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Information on EC 3.2.1.139 - alpha-glucuronidase and Organism(s) Cellvibrio japonicus and UniProt Accession B3PC73
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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
-
xylopyranosyl
-
cellvibrio
- analysis
- degradation
- synthesis
- molecular biology
The taxonomic range for the selected organisms is: Cellvibrio japonicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
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, 4-o-methylglucuronidase, agu4b, agu115, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
(4-O-methyl)-alpha-glucuronidase
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-
-
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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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-
-
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Alpha-glucosiduronase
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-
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alpha-glucuronidase
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-
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Aryl alpha-glucuronidase
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-
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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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-
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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
4-O-methyl-D-glucuronoxylan + H2O
4-O-methyl-D-glucuronic acid + xylan
-
-
-
?
aldotriouronic acid + H2O
4-O-methyl-alpha-D-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)Xyl
-
-
-
?
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside + H2O
4-nitrophenyl-D-xylopyranoside + 4-O-methyl-alpha-D-glucuronate
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-
-
-
?
aldotriouronic acid + H2O
4-O-methyl-alpha-D-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)Xyl
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-
-
-
?
additional information
?
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the role of the glucuronidase, in combination with cell-associated xylanases could be to hydrolyze decorated xylooligosaccharides, generated by extracellular hemicellulases, to xylose and 4-O-methyl-D-glucuronic acid, enabling the pseudomonad to preferentially utilize the sugars derived from these polymers
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-
?
additional information
?
-
-
the role of the glucuronidase, in combination with cell-associated xylanases could be to hydrolyze decorated xylooligosaccharides, generated by extracellular hemicellulases, to xylose and 4-O-methyl-D-glucuronic acid, enabling the pseudomonad to preferentially utilize the sugars derived from these polymers
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-
?
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 role of the glucuronidase, in combination with cell-associated xylanases could be to hydrolyze decorated xylooligosaccharides, generated by extracellular hemicellulases, to xylose and 4-O-methyl-D-glucuronic acid, enabling the pseudomonad to preferentially utilize the sugars derived from these polymers
-
-
?
additional information
?
-
-
the role of the glucuronidase, in combination with cell-associated xylanases could be to hydrolyze decorated xylooligosaccharides, generated by extracellular hemicellulases, to xylose and 4-O-methyl-D-glucuronic acid, enabling the pseudomonad to preferentially utilize the sugars derived from these polymers
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.19
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
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37°C, pH 7.0, mutant enzyme V210G
0.21
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
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37°C, pH 7.0, wild-type enzyme
0.69
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
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37°C, pH 7.0, mutant enzyme K288A
0.82
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
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37°C, pH 7.0, mutant enzyme W543A
0.86
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
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37°C, pH 7.0, mutant enzyme V210A
1.6
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37°C, pH 7.0, mutant enzyme K360A
2.1
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
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37°C, pH 7.0, mutant enzyme W160A
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.014
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
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37°C, pH 7.0, mutant enzyme K288A
0.09
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37°C, pH 7.0, mutant enzyme W160A
0.2
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37°C, pH 7.0, mutant enzyme K360A
0.38
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37°C, pH 7.0, mutant enzyme W543A
127
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37°C, pH 7.0, mutant enzyme V210G
143
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37°C, pH 7.0, wild-type enzyme
220
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
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37°C, pH 7.0, mutant enzyme V210A
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5 - 8
pH 5: 20% of maximal activity, pH 8: about 60% of maximal activity
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
crystal structure of mutant E292A in complex with its substrate aldobiouronic acid
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
E292A
K288A
-
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
-
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
-
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
-
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
-
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
-
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
susceptible to proteinase attack, inactivation by trypsin is similar to the inactivation rate for the intracellular enzyme malate dehydrogenase
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Nurizzo, D.; Nagy, T.; Gilbert, H.J.; Davies, G.J.
The structural basis for catalysis and specificity of the Pseudomonas cellulosa alpha-glucuronidase, GlcA67A
Structure
10
547-556
2002
Cellvibrio japonicus
Nagy, T.; Emami, K.; Fontes, C.M.; Ferreira, L.M.; Humphry, D.R.; Gilbert, H.J.
The membrane-bound alpha-glucuronidase from Pseudomonas cellulosa hydrolyzes 4-O-methyl-D-glucuronoxylooligosaccharides but not 4-O-methyl-D-glucuronoxylan
J. Bacteriol.
184
4925-4929
2002
Cellvibrio japonicus (B3PC73), Cellvibrio japonicus, Cellvibrio mixtus (Q8VP73), Cellvibrio mixtus
Nagy, T.; Nurizzo, D.; Davies, G.J.; Biely, P.; Lakey, J.H.; Bolam, D.N.; Gilbert, H.J.
The alpha-glucuronidase, GlcA67A, of Cellvibrio japonicus utilizes the carboxylate and methyl groups of aldobiouronic acid as important substrate recognition determinants
J. Biol. Chem.
278
20286-20292
2003
Cellvibrio japonicus
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