3.2.1.139: alpha-glucuronidase
This is an abbreviated version!
For detailed information about alpha-glucuronidase, go to the full flat file.
Word Map on EC 3.2.1.139
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3.2.1.139
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glucuronoxylans
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glucuronic
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agua
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endoxylanase
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beta-xylosidase
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xylooligosaccharides
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4-o-methyl-d-glucuronic
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xylanases
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meglca
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hardwood
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birchwood
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hemicelluloses
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schizophyllum
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arabinoxylans
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aldouronic
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xylotriose
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4-o-methylated
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4-o-methylglucuronic
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hemicellulolytic
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methylglucuronic
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arabinofuranosidase
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xylopyranosyl
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cellvibrio
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analysis
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degradation
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synthesis
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molecular biology
- 3.2.1.139
- glucuronoxylans
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glucuronic
-
agua
- endoxylanase
- beta-xylosidase
- xylooligosaccharides
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4-o-methyl-d-glucuronic
- xylanases
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meglca
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hardwood
-
birchwood
- hemicelluloses
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schizophyllum
- arabinoxylans
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aldouronic
- xylotriose
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4-o-methylated
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4-o-methylglucuronic
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hemicellulolytic
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methylglucuronic
- arabinofuranosidase
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xylopyranosyl
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cellvibrio
- analysis
- degradation
- synthesis
- molecular biology
Reaction
Synonyms
(4-O-methyl)-alpha-glucuronidase, 4-O-methylglucuronidase, aGlu, Agu115, Agu115A, Agu4B, AguA, alpha-(4-O-methyl)-D-glucuronidase, alpha-D-glucuronidase, Alpha-glucosiduronase, alpha-glucosiduronate glucuronohydrolase, alpha-glucuronidase, amylouronate hydrolase-I, Aryl alpha-glucuronidase, AugA, AUH-I, BoAgu115A, DEG75-AG, GH115, GH115 glucuronidase, GH67, GH67 alpha-glucuronidase, GlcA115A, GlcA67A, GLRI, glucuronidase, alpha-, glycosyl hydrolase family 115 alpha-glucuronidase, non-xylanolytic alpha-glucuronidase, p-nitrophenyl alpha-D-glucuronide-hydrolyzing enzyme, Pjdr2_5977, PNP-GAase, RUM630-AG, Sde_1755, TrDCase, TreDCase
ECTree
3.2.1.139 alpha-glucuronidaseAdvanced search results
results (
results (Engineering
Engineering on EC 3.2.1.139 - alpha-glucuronidase
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PROTEIN VARIANTS 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
D192A
site-directed mutagenesis, the mutation has no effect on the enzyme activity
D206A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D396N
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
D478A
site-directed mutagenesis, the mutation has no effect on the enzyme activity
E162A
site-directed mutagenesis, the mutation has no effect on the enzyme activity
E375A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E782A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
E785A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
H275A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
H422A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
K374A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N205A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
N398A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
N462A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
R328A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
W169A
site-directed mutagenesis, the mutation has no effect on the enzyme activity
W249A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y373A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y420A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
Y425A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y788A
site-directed mutagenesis, the mutant shows reduced activity compared to the wild-type enzyme
Y792A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
E292A
K288A
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kcat/KM for the substrate 4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside is 0.003% of wild-type value
K360A
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kcat/KM for the substrate 4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside is 0.019% of wild-type value
R325A
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kcat/KM for the substrate 4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside is 0.000096% of wild-type value
V210A
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kcat/KM for the substrate 4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside is 38% of wild-type value
V210G
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kcat/KM for the substrate 4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside is identical to wild-type value
V210N
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kcat/KM for the substrate 4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside is 9.4% of wild-type value
V210S
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kcat/KM for the substrate 4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside is 4.3% of wild-type value
W160A
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kcat/KM for the substrate 4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside is 0.0064% of wild-type value
W543A
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kcat/KM for the substrate 4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside is 0.069% of wild-type value
W328E/R329T
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activity of the monomeric mutant enzyme is significantly lower than activity of dimeric wild-type enzyme
W328E/R329T/R665N
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activity of the monomeric mutant enzyme is significantly lower than activity of dimeric wild-type enzyme, melting temperature is 0.5°C lower than. OPtimal temperature is around 35°C, compared to 65° for the wild-type enzym
W328E/R329T
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activity of the monomeric mutant enzyme is significantly lower than activity of dimeric wild-type enzyme
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W328E/R329T/R665N
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activity of the monomeric mutant enzyme is significantly lower than activity of dimeric wild-type enzyme, melting temperature is 0.5°C lower than. OPtimal temperature is around 35°C, compared to 65° for the wild-type enzym
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D335A
D335A
additional information
additional information
deletion of C-terminal residues 1-526, 1-639, and 1-665 results in inactive enzyme mutants
additional information
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deletion of C-terminal residues 1-526, 1-639, and 1-665 results in inactive enzyme mutants
additional information
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truncated forms of the enzyme, lacking either 126 amino acids from its N-terminus or 81 amino acids from its C-terminus, exhibit low residual activity
additional information
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truncated forms of the enzyme, lacking either 126 amino acids from its N-terminus or 81 amino acids from its C-terminus, exhibit low residual activity
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