3.2.1.31: beta-glucuronidase
This is an abbreviated version!
For detailed information about beta-glucuronidase, go to the full flat file.
Word Map on EC 3.2.1.31
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3.2.1.31
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lysosomal
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urine
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urinary
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neutrophil
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bile
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leukocyte
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granule
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lysozyme
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polymorphonuclear
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hydrolases
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protoplasts
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mucopolysaccharidosis
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agrobacterium
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cathepsins
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cytochemical
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biliary
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tumefaciens
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cauliflower
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n-acetyl-beta-d-glucosaminidase
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beta-n-acetylglucosaminidase
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alpha-mannosidase
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degranulation
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glycosaminoglycans
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sulfatase
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glucuronic
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azurophilic
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beta-hexosaminidase
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nitroreductase
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nptii
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hygromycin
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zymosan
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alpha-galactosidase
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bombard
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calli
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glycosidases
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agrobacterium-mediated
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deconjugation
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neomycin
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unconjugated
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beta-d-galactosidase
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arylsulphatase
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fmlp
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diagnostics
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alpha-l-fucosidase
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synthesis
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coliforms
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medicine
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biotechnology
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alpha-naphthyl
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toxicology
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pomatia
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analysis
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hexosaminidase
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crevicular
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1,2-dimethylhydrazine
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drug development
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nutrition
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molecular biology
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alpha-l-iduronidase
- 3.2.1.31
- lysosomal
- urine
- urinary
- neutrophil
- bile
- leukocyte
- granule
- lysozyme
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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
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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
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crevicular
- 1,2-dimethylhydrazine
- drug development
- nutrition
- molecular biology
- alpha-l-iduronidase
Reaction
Synonyms
beta-D-glucuronidase, Beta-D-glucuronoside glucuronosohydrolase, Beta-G1, beta-Gluc, beta-glucuronidase, beta-glucuronidase A, betaG, BLG, exo-beta-D-glucuronidase, exo-beta-glucuronidase, GlcAase, glucuronidase, beta-glucuronide glucuronohydrolase, GUR, GUS, Gus2, GusA, GusB, hGUSB, ketodase, More, PGUS, TM1062, TmGUSI, UidA
ECTree
3.2.1.31 beta-glucuronidaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.1.31 - beta-glucuronidase
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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
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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
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R563Q
Aspergillus oryzae Li-3
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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
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D531E/S557V/N566S/G601S
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saturation mutagenesis, mutant 1.13, altered substrate specificity compared to the wild-type enzyme
Q493R/T509A/M532T/N550S/G559S/N566S
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mutant showing improved thermostability retaining 75% of its activity when heated at 80°C for 10 min
S193N/G466A/Q951R
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212% increased activity compared to the wild type enzyme
S193N/T266A/Q267R/Q626R
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167% increased activity compared to the wild type enzyme
S193N/V411A/D448G
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172% increased activity compared to the wild type enzyme
S22N/G81S/K257E/T509A/S557P/N566S/K568Q/Q598R/stop604W
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saturation mutagenesis, mutant 1.15, altered substrate specificity compared to the wild-type enzyme
S557I/N566A/K568R/A580V
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saturation mutagenesis, mutant 1.16, altered substrate specificity compared to the wild-type enzyme
S557Q/N566K/K568S/Q598stop
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saturation mutagenesis, mutant 1.2, altered substrate specificity compared to the wild-type enzyme
T266A/Q267R/Q626R
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137% increased activity compared to the wild type enzyme
V473A/S557P/N566S/K568Q
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saturation mutagenesis, mutant 4.7, altered substrate specificity compared to the wild-type enzyme
E451A
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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
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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
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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
E383Q
E476A
site-directed mutagenesis, the mutant enzyme shows increased thermal stability at 85°C compared to the wild-type enzyme
E383A
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mutant E383A and wild-type enzyme show a similar melting temperatures of about 85°C
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E383Q
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mutant enzyme has a reduced thermostability, becoming unfolded at 72°C
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E383A
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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site-directed mutagenesis, the mutant enzyme shows reduced activity and similar thermal stability at 85°C compared to the wild-type enzyme
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E383Q
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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site-directed mutagenesis, the mutant enzyme shows reduced activity and thermal stability at 85°C compared to the wild-type enzyme
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E476A
Thermotoga maritima MSB8 / DSM 3109 / ATCC 43589
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site-directed mutagenesis, the mutant enzyme shows increased thermal stability at 85°C compared to the wild-type enzyme
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additional information
E383A
site-directed mutagenesis, the mutant enzyme shows reduced activity and similar thermal stability at 85°C compared to the wild-type enzyme
E383A
mutant E383A and wild-type enzyme show a similar melting temperatures of about 85°C
E383Q
site-directed mutagenesis, the mutant enzyme shows reduced activity and thermal stability at 85°C compared to the wild-type enzyme
E383Q
mutant enzyme has a reduced thermostability, becoming unfolded at 72°C
additional information
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fusion gene of beta-glucuronidase with promoter gene of 9-cis-epoxycarotenoid dioxygenase, EC 1.13.11.51
additional information
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fusion gene of beta-glucuronidase with promoter gene of 9-cis-epoxycarotenoid dioxygenase, EC 1.13.11.51
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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
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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
