
Substrates: -
Products: -
Products: -
?
4-nitrophenol beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
Aspergillus oryzae Li-3
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Bacteroides fragilis CCUG 4856
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Bacteroides fragilis Onslow
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
-
Substrates: -
Products: -
Products: -
?
4-nitrophenol-O-beta-D-glucuronide + H2O
D-glucuronate + 4-nitrophenol
Roseburia intestinalis DSM 14610
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-galactosiduronide + H2O
4-nitrophenol + beta-D-galactosiduronic acid
Substrates: the enzyme has a moderately broad specificity, hydrolysing a range of 4-nitrophenyl glycoside substrates, but has greatest activity on 4-nitrophenyl beta-D-glucuronide. The catalytic nucleophile is Glu476 within the sequence VTEFGAD
Products: -
Products: -
?
4-nitrophenyl beta-D-galactosiduronide + H2O
4-nitrophenol + beta-D-galactosiduronic acid
Substrates: the enzyme has a moderately broad specificity, hydrolysing a range of 4-nitrophenyl glycoside substrates, but has greatest activity on 4-nitrophenyl beta-D-glucuronide. The catalytic nucleophile is Glu476 within the sequence VTEFGAD
Products: -
Products: -
?
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
-
Substrates: 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
Products: -
Products: -
?
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
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
Substrates: the enzyme has a moderately broad specificity, hydrolysing a range of 4-nitrophenyl glycoside substrates, but has greatest activity on 4-nitrophenyl beta-D-glucuronide. The catalytic nucleophile is Glu476 within the sequence VTEFGAD
Products: -
Products: -
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + D-glucose
Substrates: the enzyme has a moderately broad specificity, hydrolysing a range of 4-nitrophenyl glycoside substrates, but has greatest activity on 4-nitrophenyl beta-D-glucuronide. The catalytic nucleophile is Glu476 within the sequence VTEFGAD
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronic acid + H2O
4-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronic acid + H2O
4-nitrophenol + D-glucuronic acid
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
A0A0H1IHR6
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
Substrates: the enzyme has a moderately broad specificity, hydrolysing a range of 4-nitrophenyl glycoside substrates, but has greatest activity on 4-nitrophenyl beta-D-glucuronide. The catalytic nucleophile is Glu476 within the sequence VTEFGAD
Products: -
Products: -
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
Substrates: the enzyme has a moderately broad specificity, hydrolysing a range of 4-nitrophenyl glycoside substrates, but has greatest activity on 4-nitrophenyl beta-D-glucuronide. The catalytic nucleophile is Glu476 within the sequence VTEFGAD
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Bacteroides fragilis CCUG 4856
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Bacteroides fragilis Onslow
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
-
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Roseburia intestinalis DSM 14610
-
Substrates: -
Products: -
Products: -
?
baicalin + H2O
baicalein + beta-D-glucuronate
-
Substrates: a major flavonoid derived from the root of Scutellaria baicalensis
Products: productivity of 73%
Products: productivity of 73%
?
baicalin + H2O
baicalein + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
baicalin + H2O
baicalein + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
bilirubin diglucuronide + H2O
bilirubin + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
bilirubin diglucuronide + H2O
bilirubin + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide + H2O
glycyrrhetic acid + D-glucuronate
Substrates: the enzyme shows similar activities toward both glycyrrhizin and glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
Products: -
Products: -
?
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide + H2O
glycyrrhetic acid + D-glucuronate
Aspergillus oryzae Li-3
Substrates: the enzyme shows similar activities toward both glycyrrhizin and glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
Products: -
Products: -
?
glycyrrhizin + H2O
18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide + beta-D-glucuronic acid
-
Substrates: specific substrate of isozymes I and II
Products: -
Products: -
?
glycyrrhizin + H2O
18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide + beta-D-glucuronic acid
-
Substrates: specific substrate of isozymes I and II
Products: -
Products: -
?
glycyrrhizin + H2O
18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide + beta-D-glucuronic acid
Substrates: -
Products: -
Products: -
?
glycyrrhizin + H2O
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide + D-glucuronate
Substrates: the enzyme shows similar activities toward both glycyrrhizin and glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
Products: -
Products: -
?
glycyrrhizin + H2O
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide + D-glucuronate
Aspergillus oryzae Li-3
Substrates: the enzyme shows similar activities toward both glycyrrhizin and glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
Products: -
Products: -
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + beta-D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + beta-D-glucuronic acid
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + beta-D-glucuronic acid
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronate
-
Substrates: -
Products: -
Products: -
?
phenolphthalein beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
phenolphthalein beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
phenolphthalein beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
phenolphthalein-beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
phenolphthalein-beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
phenolphthalein-beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
phenolphthalein-beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
-
Substrates: -
Products: -
Products: -
?
wogonin 7-O-beta-D-glucuronide + H2O
wogonin + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
wogonin 7-O-beta-D-glucuronide + H2O
wogonin + beta-D-glucuronate
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is slightly inducible by Met-Gly
Products: -
Products: -
?
additional information
?
-
-
Substrates: transglycosylation activity
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: the enzyme does not show strict specificity toward the aglycone moiety and exhibits activity toward all the natural and artificial substrates. Strict glycan specificity and hydrolyzes only the artificial substrate containing glucuronide groups
Products: -
Products: -
?
additional information
?
-
Aspergillus oryzae Li-3
Substrates: the enzyme does not show strict specificity toward the aglycone moiety and exhibits activity toward all the natural and artificial substrates. Strict glycan specificity and hydrolyzes only the artificial substrate containing glucuronide groups
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is not inducible by Met-Gly
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in physiology, in tissues, in body fluids
Products: -
Products: -
?
additional information
?
-
Substrates: the recombinant enzyme is active with hyaluronan oligosaccharides of C4-20 chain length with GlcA on non-reducing and N-acetyl-D-glucosamine (GlcNAc) on reducing end, GlcA and oligoHA with GlcNAc at both ends are released as products. No activity with a C2 substrate of with NN7 is a heptasaccharide with N-acetyl-D-glucosamine on both ends or with NA8 oligosaccharide, with GlcNAc at the non-reducing end and GlcA at the reducing end. But the enzyme is active with AA5 oligosaccharide with beta-D-GlcA at both ends has the following structure (->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->). Substrate specificity, overview. Immobilized and free recombinant enzymes show similar substrate specificities
Products: -
Products: -
-
additional information
?
