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
SUBSTRATE
PRODUCT                      
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
-
-
?
2-O-alpha-(4-O-methyl-alpha-D-glucopyranosyluronic)-D-xylobiose + H2O
4-O-methylglucuronic acid + D-xylobiose
show the reaction diagram
-
i.e. aldotriouronic acid
-
-
?
2-O-alpha-(4-O-methyl-alpha-D-glucuronosyl)-xylotriose + H2O
4-O-methyl-alpha-D-glucuronic acid + xylotriose
show the reaction diagram
Geobacillus stearothermophilus, Geobacillus stearothermophilus T-6
-
i.e. aldotetraouronic acid
-
-
?
2-O-alpha-D-glucopyranosyluronic acid-D-xylose + H2O
alpha-D-glucopyranosyluronic acid + D-xylose
show the reaction diagram
-
-
-
-
-
2-O-alpha-D-glucuronosyl-D-xylose + H2O
D-glucuronate + D-xylose
show the reaction diagram
-
-
-
-
-
3-O-alpha-D-glucuronosyl-D-xylose + H2O
D-glucuronate + D-xylose
show the reaction diagram
-
-
-
-
-
4-nitrophenyl 2-(4-O-methyl-alpha-D-glucopyranosyl)-beta-D-xylopyranoside + H2O
4-nitrophenyl beta-D-xylopyranoside + 4-O-methyl-alpha-D-glucopyranose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside + H2O
4-nitrophenyl-D-xylopyranoside + 4-O-methyl-alpha-D-glucuronate
show the reaction diagram
-
-
-
-
?
4-O-alpha-D-glucuronosyl-D-xylose + H2O
D-glucuronate + D-xylose
show the reaction diagram
-
-
-
-
-
4-O-Me-GlcAalpha(1-2)Xylbeta(1-4)Xylbeta(1-4)Xyl + H2O
4-O-methyl-alpha-D-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)Xyl
show the reaction diagram
A3LY17, -
from beechwood, de-estrification of the methyl ester of MeGlcA with glucuronoyl esterase
de-estrification of the methyl ester of MeGlcA with glucuronoyl esterase
-
?
4-O-Me-GlcAalpha(1-2)Xylbeta(1-4)Xylbeta(1-4)[4-O-Me-GlcAalpha(1-2)]Xylbeta(1-4)Xyl + H2O
4-O-methyl-alpha-D-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)[4-O-Me-GlcAalpha(1-2)]Xylbeta(1-4)Xyl
show the reaction diagram
A3LY17, -
hydrolysis product of endoxylanases on glucuronoxylan
de-estrification of the methyl ester of MeGlcA with glucuronoyl esterase
-
?
4-O-methyl-alpha-D-glucopyranuronosyl-(1-2)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
4-O-methyl-alpha-D-glucuronic acid + beta-D-xylopyranose
show the reaction diagram
-
-
-
-
?
4-O-methyl-alpha-D-glucopyranuronosyl-(1-2)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose + H2O
4-O-methyl-alpha-D-glucuronic acid + beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranosyl-(1-4)-beta-D-xylopyranose
show the reaction diagram
-
-
-
-
?
4-O-methyl-D-glucuronoxylan + H2O
4-O-methyl-D-glucuronic acid + ?
show the reaction diagram
Q8VP74
-
-
-
?
