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Information on EC 3.2.1.139 - alpha-glucuronidase and Organism(s) Geobacillus stearothermophilus and UniProt Accession Q09LY5
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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: Geobacillus stearothermophilus
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, rum630-ag, pjdr2_5977, 4-o-methylglucuronidase, 
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
1,2-linked glucuronic acid of non-reducing xylose-oligosaccahrides + H2O
D-glucuronic acid + ?
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
-
-
?
aldouronic acid + H2O
D-xylose + 4-O-methyl-D-glucuronic acid
mixtures of aldobiouronic, aldottriouronic, aldotetraouronic, and aldopentaouronic acid, glucuronic acid groups attached via 1,2-linkage to xylose or non-reducing terminal residue of xylose-oligosaccharides
direct product of aldobiouronic acid
-
?
2-O-alpha-(4-O-methyl-alpha-D-glucopyranosyluronic)-D-xylobiose + H2O
4-O-methylglucuronic acid + D-xylobiose
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i.e. aldotriouronic acid
-
-
?
2-O-alpha-(4-O-methyl-alpha-D-glucuronosyl)-xylotriose + H2O
4-O-methyl-alpha-D-glucuronic acid + xylotriose
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i.e. aldotetraouronic acid
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-
?
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
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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
1,2-linked glucuronic acid of non-reducing xylose-oligosaccahrides + H2O
D-glucuronic acid + ?
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
?
-
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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
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-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.78
2-O-alpha-(4-O-methyl-alpha-D-glucopyranosyluronic)-D-xylobiose
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40°C, pH 6.5
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
15.3
-
hydrolysis of 2-O-alpha-(4-O-methyl-alpha-D-glucopyranosyluronic)-D-xylobiose
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4.5 - 7.5
-
about 40% of maximal activity at pH 4.5 and pH 7.5
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
65
TEMPERATURE RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
20 - 55
-
20°C: about 50% of maximal activity, 55°C: about 40% of maximal activity, mutant enzyme W328E/R329T/R665N
45 - 70
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45°C: about 35% of maximal activity, 70°C: about 50% of maximal activity
60 - 70
-
40°C: about 40% of maximal activity, 70°C: about 90% of maximal activity, wild-type enzyme
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
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). AGUA_GEOSE
679
0
78484
Swiss-Prot
Chloroplast (Reliability: 2)
PDB
SCOP
CATH
UNIPROT
ORGANISM
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
78339
-
1 * 78339, mutant enzymeW328E/R329T, calculated from sequence
78381
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1 * 78381, mutant enzymeW328E/R329T/R665N, calculated from sequence
78500
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1 * 78500, mutant enzymes W328E/R329T/R665N and W328E/R329T, SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
dimer
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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
monomer
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1 * 78339, mutant enzymeW328E/R329T, calculated from sequence
monomer
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1 * 78381, mutant enzymeW328E/R329T/R665N, calculated from sequence
monomer
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1 * 78500, mutant enzymes W328E/R329T/R665N and W328E/R329T, SDS-PAGE
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
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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
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
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
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
70
73
-
melting temperature of mutant enzyme W328E/R329T/R665N is 72.9°C, melting temperature of wild-type enzyme is 73.4°C
75
70
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20 min, wild-type enzyme and mutant enzyme W328E/R329T/R665N, about 10% loss of activity
75
-
20 min, wild-type enzyme loses 70% of its activity, mutant enzyme W328E/R329T/R665N copletely loses activity
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
soluble phase onto HisTrap HP column, eluted with imidazole gradient in sodium phosphate buffer, pH 8, and 300 mM sodium chloride
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
Escherichia coli BL21(DE3)pLysE, Luria-Bertani broth, 37°C, plasmid pET29-Gste-AG-his-S
overexpression in Escherichia coli using the T7 polymerase expression system
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
molecular biology
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Zaide, G.; Shallom, D.; Shulami, S.; Zolotnitsky, G.; Golan, G.; Baasov, T.; Shoham, G.; Shoham, Y.
Biochemical characterization and identification of catalytic residues in alpha-glucuronidase from Bacillus stearothermophilus T-6
Eur. J. Biochem.
268
3006-3016
2001
Geobacillus stearothermophilus, Geobacillus stearothermophilus T-6
Golan, G.; Shallom, D.; Teplitsky, A.; Zaide, G.; Shulami, S.; Baasov, T.; Stojanoff, V.; Thompson, A.; Shoham, Y.; Shoham, G.
Crystal structures of Geobacillus stearothermophilus alpha-glucuronidase complexed with its substrate and products: mechanistic implications
J. Biol. Chem.
279
3014-3024
2004
Geobacillus stearothermophilus
Teplitsky, A.; Shulami, S.; Moryles, S.; Zaide, G.; Shoham, Y.; Shoham, G.
Crystallization and preliminary X-ray analysis of alpha-D-glucuronidase from Bacillus stearothermophilus T-6
Acta Crystallogr. Sect. D
D55
869-872
1999
Geobacillus stearothermophilus, Geobacillus stearothermophilus T-6
-
Choi, I.D.; Kim, H.Y.; Choi, Y.J.
Gene cloning and characterization of alpha-glucuronidase of Bacillus stearothermophilus No. 236
Biosci. Biotechnol. Biochem.
64
2530-2537
2000
Geobacillus stearothermophilus
Shallom, D.; Golan, G.; Shoham, G.; Shoham, Y.
Effect of dimer dissociation on activity and thermostability of the alpha-glucuronidase from Geobacillus stearothermophilus: dissecting the different oligomeric forms of family 67 glycoside hydrolases
J. Bacteriol.
186
6928-6937
2004
Geobacillus stearothermophilus, Geobacillus stearothermophilus T-6
Lee, C.C.; Wagschal, K.; Kibblewhite-Accinelli, R.E.; Orts, W.J.; Robertson, G.H.; Wong, D.W.
An alpha-glucuronidase enzyme activity assay adaptable for solid phase screening
Appl. Biochem. Biotechnol.
155
314-320
2009
Geobacillus stearothermophilus (Q09LY5), Geobacillus stearothermophilus T6 (Q09LY5)
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