Information on EC 3.2.1.139 - alpha-glucuronidase

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The expected taxonomic range for this enzyme is: Eukaryota, Bacteria

EC NUMBER
COMMENTARY
3.2.1.139
-
RECOMMENDED NAME
GeneOntology No.
alpha-glucuronidase
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
an alpha-D-glucuronoside + H2O = an alcohol + D-glucuronate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
hydrolysis
A3LY17, -
-
hydrolysis
Geobacillus stearothermophilus T6
-
-
-
hydrolysis of O-glycosyl bond
-
-
-
-
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
(4-O-methyl)-alpha-glucuronidase
-
-
-
-
4-O-methylglucuronidase
-
-
-
-
Agu115
Schizophyllum commune ATCC 38548
-
-
-
Agu4B
P96105
-
AguA
Geobacillus stearothermophilus T-6
-
-
-
AguA
Talaromyces emersonii CBS 814.70
-
-
-
alpha-(4-O-methyl)-D-glucuronidase
-
-
-
-
alpha-D-glucuronidase
-
-
-
-
Alpha-glucosiduronase
-
-
-
-
alpha-glucosiduronate glucuronohydrolase
-
-
alpha-glucosiduronate glucuronohydrolase
-
-
-
alpha-glucuronidase
-
-
-
-
alpha-glucuronidase
Q09LY5
-
alpha-glucuronidase
Geobacillus stearothermophilus T6
Q09LY5
-
-
alpha-glucuronidase
A3LY17
-
amylouronate hydrolase-I
-
-
amylouronate hydrolase-I
-
-
-
Aryl alpha-glucuronidase
-
-
-
-
GH67 alpha-glucuronidase
-
-
GH67 alpha-glucuronidase
-
-
-
GLRI
-
-
-
-
glucuronidase, alpha-
-
-
-
-
non-xylanolytic alpha-glucuronidase
P96105
-
p-nitrophenyl alpha-D-glucuronide-hydrolyzing enzyme
-
-
-
-
PNP-GAase
-
-
-
-
TreDCase
-
-
CAS REGISTRY NUMBER
COMMENTARY
37259-81-7
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
strain 5-16
-
-
Manually annotated by BRENDA team
Aspergillus niger 5-16
strain 5-16
-
-
Manually annotated by BRENDA team
NRRL Y-2311-1
-
-
Manually annotated by BRENDA team
Aureobasidium pullulans NRRL Y-2311-1
NRRL Y-2311-1
-
-
Manually annotated by BRENDA team
strain J-37
-
-
Manually annotated by BRENDA team
Bacteroides sp. J-37
strain J-37
-
-
Manually annotated by BRENDA team
-
Q8VP74
SwissProt
Manually annotated by BRENDA team
strain T-6, recombinant enzyme
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus T-6
strain T-6
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus T-6
strain T-6, recombinant enzyme
-
-
Manually annotated by BRENDA team
Geobacillus stearothermophilus T6
T6
UniProt
Manually annotated by BRENDA team
RUT C-30
-
-
Manually annotated by BRENDA team
strain RUT C-30
-
-
Manually annotated by BRENDA team
Hypocrea jecorina RUT C-30
RUT C-30
-
-
Manually annotated by BRENDA team
Hypocrea jecorina RUT C-30
strain RUT C-30
-
-
Manually annotated by BRENDA team
no activity in Neocallimastix frontalis
-
-
-
Manually annotated by BRENDA team
no activity in Neocallimastix patriciarum
-
-
-
Manually annotated by BRENDA team
strain JDR-2
-
-
Manually annotated by BRENDA team
strain TH501b
-
-
Manually annotated by BRENDA team
strain JDR-2
-
-
Manually annotated by BRENDA team
strain TH501b
-
-
Manually annotated by BRENDA team
Polyporus versicolor
-
-
-
Manually annotated by BRENDA team
gene ABN67901, EMBL; CBS 6054
UniProt
Manually annotated by BRENDA team
Schizophyllum commune ATCC 38548
-
-
-
Manually annotated by BRENDA team
strain CBS 814.70
-
-
Manually annotated by BRENDA team
Talaromyces emersonii CBS 814.70
strain CBS 814.70
-
-
Manually annotated by BRENDA team
strain JW/SL-YS485
-
-
Manually annotated by BRENDA team
Thermoanaerobacterium sp. JW/SL-YS485
strain JW/SL-YS485
-
-
Manually annotated by BRENDA team
strain MSB8
-
-
Manually annotated by BRENDA team
strain MSB8
UniProt
Manually annotated by BRENDA team
Tyromyces palustris
-
-
-
Manually annotated by BRENDA team
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
1,2-linked glucuronic acid of non-reducing xylose-oligosaccahrides + H2O
D-glucuronic acid + ?