4-O-methyl-glucuronosyl-xylan + H2O
4-O-methyl-glucuronate + xylan
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylan + H2O
4-O-methyl-glucuronate + xylan
show the reaction diagram
-
at 52% of the activity with 4-O-methyl-glucuronosyl-xylobiose
-
-
-
4-O-methyl-glucuronosyl-xylan + H2O
4-O-methyl-glucuronate + xylan
show the reaction diagram
Thermoanaerobacterium sp. JW/SL-YS485
-
-
-
-
-
4-O-methyl-glucuronosyl-xylitol + H2O
4-O-methyl-glucuronate + xylitol
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylobiose + H2O
4-O-methyl-glucuronate + xylobiose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylobiose + H2O
4-O-methyl-glucuronate + xylobiose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylobiose + H2O
4-O-methyl-glucuronate + xylobiose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylobiose + H2O
4-O-methyl-glucuronate + xylobiose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylobiose + H2O
4-O-methyl-glucuronate + xylobiose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylobiose + H2O
4-O-methyl-glucuronate + xylobiose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylobiose + H2O
4-O-methyl-glucuronate + xylobiose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylobiose + H2O
4-O-methyl-glucuronate + xylobiose
show the reaction diagram
Hypocrea jecorina RUT C-30
-
-
-
-
-
4-O-methyl-glucuronosyl-xyloheptaose + H2O
4-O-methyl-glucuronate + xyloheptaose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylohexaose + H2O
4-O-methyl-glucuronate + xylohexaose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylohexaose + H2O
4-O-methyl-glucuronate + xylohexaose
show the reaction diagram
-
at 53% of the activity with 4-O-methyl-glucuronosyl-xylobiose
-
-
-
4-O-methyl-glucuronosyl-xylopentaose + H2O
4-O-methyl-glucuronate + xylopentaose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylopentaose + H2O
4-O-methyl-glucuronate + xylopentaose
show the reaction diagram
-
at 50% of the activity with 4-O-methyl-glucuronosyl-xylobiose
-
-
-
4-O-methyl-glucuronosyl-xylose + H2O
4-O-methyl-glucuronate + xylose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylose + H2O
4-O-methyl-glucuronate + xylose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylose + H2O
4-O-methyl-glucuronate + xylose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylose + H2O
4-O-methyl-glucuronate + xylose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylose + H2O
4-O-methyl-glucuronate + xylose
show the reaction diagram
-
no activity
-
-
-
4-O-methyl-glucuronosyl-xylose + H2O
4-O-methyl-glucuronate + xylose
show the reaction diagram
-
no activity
-
-
-
4-O-methyl-glucuronosyl-xylose + H2O
4-O-methyl-glucuronate + xylose
show the reaction diagram
-
96% of the activity with 4-O-methyl-glucuronosyl-xylobiose
-
-
-
4-O-methyl-glucuronosyl-xylose + H2O
4-O-methyl-glucuronate + xylose
show the reaction diagram
Hypocrea jecorina RUT C-30
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotetraose + H2O
4-O-methyl-glucuronate + xylotetraose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotetraose + H2O
4-O-methyl-glucuronate + xylotetraose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotetraose + H2O
4-O-methyl-glucuronate + xylotetraose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotetraose + H2O
4-O-methyl-glucuronate + xylotetraose
show the reaction diagram
-
at 96% of the activity with 4-O-methyl-glucuronosyl-xylobiose
-
-
-
4-O-methyl-glucuronosyl-xylotetraose + H2O
4-O-methyl-glucuronate + xylotetraose
show the reaction diagram
Thermoanaerobacterium sp. JW/SL-YS485
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotetraose + H2O
4-O-methyl-glucuronate + xylotetraose
show the reaction diagram
Hypocrea jecorina RUT C-30
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
-
at 96% of the activity 4-O-methyl-glucuronosyl-xylobiose
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
-
at 99% of the activity with 4-O-methyl-glucuronosyl-xylobiose
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
Thermoanaerobacterium sp. JW/SL-YS485
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
Hypocrea jecorina RUT C-30
-
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
Aspergillus niger 5-16
-
-
-
-
-
acetylated glucuronoxylan + H2O
?
show the reaction diagram
-
-
-
-
-
aldobiouronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldobiouronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldobiouronic acid + H2O
?
show the reaction diagram
Q8VP74
-
-
-
?
aldobiouroniuc acid + H2O
?
show the reaction diagram
Aureobasidium pullulans, Aureobasidium pullulans NRRL Y-2311-1
-
-
-
-
?
aldohexauronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldohexauronic acid + H2O
?
show the reaction diagram
Schizophyllum commune, Schizophyllum commune ATCC 38548
-
best substrate
-
-
?
aldopentaouronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldopentaouronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldopentaouronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldopentaouronic acid + H2O
?
show the reaction diagram
Q8VP74
-
-
-
?
aldopentaouronic acid + H2O
?
show the reaction diagram
Talaromyces emersonii CBS 814.70
-
-
-
-
?
aldopentaouronic acid + H2O
?
show the reaction diagram
Aureobasidium pullulans NRRL Y-2311-1
-
-
-
-
?
aldopentauronic acid + H2O
4-O-methyl-D-glucuronic acid + ?
show the reaction diagram
-
-
-
-
?
aldopentauronic acid + H2O
4-O-methyl-D-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xyl
show the reaction diagram
-
-
-
-
?
