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Information on EC 3.2.1.31 - beta-glucuronidase and Organism(s) Escherichia coli and UniProt Accession P05804
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3.2.1.31 beta-glucuronidaseSpecify your search results
Word Map
- 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
The taxonomic range for the selected organisms is: Escherichia coli
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
beta-glucuronidase, beta-d-glucuronidase, betag, beta-gluc, beta-glucuronidase a, hgusb, exo-beta-glucuronidase, tmgusi, exo-beta-d-glucuronidase, ketodase, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
Beta-D-glucuronoside glucuronosohydrolase
-
-
-
-
Beta-G1
-
-
-
-
exo-beta-D-glucuronidase
-
-
-
-
glucuronidase, beta-glucuronide glucuronohydrolase
-
-
-
-
GUS
ketodase
-
-
-
-
GUS
-
-
-
-
PATHWAY SOURCE
PATHWAYS
BRENDA
KEGG
-
-, -
SYSTEMATIC NAME
IUBMB Comments
beta-D-glucuronoside glucuronosohydrolase
-
CAS REGISTRY NUMBER
COMMENTARY
9001-45-0
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronate
-
-
-
?
4-methylumbelliferyl-beta-D-glucuronide + H2O
4-methylumbelliferone + D-glucuronic acid
-
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + beta-D-glucuronic acid
-
-
-
-
?
4-nitrophenyl beta-D-glucuronide + H2O
4-nitrophenol + D-glucuronic acid
-
-
-
-
?
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylopyranose
-
preferred substrate
-
-
?
5-bromo-4-chloro-3-indoyl-beta-D-glucuronide + H2O
5-bromo-4-chloro-1H-indol-3-ol + beta-D-glucuronate
-
-
-
-
?
baicalin + H2O
baicalein + beta-D-glucuronate
-
a major flavonoid derived from the root of Scutellaria baicalensis
productivity of 73%
-
?
carboxyumbelliferyl-beta-D-glucuronide + H2O
carboxyumbelliferone + beta-D-glucuronate
-
-
-
-
?
methylumbelliferyl-beta-D-glucuronide + H2O
methylumbelliferone + beta-D-glucuronate
-
-
-
-
?
o-nitrophenyl-beta-D-glucuronide + H2O
o-nitrophenol + D-glucuronic acid
-
-
-
-
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronate
-
-
-
-
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronic acid
-
-
-
-
?
phenolphthalein-beta-D-glucuronide + H2O
phenolphthalein + D-glucuronic acid
-
-
-
-
?
additional information
?
-
-
the potent beta-glucuronidase activity caused by the glucuronic acid conjugates from xenobiotics and endogenous compounds is a prime factor in the etiology of colon cancer
-
-
?
additional information
?
-
-
when beta-glucuronidase producing bacteria infect the bile, the pH of the bile becomes raised, the high pH and bile induce the enzyme, and then bilirubin gallstones can be easily formed
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
the potent beta-glucuronidase activity caused by the glucuronic acid conjugates from xenobiotics and endogenous compounds is a prime factor in the etiology of colon cancer
-
-
?
additional information
?