show the reaction diagram
Geobacillus stearothermophilus, Geobacillus stearothermophilus T6
Q09LY5
hemicellulose consists mostly of xylan, a polymer of beta-1,4-linked xylose residues, and has among others side chains of glucuronic acid, attached by 1,2-glycosidic bonds
-
-
?
additional information
?
-
-
-
-
-
-
additional information
?
-
-
enzyme is involved in hydrolysis of wood xylans
-
-
-
additional information
?
-
-
important enzyme for the utilization of substituted xylans
-
-
-
additional information
?
-
-
the three enzymes, xylanase, alpha-D-glucuronidase, and beta-glucosidase, together are responsible for complete degradation of larchwood xylan to xylose and 4-O-methyl-alpha-D-glucuronic acid
-
-
-
additional information
?
-
-
enzyme is induced by growth on beech wood or birch wood
-
-
-
additional information
?
-
-
the enzyme is involved in hydrolysis of xylan. Presence of endoxylanase is critical for efficient alpha-glucuronidase activity, and efficient alpha-glucuronidase activity is essential for the complete hydrolysis of intact xylan
-
-
-
additional information
?
-
Q8VP74
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
?
-
Thermoanaerobacterium sp. JW/SL-YS485
-
important enzyme for the utilization of substituted xylans, enzyme is induced by growth on beech wood or birch wood
-
-
-
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.54
-
4-O-methyl-glucuronic acid
-
37C, pH 7.0, wild-type enzyme
77.1
-
glucose
-
37C, pH 7.0, wild-type enzyme
3.84
-
glucuronic acid
-
37C, pH 7.0, wild-type enzyme
64.3
-
glucuronic acid
-
37C, pH 7.0, mutant enzyme V210N
78.3
-
glucuronic acid
-
37C, pH 7.0, mutant enzyme V210S
69.5
-
xylose
-
37C, pH 7.0, wild-type enzyme
SPECIFIC ACTIVITY [µmol/min/mg]
SPECIFIC ACTIVITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
0.07
-
-
crude extract
2.8
-
-
after 41.5fold purification
15.3
-
-
hydrolysis of 2-O-alpha-(4-O-methyl-alpha-D-glucopyranosyluronic)-D-xylobiose
61
-
-
partially purified enzyme
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
additional information
-
-
-
pI VALUE
pI VALUE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
4
-
A3LY17, -
isoelectrofocusing on Multiphor II system using SEVALYT PRECOTES gels and markers from 3-10
4.6
-
A3LY17, -
calculated from sequence
5.34
-
-
calculated from sequence
6.1
-
-
sequence analysis
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
SOURCE
-
of the enzyme grown in cultures containing filter paper, barley straw, birchwood xylan or birchwood sawdust as carbon source
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
80000
-
-
-
91600
-
-
sequence analysis
100000
300000
-
MW ranging from 100000 to 300000, the fraction with the highest activity has a MW of 103000, gel filtration
100000
-
-
-
115000
-
-
native AUH-I, gel filtration
118000
-
-
gel filtration
118000
-
-
gel filtration
120000
-
-
gel filtration
120000
-
A3LY17, -
SDS-PAGE with 2 sets of protein markers: Fermentas no. SM0431, SERVA no. 39216
124000
-
-
gel filtration
130000
-
-
gel filtration, native PAGE
150000
-
-
gel filtration
150000
-
Q8VP74
gel filtration
160000
-
-
gel filtration
161000
-
-
gel filtration
180000
-
-
gel filtration
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
?
-
x * 91000, SDS-PAGE
?
-
x * 97000, SDS-PAGE
?
-
x * 78480, calculated from sequence
?