aldopentauronic acid + H2O
4-O-methyl-D-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xyl
show the reaction diagram
B5H8Y8
i.e. 2''-O-alpha-(4-O-methyl-alpha-D-glucuronosyl)-xylotetraose
-
-
?
aldopentauronic acid + H2O
4-O-methyl-D-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xyl
show the reaction diagram
Schizophyllum commune ATCC 38548
-
-
-
-
?
aldotetraouronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldotetraouronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldotetraouronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldotetraouronic acid + H2O
?
show the reaction diagram
Q8VP74
-
-
-
?
aldotetraouronic acid + H2O
?
show the reaction diagram
Talaromyces emersonii CBS 814.70
-
-
-
-
?
aldotetraouronic acid + H2O
?
show the reaction diagram
Geobacillus stearothermophilus T-6
-
-
-
-
?
aldotetrauronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldotetrauronic acid + H2O
?
show the reaction diagram
-
best substrate
-
-
?
aldotetrauronic acid + H2O
?
show the reaction diagram
Schizophyllum commune ATCC 38548
-
-
-
-
?
aldotriouronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldotriouronic acid + H2O
?
show the reaction diagram
Q8VP74
-
-
-
?
aldotriuronic acid + H2O
?
show the reaction diagram
Schizophyllum commune, Scheffersomyces stipitis, Schizophyllum commune ATCC 38548
-
-
-
-
?
aldouronic acid + H2O
D-xylose + ?
show the reaction diagram
Geobacillus stearothermophilus, Geobacillus stearothermophilus T6
Q09LY5
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
-
?
amylouronate + H2O
D-glucuronate + ?
show the reaction diagram
-
AUH-I is highly specific to amylouronate, amylouronate is alpha-(1,4)-linked polyglucuronic acid sodium salt or alpha-(1,4)-linked glucuronan, AUH-I hydrolyses amylouronate exolytically
-
-
?
beechwood glucuronoxylan + H2O
?
show the reaction diagram
Schizophyllum commune, Scheffersomyces stipitis, Schizophyllum commune ATCC 38548
-
-
-
-
?
beechwood xylan + H2O
4-O-methyl-D-glucuronic acid + D-glucuronic acid
show the reaction diagram
B5H8Y8
-
-
-
?
benzyl 4-O-alpha-D-glucuronosyl-beta-D-glucoside + H2O
?
show the reaction diagram
-
-
-
-
-
beta-D-glucuronyl alpha-D-glucuronic acid + H2O
D-glucuronate + alpha-D-glucuronic acid
show the reaction diagram
Bacteroides sp., Bacteroides sp. J-37
-
-
-
-
-
birchwood xylan + H2O
4-O-methyl-D-glucuronic acid + D-glucuronic acid
show the reaction diagram
B5H8Y8
-
-
-
?
GlcAalpha(1-2)Xylbeta(1-4)Xylbeta(1-4)[GlcAalpha(1-2)]Xylbeta(1-4)Xyl + H2O
alpha-D-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)[GlcAalpha(1-2)]Xylbeta(1-4)Xyl
show the reaction diagram
A3LY17, -
generated from the action of endoxylanases on polysaccharides
de-estrification of the methyl ester of MeGlcA with glucuronoyl esterase
-
?
glucuronosyl-xylotriose + H2O
glucuronate + xylotriose
show the reaction diagram
Aspergillus niger, Aspergillus niger 5-16
-
-
-
-
-
glucuronoxylan + H2O
4-O-methyl-D-glucuronic acid + ?
show the reaction diagram
-
-
-
-
?
O-alpha-D-glucopyranosyluronic acid-alpha-D-glucopyranosiduronic acid + H2O
alpha-D-glucopyranosyluronic acid + alpha-D-glucopyranosiduronic acid
show the reaction diagram
-
-
-
-
-
O-alpha-D-glucosyluronic acid alpha-D-glucosiduronic acid
D-glucuronic acid
show the reaction diagram
-
the immobilized enzyme completely hydrolyzes 100 mM of the substrate
-
-
?
O-alpha-D-glucosyluronic acid alpha-D-glucosiduronic acid + H2O
alpha-D-glucosiduronic acid + beta-D-glucosiduronic acid
show the reaction diagram
-
-
alpha-D-glucosiduronic acid and beta-D-glucosiduronic acid are produced in an equimolar ratio
-
?