-
-
when beta-glucuronidase producing bacteria infect the bile, the pH of the bile becomes raised, the high pH and bile induce the enzyme, and then bilirubin gallstones can be easily formed
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
S-saccharic acid 1,4-lactone
-
inhibits enzyme in several patients with colon cancer in addition to the healthy controls
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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
additional information
additional information
-
kinetics of mutant enzymes, overview
-
0.414
4-nitrophenyl-beta-D-glucuronide
-
mutant enzyme Q493R/T509A/M532T/N550S/G559S/N566S
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1100
4-nitrophenyl-beta-D-glucuronide
-
mutant enzyme Q493R/T509A/M532T/N550S/G559S/N566S
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
comparison of values for different substrates and organisms
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8.5
-
pH 5.0: about 45% of maximal activity, pH 8.5: about 50% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
45
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
microbiome-encoded beta-glucuronidase enzymes play important roles in human health by metabolizing drugs in the gastrointestinal tract
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
additional information
additional information
-
the enzyme is engineered as fusion with an N-terminal 76 amino acid ubiquitin-coding region. When translated in any eukaryotic cell, such ubiquitin fusions are cleaved by ubiqitin-specific proteases specifically after the C-terminus of ubiquitin, irrespective of the distal amino acid (with the exception of Pro), releasing the downstream protein with the specified amino terminus. The presence of an N-terminal uncleavable ubiquitin on GUS does not reduce activity. A version of GUS with phenylalanine at the mature N-terminus accumulates a minimum of 3fold lower than GUS with methionine at its mature N-terminus
additional information
-
rapid evolution of beta-glucuronidase specificity by saturation mutagenesis of an active site loop, DNA shuffling of point mutations, construction of diverse mutants with mutation of residues 557, 566, and 568, the mutants show increased activity with beta-D-xylopyranoside and reduced activity with beta-D-glucuronide, overview
additional information
-
encapsulation of the enzyme in biomimetic alginate/protamine/silica capsules increases the enzyme storage, recycling, pH and thermostability compared to free enzyme, overview. No appreciable loss in activity during 10 repeated reaction cycles
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
-
enzyme encapsulated in biomimetic alginate/protamine/silica capsules, no loss of activity after 11 days, 90% remaining activity after 26 days
70
-
the wild type enzyme loses its activity completely after 10 min at 70°C
ORGANIC SOLVENT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
effect of solvents on soluble and immobilized enzyme
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged wild-type and mutant enzymes from Escherichia coli by nickel affinity chromatography to homogeneity
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
gene gusA, expression of His-tagged wild-type and mutant enzymes 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
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
analysis
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
analysis
-
assay for beta-glucuronidase is able to distinguish Escherichia coli from other Escherichia species
analysis
-
enzymatic assay adapted to study the fate of fecal coliforms in survival experiments, and appears to be rapid and efficient way to estimate the microbiological quality of surface waters. The major advantage of the enzymtic assay is the very short time response, and thus this method offers a powerful, rapid, and efficient way to estimate the microbiological quality of bathing and fishing areas, and to monitor disinfection efficiencies
analysis
-
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
-
comparison of commercially available kits to assess water quality and evaluation of their ability to detect Escherichia coli. Chromocult, MI agar, Readycult, and Colilert detect beta-glucuronidase production from respectively 79.9, 79.9, 81.1, and 51.4% of the 74 Escherichia coli strains tested. These four methods detect beta-galactosidase production from respectively 85.1, 73.8, 84.1, and 84.1% of the total coliform strains tested. The high level of false-negative results for Escherichia coli recognition obtained by all four methods suggests that they may not be appropriate for identification of presumptive Escherichia coli strains
analysis
-
comparison of commercially available kits used for the simultaneous detection of coliforms and Escherichia coli from water. Membrane lactose glucuronide agar, Colilert-18, MI agar, Colitag and Chromocult agar to detect beta-D-glucuronidase activity are tested with over 1000 isolates of Escherichia coli recovered from naturally contaminated water samples. Four of the media give very similar results but membrane lactose glucuronide agar fails to detect glucuronidase activity in 15.6% of the cultures tested
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
-
construction of a noncompetitive homogeneous biosensor system for immunodetection of small molecules based on beta-glucuronidase complementation
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
-
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Bowers, L.D.; Johnson, P.R.
Characterization of immobilized beta-glucuronidase in aqueous and mixed solvent systems
Biochim. Biophys. Acta
661
100-105
1981
Escherichia coli
-
Wakabayashi, M.; Fishman,W.H.
The comparative ability of beta-glucuronidase preparations (liver, Escherichia coli, Helix pomatia, and Patella vulgata) to hydrolyze certain steroid glucosiduronic acids
J. Biol. Chem.
236
996-1001
1961
Bos taurus, Escherichia coli, Helix pomatia, Patella vulgata
Doyle, M.L.; Katzman, P.A.; Doisy, E.A.