-
Substrates: the recombinant enzyme is active with hyaluronan oligosaccharides of C4-20 chain length with GlcA on non-reducing and N-acetyl-D-glucosamine (GlcNAc) on reducing end, GlcA and oligoHA with GlcNAc at both ends are released as products. No activity with a C2 substrate of with NN7 is a heptasaccharide with N-acetyl-D-glucosamine on both ends or with NA8 oligosaccharide, with GlcNAc at the non-reducing end and GlcA at the reducing end. But the enzyme is active with AA5 oligosaccharide with beta-D-GlcA at both ends has the following structure (->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->). Substrate specificity, overview. Immobilized and free recombinant enzymes show similar substrate specificities
Products: -
Products: -
-
additional information
?
-
Bacteroides fragilis CCUG 4856
Substrates: the recombinant enzyme is active with hyaluronan oligosaccharides of C4-20 chain length with GlcA on non-reducing and N-acetyl-D-glucosamine (GlcNAc) on reducing end, GlcA and oligoHA with GlcNAc at both ends are released as products. No activity with a C2 substrate of with NN7 is a heptasaccharide with N-acetyl-D-glucosamine on both ends or with NA8 oligosaccharide, with GlcNAc at the non-reducing end and GlcA at the reducing end. But the enzyme is active with AA5 oligosaccharide with beta-D-GlcA at both ends has the following structure (->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->). Substrate specificity, overview. Immobilized and free recombinant enzymes show similar substrate specificities
Products: -
Products: -
-
additional information
?
-
Substrates: the recombinant enzyme is active with hyaluronan oligosaccharides of C4-20 chain length with GlcA on non-reducing and N-acetyl-D-glucosamine (GlcNAc) on reducing end, GlcA and oligoHA with GlcNAc at both ends are released as products. No activity with a C2 substrate of with NN7 is a heptasaccharide with N-acetyl-D-glucosamine on both ends or with NA8 oligosaccharide, with GlcNAc at the non-reducing end and GlcA at the reducing end. But the enzyme is active with AA5 oligosaccharide with beta-D-GlcA at both ends has the following structure (->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->). Substrate specificity, overview. Immobilized and free recombinant enzymes show similar substrate specificities
Products: -
Products: -
-
additional information
?
-
Substrates: the recombinant enzyme is active with hyaluronan oligosaccharides of C4-20 chain length with GlcA on non-reducing and N-acetyl-D-glucosamine (GlcNAc) on reducing end, GlcA and oligoHA with GlcNAc at both ends are released as products. No activity with a C2 substrate of with NN7 is a heptasaccharide with N-acetyl-D-glucosamine on both ends or with NA8 oligosaccharide, with GlcNAc at the non-reducing end and GlcA at the reducing end. But the enzyme is active with AA5 oligosaccharide with beta-D-GlcA at both ends has the following structure (->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->). Substrate specificity, overview. Immobilized and free recombinant enzymes show similar substrate specificities
Products: -
Products: -
-
additional information
?
-
Substrates: the recombinant enzyme is active with hyaluronan oligosaccharides of C4-20 chain length with GlcA on non-reducing and N-acetyl-D-glucosamine (GlcNAc) on reducing end, GlcA and oligoHA with GlcNAc at both ends are released as products. No activity with a C2 substrate of with NN7 is a heptasaccharide with N-acetyl-D-glucosamine on both ends or with NA8 oligosaccharide, with GlcNAc at the non-reducing end and GlcA at the reducing end. But the enzyme is active with AA5 oligosaccharide with beta-D-GlcA at both ends has the following structure (->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->). Substrate specificity, overview. Immobilized and free recombinant enzymes show similar substrate specificities
Products: -
Products: -
-
additional information
?
-
Bacteroides fragilis Onslow
Substrates: the recombinant enzyme is active with hyaluronan oligosaccharides of C4-20 chain length with GlcA on non-reducing and N-acetyl-D-glucosamine (GlcNAc) on reducing end, GlcA and oligoHA with GlcNAc at both ends are released as products. No activity with a C2 substrate of with NN7 is a heptasaccharide with N-acetyl-D-glucosamine on both ends or with NA8 oligosaccharide, with GlcNAc at the non-reducing end and GlcA at the reducing end. But the enzyme is active with AA5 oligosaccharide with beta-D-GlcA at both ends has the following structure (->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->3)-beta-D-GlcNAc-(1->4)-beta-D-GlcA-(1->). Substrate specificity, overview. Immobilized and free recombinant enzymes show similar substrate specificities
Products: -
Products: -
-
additional information
?
-
-
Substrates: role in physiology, in tissues, in body fluids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is inducible by Met-Gly
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: substrate specificity with flavonoids and phytoestrogens of crude and purified enzyme from digestive juice, overview
Products: -
Products: -
?
additional information
?
-
-
Substrates: transfer of beta-glucuronosyl residues from aryl and alicyclic glucuronides to aliphatic alcohols and glycerols
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in physiology, in tissues, in body fluids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in glycosaminoglycan metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is not inducible by Met-Gly
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is not inducible by Met-Gly
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity of isozymes I and II with 4-nitrophenyl beta-D-glucuronide, baicalin, and 18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide
Products: -
Products: -
?
additional information
?
-
-
Substrates: no activity of isozymes I and II with 4-nitrophenyl beta-D-glucuronide, baicalin, and 18beta-glycyrrhetinic acid-3-O-beta-D-glucuronide
Products: -
Products: -
?
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
LITERATURE
COMMENTARY
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
curcumin-beta-D-glucuronide + H2O
curcumin + beta-D-glucuronic acid
Substrates: curcumin, despite low systemic bioavailability, may be enzymatically activated (deconjugated) within GUSB-enriched bone to exert protective effects, a metabolic process that can also contribute to bone-protective effects of other highly glucuronidated dietary polyphenols
Products: -
Products: -
?
retinyl-beta-glucuronide + H2O
retinol + D-glucuronide
-
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Bacteroides fragilis CCUG 4856
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Bacteroides fragilis Onslow
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
-
Substrates: -
Products: -
Products: -
?
2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine beta-D-glucuronide + H2O
D-glucuronate + 2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine
Roseburia intestinalis DSM 14610
-
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Bacteroides fragilis CCUG 4856
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Bacteroides fragilis Onslow
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
-
Substrates: -
Products: -
Products: -
?
a beta-D-glucuronoside + H2O
D-glucuronate + an alcohol
Roseburia intestinalis DSM 14610
-
Substrates: -
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is slightly inducible by Met-Gly
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is not inducible by Met-Gly
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in physiology, in tissues, in body fluids
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in physiology, in tissues, in body fluids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is inducible by Met-Gly
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: role in physiology, in tissues, in body fluids
Products: -
Products: -
?
additional information
?