O-alpha-glucuronosyl alpha-D-glucuronide + H2O
D-glucuronate
show the reaction diagram
-
-
-
-
-
p-nitrophenyl alpha-D-glucuronide + H2O
p-nitrophenol + D-glucuronate
show the reaction diagram
-
-
-
-
-
p-nitrophenyl alpha-D-glucuronopyranoside + H2O
p-nitrophenol + D-glucuronate
show the reaction diagram
P96105, -
-
-
-
?
p-nitrophenyl-alpha-D-glucuronopyranoside + H2O
p-nitrophenol + D-glucuronate
show the reaction diagram
-
-
-
-
?
p-nitrophenyl-beta-D-glucuronide + H2O
p-nitrophenol + D-glucuronate
show the reaction diagram
Bacteroides sp., Bacteroides sp. J-37
-
3% of the activity with 18beta-glycyrrhetinic acid beta-D-glucuronyl alpha-D-glucuronic acid
-
-
-
reduced aldopentaouronic acid + H2O
4-O-methyl-D-glucuronic acid + ?
show the reaction diagram
-
-
-
-
?
glycyrrhizin + H2O
glycyrrhetinic acid + 2 D-glucuronate
show the reaction diagram
Bacteroides sp., Bacteroides sp. J-37
-
-
-
-
-
additional information
?
-
-
-
-
-
-
additional information
?
-
-
enzyme prefers low-molecular-weight xylooligomers as substrates. The enzyme acts almost exclusively on the bond between the terminal xylose at the nonreducing end of the xylose chain and the methyl glucuronic acid attached to it
-
-
-
additional information
?
-
-
no activity with baicalin
-
-
-
additional information
?
-
-
no activity with p-nitrophenyl-alpha-D-glucuronoside
-
-
-
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
?
-
-
no hydrolysis of O-alpha-D-glucosyluronic acid alpha-D-glucoside, O-alpha-D-glucosyluronic acid beta-D-glucosiduronic acid, O-alpha-D-glucosyluronic acid-(1,2)-beta-D-fructosiduronic acid, p-nitrophenyl-O-alpha-D-glucosiduronic acid, methyl-O-alpha-D-glucosiduronic acid, or 6-O-alpha-(4-O-alpha-D-glucosyluronic acid)-D-glucosyl-beta-cyclodextrine
-
-
-
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
-
-
-
additional information
?
-
Hypocrea jecorina RUT C-30
-
enzyme prefers low-molecular-weight xylooligomers as substrates. The enzyme acts almost exclusively on the bond between the terminal xylose at the nonreducing end of the xylose chain and the methyl glucuronic acid attached to it
-
-
-
additional information
?
-
Bacteroides sp. J-37
-
no activity with baicalin
-
-
-
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
-
-
-
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
Ag+
-
2 mM, slight activation
BaCl2
-
slight activation
Ca2+
-
2 mM, slight activation
CaCl2
-
slight activation
Cu2+
-
2 mM, slight activation
Fe3+
-
1 mM, 25% activation
FeCl3
-
slight activation
K+
-
2 mM, slight activation
Mg2+
-
2 mM, slight activation
Mn2+
-
slightly increases activity, 1 mM required for maximal activity
Na+
-
2 mM, slight activation
INHIBITORS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
4-O-Methyl-D-glucuronic acid
-
-
Ag+
-
1 mM, 90% inhibition
Ag+
-
1 mM, 58% inhibition
Cd2+
-
1 mM, strong inhibition
Cu2+
-
1 mM, strong inhibition
Cu2+
-
0.1 mM, complete inhibition
Cu2+
-
1 mM, complete inhibition
D-glucose
-
represses
D-glucuronic acid
-
-
D-glucuronic acid
-
represses
D-glucuronic acid
-
significantly inhibits in the presence of over 200 mM substrate, complete hydrolysis of 500 mM substrate is accomplished when D-glucuronic acid concentration is kept below 300-400 mM
DTT
-
50 mM, required for maximal activity
Fe2+
-
2 mM, weak inhibition
-
Fe3+
-
2 mM, weak inhibition
-
Hg2+
-
1 mM, strong inhibition
Hg2+
-
25% inhibition at 0.1 mM, complete inhibition at 1 mM
Hg2+
-
1 mM, complete inhibition
Hg2+
-
2 mM, 58% inhibition
K+
-
1 mM, 15% inhibition
Mn2+
-
1 mM, 78% inhibition
Mn2+
P96105
required
Mn2+
-
2 mM, weak inhibition
Monoiodoacetic acid
-
-
Monoiodoacetic acid
-
-
N-bromosuccinimide
