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Information on EC 3.2.1.139 - alpha-glucuronidase
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3.2.1.139 alpha-glucuronidaseIUBMB Comments
Considerable differences in the specificities of the enzymes from different fungi for alpha-D-glucosiduronates have been reported. Activity is also found in the snail.
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Word Map
- 3.2.1.139
- glucuronoxylans
-
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
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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
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Synonyms
alpha-glucuronidase, gh115, glca67a, alpha-d-glucuronidase, alpha-(4-o-methyl)-d-glucuronidase, deg75-ag, boagu115a, agu4b, agu115, agu115a, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(4-O-methyl)-alpha-glucuronidase
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4-O-methylglucuronidase
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-
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alpha-(4-O-methyl)-D-glucuronidase
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-
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alpha-D-glucuronidase
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Alpha-glucosiduronase
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alpha-glucuronidase
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-
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Aryl alpha-glucuronidase
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GLRI
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-
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glucuronidase, alpha-
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-
-
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p-nitrophenyl alpha-D-glucuronide-hydrolyzing enzyme
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-
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PNP-GAase
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-
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REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of O-glycosyl bond
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SYSTEMATIC NAME
IUBMB Comments
alpha-D-glucosiduronate glucuronohydrolase
Considerable differences in the specificities of the enzymes from different fungi for alpha-D-glucosiduronates have been reported. Activity is also found in the snail.
CAS REGISTRY NUMBER
COMMENTARY
37259-81-7
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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
additional information
?
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the enzyme hydrolyzes methyl-alpha-D-glucuronic acid side chains from the internal regions of xylan. The enzyme is required to undergo a substantial conformational change to form a productive Michaelis complex with glucuronoxylan
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-
?
additional information
?
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the enzyme hydrolyzes methyl-alpha-D-glucuronic acid side chains from the internal regions of xylan. The enzyme is required to undergo a substantial conformational change to form a productive Michaelis complex with glucuronoxylan
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-
?
additional information
?
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hydrolysis of the glucurono-xylooligosaccharides derived from mature Arabidopsis thaliana wild-type and gux1gux2 stems as well as wild-type willow, barley, sugar cane, and Miscanthus stems, BoAgu115A is an alpha-glucuronidase that targets the uronic acids that decorate xylans
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-
?
additional information
?
-
-
hydrolysis of the glucurono-xylooligosaccharides derived from mature Arabidopsis thaliana wild-type and gux1gux2 stems as well as wild-type willow, barley, sugar cane, and Miscanthus stems, BoAgu115A is an alpha-glucuronidase that targets the uronic acids that decorate xylans
-
-
?
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 enzyme hydrolyzes methyl-alpha-D-glucuronic acid side chains from the internal regions of xylan. The enzyme is required to undergo a substantial conformational change to form a productive Michaelis complex with glucuronoxylan
-
-
?
additional information
?
-
-
the enzyme hydrolyzes methyl-alpha-D-glucuronic acid side chains from the internal regions of xylan. The enzyme is required to undergo a substantial conformational change to form a productive Michaelis complex with glucuronoxylan
-
-
?
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.3
birchwood xylan
recombinant wild-type enzyme, pH 6.5, 37°C, GH30 glucuronoxylan-specific xylanase treated substrate
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1.1
birchwood xylan
recombinant wild-type enzyme, pH 6.5, 37°C, GH30 glucuronoxylan-specific xylanase treated substrate
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
11.08
birchwood xylan
recombinant wild-type enzyme, pH 6.5, 37°C, GH30 glucuronoxylan-specific xylanase treated substrate
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14.37
birchwood xylan
recombinant wild-type enzyme, pH 6.5, 37°C, GH30 glucuronoxylan-specific xylanase treated substrate
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
13.06
birchwood xylan
recombinant wild-type enzyme, pH 6.5, 37°C, GH30 glucuronoxylan-specific xylanase treated substrate
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36.95
birchwood xylan
recombinant wild-type enzyme, pH 6.5, 37°C, GH30 glucuronoxylan-specific xylanase treated substrate
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
the enzyme is a member of the glycoside hydrolase family 115, GH115
additional information
additional information
the crystal structure of BoAgu115A reveals a four-domain protein in which the active site, comprising a pocket that abuts a cleft-like structure, is housed in the second domain that adopts a TIM barrel-fold. The third domain, a five-helical bundle, and the C-terminal beta-sandwich domain make inter-chain contacts leading to protein dimerization, topology of the xylan binding cleft of the enzyme. Active site structure, overview. Residue Arg328 may contribute to substrate binding by also interacting with the carboxylate of the glucuronic acid substrate, residue His422 is a component of the catalytic apparatus
additional information
-
the crystal structure of BoAgu115A reveals a four-domain protein in which the active site, comprising a pocket that abuts a cleft-like structure, is housed in the second domain that adopts a TIM barrel-fold. The third domain, a five-helical bundle, and the C-terminal beta-sandwich domain make inter-chain contacts leading to protein dimerization, topology of the xylan binding cleft of the enzyme. Active site structure, overview. Residue Arg328 may contribute to substrate binding by also interacting with the carboxylate of the glucuronic acid substrate, residue His422 is a component of the catalytic apparatus
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). A7M022_BACO1
Bacteroides ovatus (strain ATCC 8483 / DSM 1896 / JCM 5824 / BCRC 10623 / CCUG 4943 / NCTC 11153)
856
0
98232
TrEMBL
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
199000
analytical ultracentrifugation, recombinant wild-type enzyme
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
the enzyme consists of four distinct domains, which are connected by extended loops, structure overview
additional information
-
the enzyme consists of four distinct domains, which are connected by extended loops, structure overview
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
purified recombinant His6-tagged wild-type and selenomethionine-labeled enzyme or enzyme complexed with alpha-D-glucuronic acid, 10 mg/ml protein mixed with 19% PEG3350, 0.2 M sodium citrate, pH 5.5, soaking with 300 mM glucuronic acid for the complexed structure, use of mother liquor supplemented with 15% v/v PEG 400 or paratone N oil as cryoprotectant, X-ray diffraction structure determination and analysis at 2.14-3.0 A resolution
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
additional information
additional information
deletion of C-terminal residues 1-526, 1-639, and 1-665 results in inactive enzyme mutants
additional information
-
deletion of C-terminal residues 1-526, 1-639, and 1-665 results in inactive enzyme mutants
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) to homogeneity by immobilized metal ion affinity chromatography and gel filtration
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Rogowski, A.; Basle, A.; Farinas, C.S.; Solovyova, A.; Mortimer, J.C.; Dupree, P.; Gilbert, H.J.; Bolam, D.N.
Evidence that GH115 alpha-glucuronidase activity, which is required to degrade plant biomass, is dependent on conformational flexibility
J. Biol. Chem.
289
53-64
2014
Bacteroides ovatus (A7M022), Bacteroides ovatus
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