-
-
Substrates: 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
Products: -
Products: -
?
additional information
?
-
-
Substrates: the enzyme is involved in glycosaminoglycan metabolism
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is not inducible by Met-Gly
Products: -
Products: -
?
additional information
?
-
-
Substrates: activity is not inducible by Met-Gly
Products: -
Products: -
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
K+
Mg2+
Na+
NaCl
additional information
K+
DQ459484
below 0.1 mM, recombinant enzyme expressed in Escherichia coli is activated
Mg2+
DQ459484
below 1 mM, recombinant enzyme expressed in Escherichia coli is activated
Na+
DQ459484
below 1 mM, recombinant enzyme expressed in Escherichia coli is activated
NaCl
when 4-nitrophenol-O-beta-D-glucuronide is used as a substrate at pH 3.5, the salt concentration in the reaction considerably affects the activity of rBfGUS, diminishing its activity at the highest salt concentration tested (400 mM). At pH 4.5, rBfGUS's activity is slightly reduced as the salt concentration increased. The salt concentration does not have an effect on rBfGUS's activity at pH 5.5
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
additional information
the enzyme activity is 10fold higher in acetate buffer than in sodium phosphate buffer at pH 3.5
additional information
-
Na+, K+, Mg2+, Mn2+, and Ca2+ increase the activity but with no significance
additional information
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
additional information
-
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
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3S,4R,5R)-4,5-dihydroxypiperidine-3-carboxylic acid
inhibitor is present in a 4C1 conformation within the active site, mimicking that of the glycosyl intermediate. The compound is also a moderate inhibitor of heparanase
1,1'-(3-methyl-4-phenylthieno[2,3-b]thiophene-2,5-diyl)bis(4,4,4-triethoxybut-2-en-1-one)
-
-
2-deoxy-2-fluoro-beta-D-glucosyluronic acid fluoride
mechanism-based inactivator, D-saccharic acid 1,4-lactone protects the enzyme against inactivation
Al3+
DQ459484
10 mM, recombinant enzyme expressed in Escherichia coli is completely inhibited
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+
DQ459484
recombinant enzyme expressed in Escherichia coli is slightly inhibited
Cr3+
DQ459484
10 mM, recombinant enzyme expressed in Escherichia coli is completely inhibited
estradiol
E2, displays competitive inhibition towards GUS mediated 4-nitrophenol-O-beta-D-glucuronide hydrolysis. H-bonding interaction exists between the E2-17-OH and carboxylate of Glu413 in the active site. Two additional hydrogen bonds are also formed between the H2O in the crystal structure and E2. Docking study
Fe2+
DQ459484
1 mM, recombinant enzyme expressed in Escherichia coli is completely inhibited
Fe3+
DQ459484
10 mM, recombinant enzyme expressed in Escherichia coli is completely inhibited
magnolol
a UGT1A9 selective inhibitor. Magnolol inhibits GUS competitively in catalysing the hydrolysis of 4-nitrophenol-O-beta-D-glucuronide
Mn2+
DQ459484
1 mM, recombinant enzyme expressed in Escherichia coli is completely inhibited
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
Pb2+
DQ459484
10 mM, recombinant enzyme expressed in Escherichia coli is completely inhibited
S-saccharic acid 1,4-lactone
-
inhibits enzyme in several patients with colon cancer in addition to the healthy controls
Trifluoperazine
TFP, inhibition of GUS by TFP follows the competitive model for the deglucuronidation of 4-nitrophenol-O-beta-D-glucuronide. Docking analysis indicates that the fluorine atoms seem to be important for the inhibitor-protein interaction. The fluorine atoms form an H-bonding interaction with the NH of Trp-549 and three extra H-bonds are formed with H2O
Cu2+
DQ459484
1 mM, recombinant enzyme expressed in Escherichia coli is completely inhibited
saccharic acid 1,4-lactone
80% inhibition by 0.5 mM, 88% inhibition by 1.0 mM
Zn2+
DQ459484
1 mM, recombinant enzyme expressed in Escherichia coli is completely inhibited
additional information
UDP-glucuronosyltransferases (UGTs) and beta-glucuronidase (GUS) catalyze entirely distinct metabolism reactions. UGTs are responsible for the glucuronidation of a variety of drugs, endogenous and environmental chemicals, whereas GUS hydrolyzes glucuronides and liberates the parent substrates. Information on the overlap of ligand selectivity between UGT and GUS is essential for exploring the pharmacological or toxicological effects of the inhibitors of these two metabolic enzymes. Three typical ligands of UGTs, including two specific substrates (estradiol and trifluoperazine) and one selective inhibitor (magnolol, Mag), can inhibit the activity of GUS
-
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
-
additional information
-
substituted thieno[2,3-b]thiophenes and related congeners, synthesis of compounds incorporating the thieno[2,3-b]thiophene moiety, beta-glucuronidase inhibition activity, cytotoxicity, crystal structure, and Petra/Osiris/Molinspiration analyses, overview. No activity with 1,1'-(3-phenyl-4-methylthieno[2,3-b]thiene-2,5-diyl)bis[3-(dimethylamino)prop-2-en-1-one] and diethyl-4,4'-(3-methyl-4-phenylthieno[2,3-b]thiophene-2,5-dicarbonyl)bis(1-phenyl-1H-pyrazole-3-carboxylate)
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
abscisic acid
-
1.49fold increased enzyme activity after application of 100 micromo/l abscisic acid for 6 h
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
-
salicylic acid
-
44.6% increase of enzyme activity after treatment with 1 mmol/l salicylic acid for 5 h
additional information
-
increased expression and 1.87fold enzyme activity at dehydratation
-
additional information
-
85.2% increased activity in response to 250 mmol/l NaCl for 8 h
-
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
-
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1.25
4-methylumbelliferyl-beta-D-glucuronic acid
pH and temperature not specified in the publication
3.06
4-nitrophenyl beta-D-galactosiduronide
75°C, pH 6.5, wild-type enzyme
0.91
carboxyumbelliferyl-beta-D-glucuronide
-
pH 6.5, 38°C, Vmax: 0.041 mM/min
0.065
methylumbelliferyl-beta-D-glucuronide
-
pH 6.5, 38°C, Vmax: 0.026 mM/min
1.33
4-methylumbelliferyl-beta-D-glucuronide
-
37°C, pH 4.0-5.0, mutant enzyme E451A
0.0046
4-nitrophenyl beta-D-glucuronide
65°C, pH 6.5, mutant enzyme E383Q
0.0065
4-nitrophenyl beta-D-glucuronide
65°C, pH 6.5, mutant enzyme E383A
0.083
4-nitrophenyl beta-D-glucuronide
65°C, pH 6.5, wild-type enzyme
0.15
4-nitrophenyl beta-D-glucuronide
75°C, pH 6.5, wild-type enzyme
0.414
4-nitrophenyl-beta-D-glucuronide
-
mutant enzyme Q493R/T509A/M532T/N550S/G559S/N566S
0.91
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, mutant enzyme R563K
0.92
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, wild-type enzyme
1.06
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, mutant enzyme V447Q
1.1
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, mutant enzyme A365T
1.72
glycyrrhizin
pH 5, 55°C, low-shear modeled microgravity
0.018 - 3.08
phenolphthalein beta-D-glucuronide
-
dependency on form of enzyme
additional information
additional information
-
kinetics of mutant enzymes, overview
-
additional information
additional information
Michaelis-Menten kinetics
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
443
4-nitrophenyl beta-D-galactosiduronide
75°C, pH 6.5, wild-type enzyme
0.004
4-methylumbelliferyl-beta-D-glucuronide
-
37°C, pH 5.0, mutant enzyme E540A
0.015
4-methylumbelliferyl-beta-D-glucuronide
-
37°C, pH 4.0-5.0, mutant enzyme E451A