-
-
N-bromosuccinimide
-
-
Ni2+
-
1 mM, 10% inhibition
p-hydroxymercuribenzoate
-
-
Pb2+
-
1 mM, strong inhibition
Pb2+
-
1 mM, 53% inhibition
SDS
-
2 mM, 48% inhibition
Zn2+
-
1 mM, strong inhibition
Zn2+
-
1 mM, 55% inhibition
Zn2+
-
1 mM, 43% inhibition
ACTIVATING COMPOUND
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
P96105
maximal activation at 150 mM
DTT
P96105
activates
NAD+
P96105
maximal activation at 0.5 mM
solka floc
-
low levels of activity
xylan
-
induces activity, maximum activity on beechwood xylan, activity also on oat spelt and birchwood xylan, low levels of activity on wheat arabinoxylan and larchwood xylan
L-cysteine
P96105
maximal activation at 0.6 mM, 15% of the activation with 2-mercaptoethanol
additional information
-
glutaraldehyde stabilizes
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.12
-
(3beta)-30-hydroxy-11,30-dioxoolean-12-en-3-yl 2-O-beta-D-glucopyranuronosyl-alpha-D-glucopyranosiduronic acid
-
-
17.6
-
2-O-(4-methyl-alpha-D-glucopyranosyluronic acid)-D-xylose
-
-
0.78
-
2-O-alpha-(4-O-methyl-alpha-D-glucopyranosyluronic)-D-xylobiose
-
40C, pH 6.5
0.33
-
2-O-alpha-D-Glucopyranosyluronic acid-D-xylose
-
-
0.21
-
4-nitrophenyl 2-(4-O-methyl-alpha-D-glucopyranosyl)-beta-D-xylopyranoside
-
37C, pH 5.0
0.39
-
4-nitrophenyl 2-(4-O-methyl-alpha-D-glucopyranosyl)-beta-D-xylopyranoside
-
37C, pH 5.0
0.58
-
4-nitrophenyl 2-(4-O-methyl-alpha-D-glucopyranosyl)-beta-D-xylopyranoside
-
37C, pH 5.0
0.19
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme V210G
0.21
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, wild-type enzyme
0.69
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme K288A
0.82
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme W543A
0.86
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme V210A
1.6
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme K360A
2.1
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme W160A
0.76
-
4-O-Methyl-glucuronosyl-xylobiose
-
-
0.95
-
4-O-Methyl-glucuronosyl-xylobiose
-
-
0.145
-
4-O-Methyl-glucuronosyl-xylotriose
-
-
0.37
-
4-O-Methyl-glucuronosyl-xylotriose
-
enzyme form CM-I
0.47
-
4-O-Methyl-glucuronosyl-xylotriose
-
enzyme form CM-II
0.53
-
aldobiouronic acid
-
-
0.42
-
aldopentaouronic acid
-
-
0.2
-
aldotetraouronic acid
-
55C
0.36
-
aldotetraouronic acid
-
-
0.28
-
aldotriouronic acid
-
-
0.77
-
glucuronosyl-xylotriose
-
enzyme form CM-I
0.82
-
glucuronosyl-xylotriose
-
enzyme form CM-II
0.36
-
O-alpha-D-glucopyranosyluronic acid-alpha-D-glucopyranosiduronic acid
-
-
-
0.13
-
p-nitrophenyl alpha-D-glucopyranosyluronic acid
-
-
0.1
-
p-nitrophenyl alpha-D-glucuronopyranoside
P96105
-
1
-
p-nitrophenyl-alpha-D-glucuronopyranoside
-
-
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
0.014
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme K288A
0.09
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme W160A
0.2
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme K360A
0.38
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme W543A
127
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme V210G
143
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, wild-type enzyme
220
-
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
-
37C, pH 7.0, mutant enzyme V210A
69.2
-
aldobiouronic acid
-
-
131.9
-
aldopentaouronic acid
-
-
54.9
-
aldotetraouronic acid
-
55C
102.5
-
aldotetraouronic acid
-
-
0.28
-
p-nitrophenyl alpha-D-glucuronopyranoside
P96105
-
0.0018
-
p-nitrophenyl-alpha-D-glucuronopyranoside
-
-
96
-
aldotriouronic acid
-
-
additional information
-
additional information
-
-
-
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
-
-
-