-
x * 91000, calculated from sequence
?
A3LY17, -
x * 120000, SDS-PAGE
?
B5H8Y8
x * 111000, SDS-PAGE; x * 114000, calculated from amino acid sequence
?
Aureobasidium pullulans NRRL Y-2311-1
-
x * 91000, calculated from sequence
-
?
Geobacillus stearothermophilus T-6
-
x * 78480, calculated from sequence
-
?
Hypocrea jecorina RUT C-30
-
x * 91000, SDS-PAGE
-
dimer
-
1 * 72000 + 1 * 76000, SDS-PAGE
dimer
-
2 * 71000, SDS-PAGE
dimer
-
2 * 74000, SDS-PAGE
dimer
-
2 * 77000, SDS-PAGE; 2 * 78156, calculated from sequence
dimer
-
2 * 58000, SDS-PAGE
dimer
Q8VP74
-
dimer
-
wild-type enzyme. The dimerization of AguA is essential for efficient catalysis and the dissociation into monomers results in subtle conformational changes in the structure which indirectly influence the active site region and reduce the activity
dimer
Geobacillus stearothermophilus T-6
-
wild-type enzyme. The dimerization of AguA is essential for efficient catalysis and the dissociation into monomers results in subtle conformational changes in the structure which indirectly influence the active site region and reduce the activity
-
dimer
Thermoanaerobacterium sp. JW/SL-YS485
-
2 * 74000, SDS-PAGE
-
heterodimer
-
1 *80000 + 1 * 46000, SDS-PAGE
heterodimer
-
1 *80000 + 1 * 46000, SDS-PAGE
-
monomer
-
1 * 130000, SDS-PAGE
monomer
-
1 * 107000, SDS-PAGE
monomer
-
1 * 78339, mutant enzymeW328E/R329T, calculated from sequence; 1 * 78381, mutant enzymeW328E/R329T/R665N, calculated from sequence; 1 * 78500, mutant enzymes W328E/R329T/R665N and W328E/R329T, SDS-PAGE
monomer
Aspergillus niger 5-16
-
1 * 130000, SDS-PAGE
-
monomer
Geobacillus stearothermophilus T-6
-
1 * 78339, mutant enzymeW328E/R329T, calculated from sequence; 1 * 78381, mutant enzymeW328E/R329T/R665N, calculated from sequence; 1 * 78500, mutant enzymes W328E/R329T/R665N and W328E/R329T, SDS-PAGE
-
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
additional information
-
twenty putative N-glycosylation sites and four O-glycosylation sites
additional information
Talaromyces emersonii CBS 814.70
-
twenty putative N-glycosylation sites and four O-glycosylation sites
-
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
crystal structure of mutant E292A in complex with its substrate aldobiouronic acid
-
hanging-drop vapor diffusion method
-
hanging drop method, several high resolution crystal structures of the alpha-glucuronidase in complex with its substrate and products: structure of wild-type enzyme, structure of mutant enzyme E285N, mutant enzyme in complex with aldotetraouronic acid
-
hanging-drop vapor diffusion method. Two crystal forms: T1 and M1. T1 form: space group P4(1)2(1)2 or P4(3)2(1)2 with unit-cell dimensions a = b = 76.1 A, c = 331.2 A. The crystals are mechanically strong, are stable in the X-ray beam and diffract X-rays to better than 2.4 A resolution. M1 form: space group P2(1) with unit-cell dimensions a = 65.8, b = 127.4, c = 96.6 A and beta = 97.9. The crystals are quite strong and stable and diffract to better than 2.8 A resolution
-
sitting drop vapor diffusion method, using 20% (w/v) PEG 2000 MME and 0.1 M Tris pH 7.0
B5H8Y8
GENERAL STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
susceptible to proteinase attack, inactivation by trypsin is similar to the inactivation rate for the intracellular enzyme malate dehydrogenase
Q8VP74
STORAGE STABILITY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
-18C, 4 months, complete inactivation
-
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
D365A
-
activity is 0.0001% of wild-type activity
D365C
-
activity is 0.0001% of wild-type activity
E292A
-
activity is 0.0001% of wild-type activity
E292A
-
inactive mutant enzyme
E292C
-
activity is 0.0001% of wild-type activity
E393A
-
activity is 0.0001% of wild-type activity
E393C
-
activity is22% of wild-type activity
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
-
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
-
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
-