Production and properties of bacterial beta-glucuronidase
J. Biol. Chem.
217
921-930
1955
Escherichia coli
Worley, C.K.; Ling, R.; Callis, J.
Engineering in vivo instability of firefly luciferase and Escherichia coli beta-glucuronidase in higher plants using recognition elements from the ubiquitin pathway
Plant Mol. Biol.
37
337-347
1998
Escherichia coli
Rice, E.W.; Allen, M.J.; Brenner, D.J.; Edberg, S.C.
Assay for beta-glucuronidase in species of the genus Escherichia coli and its applications for drinking-water analysis
Appl. Environ. Microbiol.
57
592-593
1991
Escherichia coli, no activity in Escherichia hermannii, no activity in Escherichia fergusonii, no activity in Escherichia vulneris, no activity in Escherichia blattae, no activity in Escherichia adecarboxylata
Tryland, I.; Fiksdal, L.
Enzyme characteristics of beta-D-galactosidase- and beta-D-glucuronidase-positive bacteria and their interference in rapid methods for detection of waterborne coliforms and Escherichia coli
Appl. Environ. Microbiol.
64
1018-1023
1998
Aerococcus viridans, Bacillus sp. (in: Bacteria), Escherichia coli, Sphingomonas paucimobilis, Staphylococcus warneri
Kim, D.H.; Jin, Y.H.
Intestinal bacterial beta-glucuronidase activity of patients with colon cancer
Arch. Pharm. Res.
24
564-567
2001
Escherichia coli
Kim, D.H.; Jin, Y.H.; Jung, E.A.; Han, M.J.; Kobashi, K.
Purification and characterization of beta-glucuronidase from Escherichia coli HGU-3, a human intestinal bacterium
Biol. Pharm. Bull.
18
1184-1188
1995
Escherichia coli, Escherichia coli HGU-3
Petit, M.; George, I.; Servais, P.
Survival of Escherichia coli in freshwater: beta-D-glucuronidase activity measurements and characterization of cellular states
Can. J. Microbiol.
46
679-684
2000
Escherichia coli
Geddie, M.L.; Matsumura, I.
Rapid evolution of beta-glucuronidase specificity by saturation mutagenesis of an active site loop
J. Biol. Chem.
279
26462-26468
2004
Escherichia coli
Chen, K.C.; Cheng, T.L.; Leu, Y.L.; Prijovich, Z.M.; Chuang, C.H.; Chen, B.M.; Roffler, S.R.
Membrane-localized activation of glucuronide prodrugs by beta-glucuronidase enzymes
Cancer Gene Ther.
14
187-200
2007
Escherichia coli, Homo sapiens, Mus musculus
Xiong, A.S.; Peng, R.H.; Zhuang, J.; Liu, J.G.; Xu, F.; Cai, B.; Guo, Z.K.; Qiao, Y.S.; Chen, J.M.; Zhang, Z.; Yao, Q.H.
Directed evolution of beta-galactosidase from Escherichia coli into beta-glucuronidase
J. Biochem. Mol. Biol.
40
419-425
2007
Escherichia coli
Xiong, A.; Peng, R.; Cheng, Z.; Li, Y.; Liu, J.; Zhuang, J.; Gao, F.; Xu, F.; Qiao, Y.; Zhang, Z.; Chen, J.; Yao, Q.
Concurrent mutations in six amino acids in beta-glucuronidase improve its thermostability
Protein Eng. Des. Sel.
20
319-325
2007
Escherichia coli
Arul, L.; Benita, G.; Balasubramanian, P.
Functional insight for beta-glucuronidase in Escherichia coli and Staphylococcus sp. RLH1
Bioinformation
2
339-343
2008
Escherichia coli (P05804), Escherichia coli, Staphylococcus sp. (Q9AFA2), Staphylococcus sp. RLH1 (Q9AFA2)
Horakova, K.; Mlejnkova, H.; Mlejnek, P.