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
3.3
3.8
-
-
4.4
-
A3LY17, -
-
5.5
-
-
at 37C, using methylglucuronoxylose as substrate
6.3
-
Q8VP74
-
additional information
-
-
3.0-3.5, immobilized TreDCase
pH RANGE
pH RANGE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
4
-
pH 2: about 30% of maximal activity, pH 4: about 70% of maximal activity
3
5
-
pH 3.0: about 80% of maximal activity, pH 5.0: about 50% of maximal activity
3
5.8
-
about 45% of maximal activity at pH 3 and at pH 5.8
3.3
7
-
pH 3.3: about 60% of maximal activity, pH 7: about 50% of maximal activity
4
5.5
A3LY17, -
at pH 4.0 25.5% and at pH 5.5 51.6% activity
4
5.6
-
about 50% of maximal activity at pH 4.5 and 5.6
4.5
7.5
-
about 40% of maximal activity at pH 4.5 and pH 7.5
4.8
6.3
-
pH 5.8: about 80% of maximal activity, pH 6.3: about 50% of maximal activity
5
6.2
-
pH 5: about 85% of maximal activity, pH 6.2: about 65% of maximal activity
5
8
-
at least 40% of maximal activity at pH-values ranging from 5 to 8
5
8
-
pH 5: about 35% of maximal activity, pH 8: about 45% of maximal activity
5
8
Q8VP74
pH 5: 20% of maximal activity, pH 8: about 60% of maximal activity
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
35
-
-
mutant enzyme W328E/R329T/R665N
40
-
-
immobilized TreDCase
40
-
-
at pH 6.0, using methylglucuronoxylose as substrate
60
-
A3LY17, -
protein unstable at this temperature with 50% activity loss in 30 min
65
-
-
wild-type enzyme
80
-
P96105
-
TEMPERATURE RANGE
TEMPERATURE MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
20
55
-
20C: about 50% of maximal activity, 55C: about 40% of maximal activity, mutant enzyme W328E/R329T/R665N
20
60
-
20C: about 35% of maximal activity, 60C: about 60% of maximal activity
30
60
-
about 40% of maximal activity at 30C and at 60C
40
75
-
40C: about 35% of maximal activity, 75C: about 30% of maximal activity
45
65
-
45C: about 80% of maximal activity, 65C: about 85% of maximal activity
45
70
-
45C: about 35% of maximal activity, 70C: about 50% of maximal activity
60
100
-
about 45% of maximal activity at 60C and at 100C
60
70
-
40C: about 40% of maximal activity, 70C: about 90% of maximal activity, wild-type enzyme
60
90
P96105
60C: about 50% of maximal activity, 90C: about 80% of maximal activity
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
pH STABILITY
pH STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
2
4
-
immobilized TreDCase
2
4.5
-
30C, stable
3
7
-
30C, 2 h, stable
3.5
-
-
50C, in absence of substrate, inactivated in 2 h
4
12
P96105
30 min, stable between pH 4 and pH 12
4
9
-
almost no enzyme activity appears at pHs lower than 4.0 and higher than 9.0
4.5
7
-
50C, 1 h, stable
4.8
5.5
-
40C, 24 h, stable
5
11
-
room temperature, 30 min, stable
5
-
-
AguA exhibits 85% of its maximal activity at pH 5.0
5.5
-
-
40C, absence of substrate, 20% loss of activity; 50C, absence of substrate, 15 min, 79% loss of activity
5.5
-
-
50C, in absence of substrate, 58% loss of activity in 24 h
6.2
7.9
-
60C, stable for 1 h
6.6
-
-
40C, 24 h, 22% loss of activity
11.5
-
-
room temperature, 30 min, 50% loss of activity
TEMPERATURE STABILITY
TEMPERATURE STABILITY MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
10
40
-
AUH-I is stable at 10-40C, but starts to lose the activity above 40C
30
-
-
pH 4.0, 24 h, stable below
40
-
-
pH 5.5, in absence of substrate, 15 min, 20% loss of activity
40
-
-
pH 6.2-7.9, stable for 1 h
40
-
A3LY17, -
stable for at least 3 h, at optimal temperature loss of 50% activity after 30 min
45
-
-
4 h, 20% loss of activity
50
-
-
pH 4.5-7.0, 1 h, stable
50
-
-
pH 6.0, 4 h, stable
50
-
-
pH 5.5, absence of substrate, 15 min, 79% loss of activity