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
D274A
-
as active as wild-type enzyme
D364A
-
0.000015% of wild-type activity
D364A/E392C
-
0.0000004% of wild-type activity
E158N
-
0.07% of wild-type activity
E285N
-
0.0002% of wild-type activity
E386Q
-
0.07% of wild-type activity
E392C
-
0.00002% of wild-type activity
W328E/R329T
-
activity of the monomeric mutant enzyme is significantly lower than activity of dimeric wild-type enzyme
W328E/R329T/R665N
-
activity of the monomeric mutant enzyme is significantly lower than activity of dimeric wild-type enzyme, melting temperature is 0.5C lower than. OPtimal temperature is around 35C, compared to 65 for the wild-type enzym
D274A
Geobacillus stearothermophilus T-6
-
as active as wild-type enzyme
-
D364A
Geobacillus stearothermophilus T-6
-
0.000015% of wild-type activity
-
E158N
Geobacillus stearothermophilus T-6
-
0.07% of wild-type activity
-
W328E/R329T
Geobacillus stearothermophilus T-6
-
activity of the monomeric mutant enzyme is significantly lower than activity of dimeric wild-type enzyme
-
W328E/R329T/R665N
Geobacillus stearothermophilus T-6
-
activity of the monomeric mutant enzyme is significantly lower than activity of dimeric wild-type enzyme, melting temperature is 0.5C lower than. OPtimal temperature is around 35C, compared to 65 for the wild-type enzym
-
E510A
-
20% of wild-type activity
additional information
-
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
E510A
Geobacillus stearothermophilus T-6
-
20% of wild-type activity
-
additional information
Geobacillus stearothermophilus T-6
-
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
-
APPLICATION
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
analysis
-
development of a precise alpha-glucuronidase assay by coupling the alpha-glucuronidase catalyzed formation of 4-nitrophenyl beta-D-xylopyranoside with its efficient hydrolysis by xylosidase. A recombinant strain of Saccharomyces cerevisiae, harboring and expressing the beta-xylosidase gene xlnD of Aspergillus niger under control of the alcohol dehydrogenase II promoter on a multicopy plasmid, is used as source of beta-xylosidase
molecular biology
Q09LY5
screening instrument to find alpha-glucuronidase genes in DNA libraries in solid phase that enables higher throughput compared to liquid phase assays - screening of 50000 clones per 15-cm petri dish, addition of beta-xylosidase increases signal, the enzyme is important in facilitating the cellulose breakdown for biofuel production
molecular biology
Geobacillus stearothermophilus T6
-
screening instrument to find alpha-glucuronidase genes in DNA libraries in solid phase that enables higher throughput compared to liquid phase assays - screening of 50000 clones per 15-cm petri dish, addition of beta-xylosidase increases signal, the enzyme is important in facilitating the cellulose breakdown for biofuel production
-
analysis
-
development of a precise alpha-glucuronidase assay by coupling the alpha-glucuronidase catalyzed formation of 4-nitrophenyl beta-D-xylopyranoside with its efficient hydrolysis by xylosidase. A recombinant strain of Saccharomyces cerevisiae, harboring and expressing the beta-xylosidase gene xlnD of Aspergillus niger under control of the alcohol dehydrogenase II promoter on a multicopy plasmid, is used as source of beta-xylosidase
analysis
Hypocrea jecorina RUT C-30
-
development of a precise alpha-glucuronidase assay by coupling the alpha-glucuronidase catalyzed formation of 4-nitrophenyl beta-D-xylopyranoside with its efficient hydrolysis by xylosidase. A recombinant strain of Saccharomyces cerevisiae, harboring and expressing the beta-xylosidase gene xlnD of Aspergillus niger under control of the alcohol dehydrogenase II promoter on a multicopy plasmid, is used as source of beta-xylosidase
-
synthesis
-
hydrolysis of amylouronate to glucuronate by AUH-I
synthesis
-
hydrolysis of amylouronate to glucuronate by AUH-I
-
additional information
-
immobilized enzyme is effective in high yield production of D-glucuronic acid