Specific detection of Escherichia coli isolated from water samples using polymerase chain reaction targeting four genes: cytochrome bd complex, lactose permease, beta-D-glucuronidase, and beta-D-galactosidase
J. Appl. Microbiol.
105
970-976
2008
Escherichia coli
Maheux, A.F.; Huppe, V.; Boissinot, M.; Picard, F.J.; Bissonnette, L.; Bernier, J.L.; Bergeron, M.G.
Analytical limits of four beta-glucuronidase and beta-galactosidase-based commercial culture methods used to detect Escherichia coli and total coliforms
J. Microbiol. Methods
75
506-514
2008
Escherichia coli
Fricker, C.R.; DeSarno, M.; Warden, P.S.; Eldred, B.J.
False-negative beta-D-glucuronidase reactions in membrane lactose glucuronide agar medium used for the simultaneous detection of coliforms and Escherichia coli from water
Lett. Appl. Microbiol.
47
539-542
2008
Escherichia coli
Mueller, J.; Nillius, D.; Hehl, A.; Hemphill, A.; Mueller, N.
Stable expression of Escherichia coli beta-glucuronidase A (GusA) in Giardia lamblia: application to high-throughput drug susceptibility testing
J. Antimicrob. Chemother.
64
1187-1191
2009
Escherichia coli
Zhang, Y.; Wu, H.; Li, L.; Li, J.; Jiang, Z.; Jiang, Y.; Chen, Y.
Enzymatic conversion of baicalin into baicalein by beta-glucuronidase encapsulated in biomimetic core-shell structured hybrid capsules
J. Mol. Catal. B
57
130-135
2009
Escherichia coli
-
Geary, J.; Nijak, G.; Larson, S.; Talley, J.
Hydrolysis of the soluble fluorescent molecule carboxyumbelliferyl-beta-d-glucuronide by E. coli beta-glucuronidase as applied in a rugged, in situ optical sensor
Enzyme Microb. Technol.
49
6-10
2011
Escherichia coli
Borisenkov, M.F.; Bakutova, L.A.; Latkin, D.S.; Golovchenko, V.V.; Vityazev, F.V.
Interaction of microbial beta-glucuronidase with vegetable pectins
J. Agric. Food Chem.
59
9922-9926
2011
Escherichia coli
Ramadan, A.; Eissa, H.; El-Domyati, F.; Saleh, O.; Ibrahim, N.; Salama, M.; Mahfouz, M.; Bahieldin, A.
Characterization of inhibitor(s) of beta-glucuronidase enzyme activity in GUS-transgenic wheat
Plant Cell Tissue Organ Cult.
107
373-381
2011
Escherichia coli
-
Kawee-Ai, A.; Kim, S.M.
Application of microalgal fucoxanthin for the reduction of colon cancer risk: inhibitory activity of fucoxanthin against beta-glucuronidase and DLD-1 cancer cells
Nat. Prod. Commun.
9
921-924
2014
Escherichia coli, Homo sapiens
Su, J.; Dong, J.; Kitaguchi, T.; Ohmuro-Matsuyama, Y.; Ueda, H.
Noncompetitive homogeneous immunodetection of small molecules based on beta-glucuronidase complementation
Analyst
143
2096-2101
2018
Escherichia coli
Pollet, R.M.; DAgostino, E.H.; Walton, W.G.; Xu, Y.; Little, M.S.; Biernat, K.A.; Pellock, S.J.; Patterson, L.M.; Creekmore, B.C.; Isenberg, H.N.; Bahethi, R.R.; Bhatt, A.P.; Liu, J.; Gharaibeh, R.Z.; Redinbo, M.R.
An atlas of beta-glucuronidases in the human intestinal microbiome
Structure
25
967-977
2017
Escherichia coli (P05804)
EXTERNAL LINKS (specific for EC-Number 3.2.1.31)
Transporter Classification Database (TCDB): 8.A.49.1.1
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