0.33
4-nitrophenyl beta-D-glucuronide
65°C, pH 6.5, mutant enzyme E383A
0.98
4-nitrophenyl beta-D-glucuronide
65°C, pH 6.5, mutant enzyme E383Q
29
4-nitrophenyl beta-D-glucuronide
65°C, pH 6.5, wild-type enzyme
68
4-nitrophenyl beta-D-glucuronide
75°C, pH 6.5, wild-type enzyme
1100
4-nitrophenyl-beta-D-glucuronide
-
mutant enzyme Q493R/T509A/M532T/N550S/G559S/N566S
0.89
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, mutant enzyme R563K
3.32
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, mutant enzyme V447Q
4.36
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, mutant enzyme A365T
7.81
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, wild-type enzyme
23.3
glycyrrhizin
pH 5, 55°C, low-shear modeled microgravity
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
145
4-nitrophenyl beta-D-galactosiduronide
75°C, pH 6.5, wild-type enzyme
0.06
4-nitrophenyl beta-D-glucoside
75°C, pH 6.5, wild-type enzyme
51
4-nitrophenyl beta-D-glucuronide
65°C, pH 6.5, mutant enzyme E383A
213
4-nitrophenyl beta-D-glucuronide
65°C, pH 6.5, mutant enzyme E383Q
352
4-nitrophenyl beta-D-glucuronide
65°C, pH 6.5, wild-type enzyme
453
4-nitrophenyl beta-D-glucuronide
75°C, pH 6.5, wild-type enzyme
0.98
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, mutant enzyme R563K
3.06
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, mutant enzyme A365T
3.13
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, mutant enzyme V447Q
8.49
glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
pH 5.0, 40°C, wild-type enzyme
13.55
glycyrrhizin
pH 5, 55°C, low-shear modeled microgravity
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00037
(3S,4R,5R)-4,5-dihydroxypiperidine-3-carboxylic acid
pH not specified in the publication, temperature not specified in the publication
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0009
1,1'-(3-methyl-4-phenylthieno[2,3-b]thiophene-2,5-diyl)bis(4,4,4-triethoxybut-2-en-1-one)
Homo sapiens
-
pH not specified in the publication, 37°C
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SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.02
crude enzyme cell extract, substrate 4-nitrophenol-O-beta-D-glucuronide, pH 6.5, 37°C
0.08
activity in crude cell extract from cell after growth for 9 h, activity-growth curve
0.09
crude enzyme cell extract, substrate 4-nitrophenol-O-beta-D-glucuronide, pH 6.5, 37°C
0.17
-
crude enzyme cell extract, substrate 4-nitrophenol-O-beta-D-glucuronide, pH 6.5, 37°C
0.73
crude enzyme cell extract, substrate 4-nitrophenol-O-beta-D-glucuronide, pH 6.5, 37°C
29.3
additional information
additional information
substrate specificity of recombinant free enzyme and recombinant immobilized enzyme, overview
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 37°C and pH 6.5
additional information
-
activities of crude and purified enzyme from digestive juice
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3.4
4 - 4.5
4.3
4.4
4.5
4.6
4.7
5.5
6.5
6.8
7.4
additional information
4
recombinant enzyme immobilized on magnetic macroporous bead cellulose (MBC)
4 - 4.5
recombinant enzyme immobilized on magnetic macroporous bead cellulose with fixed iminodiacetic acid (MBC-IDA)
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
additional information
-
comparison of values for different substrates and organisms
additional information
-
comparison of values for different substrates and organisms
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pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
3 - 5
4 - 5.5
4 - 7
pH 4.0: about 50% of maximal activity, pH 7.0: 25% of maximal activity
5 - 8.5
-
pH 5.0: about 45% of maximal activity, pH 8.5: about 50% of 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
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
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
45
52
55
60
65
70
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TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37 - 100
37°C: about 40% of maximal activity, 100°C: about 50% of maximal activity
37 - 75
37°C: about 60% of maximal activity, 75°C: about 90% of maximal activity
38 - 70
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pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
isolated from human intestinal microflora, gene uidA
SwissProt
brenda
isolated from human intestinal microflora, gene uidA
SwissProt
brenda
part of the normal flora of the respiratory and urogenital tracts of equines
UniProt
brenda
isolated from human intestinal microflora, two isozymes I and II
-
-
brenda
isolated from human intestinal microflora, two isozymes I and II
-
-
brenda
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26854, 26874, 26875, 484862, 654242, 654243, 654393, 655150, 679012, 680580, 682636, 698525, 699502, 699925, 708894, 709548, 714869, 715238, 716508, 730451, 749576
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26849, 26859, 26861, 26873, 654474, 654921, 655971, 656608, 679012, 682587, 697076, 697926, 698168, 710159, 729672, 730451, 731480, 739626
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2 different exo-beta-glucuronidases: a beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide and a beta-glucuronidase acting on chondroitin
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
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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
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additional information
additional information
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beta-glucuronidase is a lysosomal enzyme that increases in the tissues of animals in response to xenobiotics entering the body
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additional information
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CT26/betaG cell, colon carcinoma CT26 cells expressing beta-G
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additional information
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from armadillo liver infected with Mycobacterium leprae
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LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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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
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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
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digestive juice, composition of the digestive juice containing enzyme and phytoestrogen compounds, overview
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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
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Highest Expressing Human Cell Lines
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
metabolism
physiological function
malfunction
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beta-glucuronidase, an acid hydrolase that deconjugates glucuronides, may increase cancer risk
malfunction
mucopolysaccharidosis VII (MPS VII), called Sly syndrome, is caused by deficiency of the beta-glucuronidase
malfunction
two unique gene mutations in the enzyme beta-glucuronidase (GUSB), the single base pair deletion (MPSVII) and the intracisternal A particle element insertion (MPSVII2J), result in the lysosomal storage disease mucopolysaccharidosis (MPS) type VII. There is no significant phenotypic difference between the two mutations. The 2J variant is a more easily genotyped and equally affected phenotype. GUSB is necessary to degrade chondroitin-4 and -6 sulfates, dermatan sulfate, and heparan sulfate, and MPS leads to the accumulation of these glycosaminoglycans (GAGs) within the lysosomes of many cell types