50
-
-
pH 3.5, in absence of substrate, inactivation in 2 h; pH 5.0, in absence of substrate, 58% loss of activity in 24 h
50
-
-
stable up to
50
-
-
in absence of substrate, 6 h, 15% loss of activity
50
-
-
pH 4.8, 24 h, 50% loss of activity
50
-
-
half-life: 50 min
50
-
-
AguA shows 54% of the maximal activity at 50C
55
75
-
partial inactivation, but thereafter the residual activity remains nearly constant for several days
55
-
Q8VP74
rapid inactivation above
60
-
-
half-life: 14 h
60
-
-
in absence of substrate, 6 h, 58% loss of activity; in absence of substrate, t1/2: 192 min
60
-
-
pH 6.2-7.9, stable for 1 h
62
-
-
half-life: 1 h
70
-
-
in absence of substrate, t1/2: 28 min
70
-
-
20 min, no less of activity
70
-
P96105
30 min, stable up to
70
-
-
20 min, wild-type enzyme and mutant enzyme W328E/R329T/R665N, about 10% loss of activity
73
-
-
melting temperature of mutant enzyme W328E/R329T/R665N is 72.9C, melting temperature of wild-type enzyme is 73.4C
73.4
-
-
denaturation at
75
-
-
20 min, 70% loss of activity
75
-
-
20 min, wild-type enzyme loses 70% of its activity, mutant enzyme W328E/R329T/R665N copletely loses activity
80
-
P96105
30 min, 10% loss of activity
90
-
P96105
30 min, complete inactivation
additional information
-
-
1 mg/ml of substrate protects against heat inactivation
additional information
-
-
below 40C, immobilized TreDCase, treatment with glutaraldehyde does not affect thermostability
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
-
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
2 enzym forms: CM-I and CM-II
-
partially purified by gel filtration
-
soluble phase onto HisTrap HP column, eluted with imidazole gradient in sodium phosphate buffer, pH 8, and 300 mM sodium chloride
Q09LY5
HiTrap column chromatography
-
Toyopearl SuperQ column chromatography, Toyopearl phenyl column chromatography, Resource Q column chromatography, and TSKgel G3000SWXL gel filtration
-
supernatant concentrated on Amicon 10 kDa cut-off membranes, anion-exchange chromatography on HiTrap DEAE-FF column with NaCl gradient in 50 mM sodium-phosphate buffer, pH 7.0, fractions between 0.2 and 0.25 M NaCl pooled, concentrated, desalted, equilibrated in 50 mM acetate buffer, pH 4.0, with 2 M (NH4)2SO4, subjected to hydrophobic interaction chromatography on Butyl-FF column, eluted with (NH4)2SO4 gradient, active fractions between 1.1 and 0.61 M (NH4)2SO4 pooled, desalted, concentrated, subjected to 2 additional anion-exchange chromatography steps on Tricorn MonoQ 5/50GL column, first equilibrated with 50 mM sodium acetate buffer, pH 4.0, eluted with NaCl gradient, then equilibrated with 50 mM sodium phosphate buffer, pH 7.0 and NaCl gradient, concentration with Microcon 10 kDa cut-off membrane filter
A3LY17, -
Ni-NTA agarose column chromatography, DEAE-Sepharose column chromatography, and Superose 12 gel filtration
B5H8Y8
recombinant enzyme
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expression in Saccharomyces cerevisiae
-
Escherichia coli BL21(DE3)pLysE, Luria-Bertani broth, 37°C, plasmid pET29-Gste-AG-his-S
Q09LY5
expression in Escherichia coli
-
overexpression in Escherichia coli using the T7 polymerase expression system
-
expressed in Escherichia coli Rosetta(DE3) cells
-
Pichia stipitis CBS 6054 grown in YNB medium, cells washed and suspended in YNB medium with a xylooligosaccharide misture and methyl-beta-xylopyranoside, 30°C, 24 h, shaker
A3LY17, -
expressed in Escherichia coli Tuner (DE3) cells
B5H8Y8
into pGEM-T Easy vector, plasmids maintained in Escherichia coli JM109
-
expression in Escherichia coli
-
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