malfunction
amiodarone-induced thyrotoxicosis (AIT) is a common and deleterious side effect of amiodarone use. There are two types of AIT, characterized by distinct pathogenic mechanisms and, hence, different treatments. Beta-G activity does not differ significantly between AIT1 and controls. But ROC curve analysis reveals that beta-G activity has a high predictive value for destructive processes, namely AIT2 and subacute and a cut-off value of 1,480.5 nmol 4-MU/ml plasma/h is able to discriminate between destructive and non-destructive thyroid conditions with 74% sensitivity and 82% specificity. Increased activity of beta-G has been detected in several body fluids of patients suffering from bacterial infections
malfunction
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two unique gene mutations in the enzyme beta-glucuronidase (GUSB), the single base pair deletion (MPSVII) and the intracisternal A particle element insertion (MPSVII2J), result in the lysosomal storage disease mucopolysaccharidosis (MPS) type VII. There is no significant phenotypic difference between the two mutations. The 2J variant is a more easily genotyped and equally affected phenotype. GUSB is necessary to degrade chondroitin-4 and -6 sulfates, dermatan sulfate, and heparan sulfate, and MPS leads to the accumulation of these glycosaminoglycans (GAGs) within the lysosomes of many cell types
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metabolism
microbiome-encoded beta-glucuronidase enzymes play important roles in human health by metabolizing drugs in the gastrointestinal tract
metabolism
A0A0H1IHR6
microbiome-encoded beta-glucuronidase enzymes play important roles in human health by metabolizing drugs in the gastrointestinal tract
metabolism
-
microbiome-encoded beta-glucuronidase enzymes play important roles in human health by metabolizing drugs in the gastrointestinal tract
metabolism
-
microbiome-encoded beta-glucuronidase enzymes play important roles in human health by metabolizing drugs in the gastrointestinal tract
metabolism
-
microbiome-encoded beta-glucuronidase enzymes play important roles in human health by metabolizing drugs in the gastrointestinal tract
metabolism
-
microbiome-encoded beta-glucuronidase enzymes play important roles in human health by metabolizing drugs in the gastrointestinal tract
metabolism
-
microbiome-encoded beta-glucuronidase enzymes play important roles in human health by metabolizing drugs in the gastrointestinal tract
metabolism
-
microbiome-encoded beta-glucuronidase enzymes play important roles in human health by metabolizing drugs in the gastrointestinal tract
metabolism
microbiome-encoded beta-glucuronidase enzymes play important roles in human health by metabolizing drugs in the gastrointestinal tract
metabolism
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
metabolism
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
metabolism
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
metabolism
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
metabolism
-
microbiome-encoded beta-glucuronidase enzymes play important roles in human health by metabolizing drugs in the gastrointestinal tract
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metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
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metabolism
Bacteroides fragilis CCUG 4856
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interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
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metabolism
Bacteroides fragilis Onslow
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interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
metabolism
Roseburia intestinalis DSM 14610
-
interaction of gut microbes and heterocyclic amines (HCA) can result in altered bioactivities, human gut microbiota can transform mutagenic HCA to a glycerol conjugate with reduced mutagenic potential. Stepwise microbial hydrolysis and acrolein conjugation of HCA glucuronides (HCA-G), that are viable precursors for glycerol conjugated metabolites, a process which is catalyzed by bacterial beta-glucuronidase (B-GUS) and glycerol/diol dehydratase (GDH) activity. HCA-G PhIP-N2-beta-D-glucuronide (PhIP-G), a representative liver metabolite of PhIP (2-amino-1-methyl-6-phenylimidazo [4,5-b] pyridine), the most abundant carcinogenic HCA in well-cooked meat, is transformed by enzymatic activity of human gut microbial representatives of the phyla Firmicutes, Bacteroidetes, and Proteobacteria. A bioanalysis approach combined with metagenomics shows that B-GUS of Faecalibacterium prausnitzii converts PhIP-G to PhIP and GDH of Flavonifractor plautii, Blautia obeum, Eubacterium hallii, and Lactobacillus reuteri convert PhIP to PhIP-M1 in the presence of glycerol. In addition, B-GUS- and GDH-positive bacteria cooperatively converts PhIP-G to PhIP-M1. GDH and HCA transformation activity in CRC patients, overview
-
physiological function
-
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-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates
physiological function
GUSB is necessary to degrade chondroitin-4 and -6 sulfates, dermatan sulfate, and heparan sulfate
physiological function
beta-glucuronidase (beta-G) is a lysosomal enzyme released into the extracellular fluid during inflammation. The enzyme is responsible for catalyzing the hydrolysis of glycosaminoglycans, thus participating in the degradation of extracellular matrix components. During inflammation, beta-G is released from lysosomes to the extracellular fluid, either as a result of tissue damage or as a secretory product of white blood cells
physiological function
enzyme GUS hydrolyzes glucuronides and liberates the parent substrates
physiological function
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
physiological function
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
physiological function
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
physiological function
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
physiological function
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
GUSB is necessary to degrade chondroitin-4 and -6 sulfates, dermatan sulfate, and heparan sulfate
-
physiological function
-
enzyme GUS hydrolyzes glucuronides and liberates the parent substrates
-
physiological function
Bacteroides fragilis CCUG 4856
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates
-
physiological function
Bacteroides fragilis CCUG 4856
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
Bacteroides fragilis Onslow
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates
-
physiological function
Bacteroides fragilis Onslow
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
physiological function
Roseburia intestinalis DSM 14610
-
in the intestine, glucuronide conjugates can be hydrolyzed by bacterial beta-glucuronidases (B-GUS), which liberate potentially bioactive aglycones, the release of OH-N-products can potentially lead to mutagenicity via interaction with colon epithelial cells. For HCA-N2-beta-D-glucuronide (HCA-G), heterocyclic amines (HCA) may be taken up into the liver, where it may be activated and potentially damage molecular targets such as DNA, or it may be converted back to HCA-G, re-entering the intestine
-
Show AA Sequence and Transmembrane Helices (4236 entries)
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
Please use the AA Sequence and Transmembrane Helices Search for a specific query.
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
250000 - 310000
280000 - 300000
-
gel filtration, beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide
290000
71000
75000
79000
-
2 * 79000, intracellular human beta-glucuronidase in transfected BHK cells, SDS-PAGE
83000
-
4 * 83000, the enzyme consists of two disulfide-linked dimers, wild-type enzyme and secreted recombinant enzyme, SDS-PAGE
75000
-
x * 75000, SDS-PAGE, beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
homotetramer
monomer
tetramer
additional information
?
-
x * 75000, SDS-PAGE, beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide
dimer
-
2 * 79000, intracellular human beta-glucuronidase in transfected BHK cells, SDS-PAGE
homotetramer
each monomer comprises three distinct domains: a sugar-binding, an immunoglobulin-like beta-sandwich, and a TIM barrel domain
homotetramer
Aspergillus oryzae Li-3
-
each monomer comprises three distinct domains: a sugar-binding, an immunoglobulin-like beta-sandwich, and a TIM barrel domain
-
tetramer
-
4 * 83000, the enzyme consists of two disulfide-linked dimers, wild-type enzyme and secreted recombinant enzyme, 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
domain organization, overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
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
glycoprotein
-
sequence contains 12 putative glycosylation sites. Treatment with endoglycanase F reduces the molecular mass to 55000 Da
glycoprotein
-
glycosylated at Asn173 and Asn420 with high mannose-type oligosaccharides
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
proteolytic modification
-
sequence contains a putative signal sequence, calculated molecular mass of immature protein is 58859
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
proteolytic modification
sequence contains a putative signal sequence, calculated molecular mass of immature protein is 60235
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
sitting drop vapor diffusion method at 16°C, structure of the enzyme is determined at 3.1 A resolution and structure of the inactive mutant enzyme E414D/E505D in complex with the native substrate glycyrrhetic acid 3-O-mono-beta-glucuronide at 2.6 A resolution
3D model shows catalytic resiudes E396, E508, and Y471in loop regions
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
A365H/R563E
the yield of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide of the mutant enzyme is 96% compared to less than 10% produced by wild-type enzyme, resulting in nearly complete alteration of the substrate selectivity of the glucuronyl hydrolase from glycyrrhetic acid to glycyrrhetinic acid 3-O-mono-beta-D-glucuronide formation. No activity with glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
A365Q
the yield of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide of the mutant enzyme is 65% compared to less than 10% produced by wild-type enzyme
A365T
the yield of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide of the mutant enzyme is 61% compared to less than 10% produced by wild-type enzyme
A365T/R563E
the yield of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide of the mutant enzyme is 95% compared to less than 10% produced by wild-type enzyme, resulting in nearly complete alteration of the substrate selectivity of the glucuronyl hydrolase from glycyrrhetic acid to glycyrrhetinic acid 3-O-mono-beta-D-glucuronide formation. No activity with glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
R563E
the yield of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide of the mutant enzyme is 77% compared to less than 10% produced by wild-type enzyme
R563K
the yield of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide of the mutant enzyme is 58% compared to less than 10% produced by wild-type enzyme. The catalytic efficiency (kcat/Km) toward glycyrrhetinic acid 3-O-mono-beta-D-glucuronide decreases by 88.4%, whereas kcat/Km toward GL decreases by 12.3%, confirming site 563 has a dramatic effect on substrate specificity
R563Q
the yield of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide of the mutant enzyme is 42% compared to less than 10% produced by wild-type enzyme
V447Q
the yield of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide of the mutant enzyme is 81% compared to less than 10% produced by wild-type enzyme
V447Q/R563K
the yield of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide of the mutant enzyme is 95% compared to less than 10% produced by wild-type enzyme, resulting in nearly complete alteration of the substrate selectivity of the glucuronyl hydrolase from glycyrrhetic acid to glycyrrhetinic acid 3-O-mono-beta-D-glucuronide formation. No activity with glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
R563K
Aspergillus oryzae Li-3
-
the yield of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide of the mutant enzyme is 58% compared to less than 10% produced by wild-type enzyme. The catalytic efficiency (kcat/Km) toward glycyrrhetinic acid 3-O-mono-beta-D-glucuronide decreases by 88.4%, whereas kcat/Km toward GL decreases by 12.3%, confirming site 563 has a dramatic effect on substrate specificity
-
R563Q
Aspergillus oryzae Li-3
-
the yield of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide of the mutant enzyme is 42% compared to less than 10% produced by wild-type enzyme
-
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 80°C 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
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
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 68°C
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 68°C
E383A
mutant E383A and wild-type enzyme show a similar melting temperatures of about 85°C
E383Q
mutant enzyme has a reduced thermostability, becoming unfolded at 72°C
E383A
-
mutant E383A and wild-type enzyme show a similar melting temperatures of about 85°C
-
E383Q
-
mutant enzyme has a reduced thermostability, becoming unfolded at 72°C
-
additional information
additional information
-
fusion gene of beta-glucuronidase with promoter gene of 9-cis-epoxycarotenoid dioxygenase, EC 1.13.11.51
additional information
-
fusion gene of beta-glucuronidase with promoter gene of 9-cis-epoxycarotenoid dioxygenase, EC 1.13.11.51
-
additional information
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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
additional information
immobilization of recombinant BfGUS on magnetic macroporous bead cellulose (MBC) using a standard method based on periodate oxidation of MBC, binding method and kinetics, overview. Immobilized and free recombinant enzymes show similar substrate specificities, but different pH optima. After 8 weeks of storage, both carriers are stable and maintain over 75% of their initial activity
additional information
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immobilization of recombinant BfGUS on magnetic macroporous bead cellulose (MBC) using a standard method based on periodate oxidation of MBC, binding method and kinetics, overview. Immobilized and free recombinant enzymes show similar substrate specificities, but different pH optima. After 8 weeks of storage, both carriers are stable and maintain over 75% of their initial activity
-
additional information
Bacteroides fragilis CCUG 4856
-
immobilization of recombinant BfGUS on magnetic macroporous bead cellulose (MBC) using a standard method based on periodate oxidation of MBC, binding method and kinetics, overview. Immobilized and free recombinant enzymes show similar substrate specificities, but different pH optima. After 8 weeks of storage, both carriers are stable and maintain over 75% of their initial activity
-
additional information
-
immobilization of recombinant BfGUS on magnetic macroporous bead cellulose (MBC) using a standard method based on periodate oxidation of MBC, binding method and kinetics, overview. Immobilized and free recombinant enzymes show similar substrate specificities, but different pH optima. After 8 weeks of storage, both carriers are stable and maintain over 75% of their initial activity
-
additional information
-
immobilization of recombinant BfGUS on magnetic macroporous bead cellulose (MBC) using a standard method based on periodate oxidation of MBC, binding method and kinetics, overview. Immobilized and free recombinant enzymes show similar substrate specificities, but different pH optima. After 8 weeks of storage, both carriers are stable and maintain over 75% of their initial activity
-
additional information
-
immobilization of recombinant BfGUS on magnetic macroporous bead cellulose (MBC) using a standard method based on periodate oxidation of MBC, binding method and kinetics, overview. Immobilized and free recombinant enzymes show similar substrate specificities, but different pH optima. After 8 weeks of storage, both carriers are stable and maintain over 75% of their initial activity
-
additional information
Bacteroides fragilis Onslow
-
immobilization of recombinant BfGUS on magnetic macroporous bead cellulose (MBC) using a standard method based on periodate oxidation of MBC, binding method and kinetics, overview. Immobilized and free recombinant enzymes show similar substrate specificities, but different pH optima. After 8 weeks of storage, both carriers are stable and maintain over 75% of their initial activity
-
additional information
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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
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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
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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
additional information
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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
additional information
two unique gene mutations in the enzyme beta-glucuronidase (GUSB) result in the lysosomal storage disease mucopolysaccharidosis (MPS) type VII. The single base pair deletion (MPSVII) and the intracisternal A particle element insertion (MPSVII2J) in GUSB in the mouse mutation model B6.Cg-Gusbmps/BrkJ are compared with control animals by skeletal measures, electroretinography, auditory-evoked brainstem response, and life span on a C57BL/6J background strain. In all measures, there is no significant phenotypic difference between the two mutations. The 2J variant is a more easily genotyped and equally affected phenotype. Detailed overview
additional information
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two unique gene mutations in the enzyme beta-glucuronidase (GUSB) result in the lysosomal storage disease mucopolysaccharidosis (MPS) type VII. The single base pair deletion (MPSVII) and the intracisternal A particle element insertion (MPSVII2J) in GUSB in the mouse mutation model B6.Cg-Gusbmps/BrkJ are compared with control animals by skeletal measures, electroretinography, auditory-evoked brainstem response, and life span on a C57BL/6J background strain. In all measures, there is no significant phenotypic difference between the two mutations. The 2J variant is a more easily genotyped and equally affected phenotype. Detailed overview
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pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
-
80 min, purified recombinant enzyme, 37°C, completely stable
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
50
55
60
62
unfolding of the E383Q mutant can be observed within the first 8 min while the E383A mutant does not show any denaturation even after 1 h
65
65 - 80
DQ459484
30 min, enzyme expressed in Arabidopsis thaliana is stable
68
70
72
mutant enzyme E383Q has a reduced thermostability, becoming unfolded at 72°C
85
37
-
enzyme encapsulated in biomimetic alginate/protamine/silica capsules, no loss of activity after 11 days, 90% remaining activity after 26 days
37
-
80 min, purified recombinant enzyme, pH 5.0-8.0, completely stable
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
-
the wild type enzyme loses its activity completely after 10 min at 70°C
85
DQ459484
30 min, enzyme expressed in Escherichia coli retains more than 80% of its activity
85
half-life: 3 h. Mutant E383A and wild-type enzyme show a similar melting temperatures of about 85°C
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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
the enzyme acting on chondroitin is less stable than enzyme acting on p-nitrophenylphosphate
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ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
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effect of solvents on soluble and immobilized enzyme
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STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-20°C or 4°C, 0.02 M sodium acetate buffer, pH 5.2, 0.15 M NaCl, 1 mg/ml protein, several months, sucrose prevents aggregation
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-20°C, enzyme acting on chondroitin retains high level of activity for at least 1 month
-
-20°C, form I: unstable, form II: 6 months, both forms stable in whole flies
-
0°C, 0.2 M potassium phosphate buffer, pH 8.0, 3 days, unstable at -20°C or 4°C or in sodium acetate buffer pH 4.0
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recombinant enzyme immobilized in 0.1 M acetate buffer pH 5 at 4°C, after 8 weeks of storage, both carriers are stable and maintain over 75% of their initial activity
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2 different exo-beta-glucuronidases: a beta-glucuronidase acting on p-nitrophenyl-beta-D-glucuronide and a beta-glucuronidase acting on chondroitin
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2 forms
3 forms
Blue Sepharose FF column chromatography, phenyl-Sepharose high-Sub FF column chromatography, DEAE-Sephacel column chromatography
-
DEAE Sepharose Fast Flow column chromatography and polyethyleneimine gel filtration
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from liver microsomes by calcium precipitation, immunoaffinity chromatography, preparative PAGE, gel filtration, and anion exchange chromatography to homogeneity
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native enzyme from digestive juice by ion exchange chromatography on a resin containing a polymeric sorbent
-
native enzyme from eggs, by ammonium sulfate fractionation, anion exchange chromatography, and heparin affinity chromatography
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native isozymes I and II to homogeneity by ammonium sulfate fractionation, hydrophobic interaction, ion exchange, and hydroxyapatite chromatographies, and glycyrrhizin affinity chromatography
-
Ni2+-affinity chromatography, anion-exchange chromatography, and gel filtration
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography to homogeneity
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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)
DNA and amino acid sequence determination and analysis, sequence comparisons, phylogenetic tree
expressed in 3T3 fibroblasts and EJ carcinoma cells
expressed in Escherichia coli
expression in both Escherichia coli and Arabidopsis thaliana. The enzyme expressed in transformed Escherichia coli cells exhibits maximum hydrolytic activity at 65°C and pH 6.5 and retains more than 80% activity after incubation at 85°C for 30 min. Activity in transgenic Arabidopsis thaliana plants containing TmGUSI is also stable over the temperature range 65-80°C
DQ459484
expression in Escherichia coli. Although Escherichia coli possesses an endogenous beta-glucuronidase activity, a short treatment at 80°C of the crude extract causes the precipitation of most Escherichia coli protein, resulting in an enrichment of the Sulfolobus beta-glucuronidase
expression in Pichia pastoris
expression of red fluorescent protein, RFP, fusion Gus in COS-7 cells, coexpression with GFP-tagged esterase 22
-
expression of the protein His6-tagged at its N terminus in Escherichia coli
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
-
gene gusA, expression of His-tagged wild-type and mutant enzymes in Escherichia coli
-
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
GUS, DNA and amino acid sequence determination, analysis and comparison, overexpression of the His-tagged enzyme in Escherichia coli strain GMS407
-
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
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
-
wild-type and mutant enzymes expressed COS cells and GUSB-deficient fibroblasts from the SV40 late promoter in vector pJC119
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
beta-glucuronidase is a lysosomal enzyme that increases in the tissues of animals in response to xenobiotics entering the body
-
enhanced expression when grown on agar plates supplemented with 4% sucrose under high light growth conditions
-
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
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
biotechnology
diagnostics
drug development
-
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
molecular biology
nutrition
-
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
synthesis
toxicology
additional information
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
-
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
-
assay for beta-glucuronidase is able to distinguish Escherichia coli from other Escherichia species
analysis
-
the enzyme is useful in analysis of phytoestrogens and related compounds in human biofluids, e.g. urine
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
analysis
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
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
Sulfolobus gene can be used as reporter in any thermophilic microorganism lacking an endogenous beta-glucuronidase activity
analysis
-
construction of a noncompetitive homogeneous biosensor system for immunodetection of small molecules based on beta-glucuronidase complementation
analysis
-
Sulfolobus gene can be used as reporter in any thermophilic microorganism lacking an endogenous beta-glucuronidase activity
-
biotechnology
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
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
-
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
-
diagnostics
-
the enzyme is useful in analysis of phytoestrogens and related compounds in human biofluids, e.g. urine
diagnostics
-
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
diagnostics
a technique for MPS VII diagnosis is adapted for smaller amounts of sample and reagents. That will facilitate the use of smaller amounts of samples, which may be used for other techniques and to save material. Given the importance of early MPS VII diagnosis due to the severity of the disease, using reliable diagnostic techniques in dried blood spots is essential
diagnostics
amiodarone-induced thyrotoxicosis (AIT) is a common and deleterious side effect of amiodarone use. There are two types of AIT, characterized by distinct pathogenic mechanisms and different treatments. Discriminating between type 1 (AIT1) and type 2 (AIT2) AIT is often very challenging. Plasma beta-G activity performs well in distinguishing AIT1 from AIT2
medicine
-
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
-
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
-
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
medicine
-
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
medicine
-
measurement of beta-glucuronidase activity has no additive clinical value following a parathion overdose in humans
medicine
-
bronchoalveolar lavage fluid of children with culture-positive bacterial inflammation displays a significant increase of beta-glucuronidase activity. beta-Glucuronidase activity shows superior predictive ability for bacterial lung infection than other markers of inflammation
medicine
-
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
-
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
-
beta-glucuronidase is the most frequent reporter gene in plants. Beta-glucuronidase enzyme activity is not only tissue-specific but also genotype-dependent
molecular biology
DQ459484
use of beta-glucuronidase from Thermotoga maritima as a thermostable marker in higher plants, reporter enzyme in plant genetic research
synthesis
the enzyme appears suitable for use in enzymatic oligosaccharide synthesis in either the transglycosylation mode or by use of glycosynthase and thioglycoligase approaches
synthesis
mutant enzyme A365H/R563E has great potential in the industrial production of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
synthesis
-
the enzyme appears suitable for use in enzymatic oligosaccharide synthesis in either the transglycosylation mode or by use of glycosynthase and thioglycoligase approaches
-
synthesis
Aspergillus oryzae Li-3
-
mutant enzyme A365H/R563E has great potential in the industrial production of glycyrrhetinic acid 3-O-mono-beta-D-glucuronide
-
toxicology
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
-
measurement of beta-glucuronidase activity has no additive clinical value following a parathion overdose in humans
additional information
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates. Lack of specificity towards hyaluronan (HA) for most beta-D-glucuronidases, in addition to the high cost and low purity of those active on HA, have prevented their widespread application
additional information
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates. Lack of specificity towards hyaluronan (HA) for most beta-D-glucuronidases, in addition to the high cost and low purity of those active on HA, have prevented their widespread application
-
additional information
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates. Lack of specificity towards hyaluronan (HA) for most beta-D-glucuronidases, in addition to the high cost and low purity of those active on HA, have prevented their widespread application
-
additional information
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates. Lack of specificity towards hyaluronan (HA) for most beta-D-glucuronidases, in addition to the high cost and low purity of those active on HA, have prevented their widespread application
-
additional information
Bacteroides fragilis CCUG 4856
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates. Lack of specificity towards hyaluronan (HA) for most beta-D-glucuronidases, in addition to the high cost and low purity of those active on HA, have prevented their widespread application
-
additional information
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates. Lack of specificity towards hyaluronan (HA) for most beta-D-glucuronidases, in addition to the high cost and low purity of those active on HA, have prevented their widespread application
-
additional information
Bacteroides fragilis Onslow
-
beta-D-glucuronidases catalyze the hydrolysis of a beta-D-glucuronic acid residue from the non-reducing end of various substrates. Lack of specificity towards hyaluronan (HA) for most beta-D-glucuronidases, in addition to the high cost and low purity of those active on HA, have prevented their widespread application
-
EXTERNAL LINKS (specific for EC-Number 3.2.1.31)
Transporter Classification Database (TCDB): 8.A.49.1.1
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Release 2026.1 (March 2026)
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