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
LITERATURE
an alpha-D-glucuronoside + H2O = an alcohol + D-glucuronate
show the reaction diagram
-
-
-
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
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
COMMENTARY
LITERATURE
(4-O-methyl)-alpha-glucuronidase
-
-
-
-
4-O-methylglucuronidase
-
-
-
-
Agu115
Schizophyllum commune ATCC 38548
-
-
-
AguA
Geobacillus stearothermophilus T-6
-
-
-
AguA
Rasamsonia 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
-
-
alpha-glucuronidase
-
amylouronate hydrolase-I
-
-
amylouronate hydrolase-I
-
-
-
Aryl alpha-glucuronidase
-
-
-
-
GH115 glucuronidase
-
GH67 alpha-glucuronidase
-
-
GH67 alpha-glucuronidase
-
-
-
GH67 alpha-glucuronidase
-
-
GLRI
-
-
-
-
glucuronidase, alpha-
-
-
-
-
non-xylanolytic alpha-glucuronidase
-
p-nitrophenyl alpha-D-glucuronide-hydrolyzing enzyme
-
-
-
-
PNP-GAase
-
-
-
-
TreDCase
-
-
CAS REGISTRY NUMBER
COMMENTARY
37259-81-7
-
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
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
Clostridium stercorarium
-
-
-
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
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
strain CBS 814.70
-
-
Manually annotated by BRENDA team
Rasamsonia emersonii CBS 814.70
strain CBS 814.70
-
-
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 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
RUT C-30
-
-
Manually annotated by BRENDA team
strain RUT C-30
-
-
Manually annotated by BRENDA team
strain RUT C-30
-
-
Manually annotated by BRENDA team
Tyromyces palustris
-
-
-
Manually annotated by BRENDA team
gene deg75-AG
-
-
Manually annotated by BRENDA team
gene rum630-AG, isolated from a mixed population of microorganisms from rumen
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
-
the enzyme is a member of the family GH 115
evolution
-
the enzyme is classified in family 67 of the glycosyl hydrolases
evolution
the enzyme is a member of the glycoside hydrolase family 115, GH115
evolution
-
the enzyme is classified in family 67 of the glycosyl hydrolases
-
metabolism
-
the enzyme acts in synergy with endoxylanases and other xylanolytic enzymes in the biodegradation of xylan
physiological function
-
alpha-glucuronidase enzymes play an essential role in the full enzymatic hydrolysis of hemicellulose
metabolism
-
the enzyme acts in synergy with endoxylanases and other xylanolytic enzymes in the biodegradation of xylan
-
additional information
-
the enzyme binds strongly to cellulose, thus it likely possesses a carbohydrate binding module
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 enzyme protein sequence contains two highly conserved amino acids, D43 and E462, that are implicated as critical catalytic residues
additional information
-
the enzyme binds strongly to cellulose, thus it likely possesses a carbohydrate binding module
-
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT
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
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
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
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
-
-
?
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
-
-
-
-
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-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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
-
-
-
-
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
Clostridium stercorarium
-
-
-
-
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
Aspergillus niger 5-16
-
-
-
-
4-O-methyl-glucuronosyl-xylotriose + H2O
4-O-methyl-glucuronate + xylotriose
show the reaction diagram
-
-
-
-
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
-
-
-
?
aldobiouroniuc acid + H2O
?
show the reaction diagram
Aureobasidium pullulans, Aureobasidium pullulans NRRL Y-2311-1
-
-
-
-
?
aldohexaouronic acid + H2O
?
show the reaction diagram
-
-
-
-
?
aldohexaouronic 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
-
-
-
?
aldopentaouronic acid + H2O
?
show the reaction diagram
Aureobasidium pullulans NRRL Y-2311-1
-
-
-
-
?
aldopentaouronic acid + H2O
?
show the reaction diagram
Rasamsonia emersonii CBS 814.70
-
-
-
-
?
aldopentaouronic acid + H2O
4-O-methyl-D-glucuronic acid + Xylbeta(1-4)Xylbeta(1-4)Xylbeta(1-4)Xyl 2
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
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
-
-
-
?
aldotetraouronic acid + H2O
?
show the reaction diagram
Geobacillus stearothermophilus T-6
-
-
-
-
?
aldotetraouronic acid + H2O
?
show the reaction diagram
Rasamsonia emersonii CBS 814.70
-
-
-
-
?
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
-
-
-
-
?
aldotriouronic acid + H2O
?
show the reaction diagram
-
-
-
?
aldotriouronic acid + H2O
?
show the reaction diagram
Schizophyllum commune ATCC 38548
-
-
-
-
?
aldouronic acid + H2O
D-xylose + ?
show the reaction diagram
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
?
show the reaction diagram
-
-
-
?
beechwood xylan + H2O
4-O-methyl-D-glucuronic acid + D-glucuronic acid
show the reaction diagram
-
-
?
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
?
show the reaction diagram
-
-
-
-
?
birchwood xylan + H2O
?
show the reaction diagram
-
-
-
?
birchwood xylan + H2O
?
show the reaction diagram
-
-
release of reduced sugar
-
?
birchwood xylan + H2O
4-O-methyl-D-glucuronic acid + D-glucuronic acid
show the reaction diagram
-
-
?
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
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-glucuronide + H2O
p-nitrophenol + D-glucuronate
show the reaction diagram
-
-
-
-
p-nitrophenyl alpha-D-glucuronopyranoside + H2O
p-nitrophenol + D-glucuronate
show the reaction diagram
-
-
?
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
?
-
Thermoanaerobacterium saccharolyticum, Clostridium stercorarium
-
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
?
-
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
?
-
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
?
-
-
alpha-glucuronidases act on xylan side-chains and release methyl glucuronic acid residues. The enzyme is active on xylooligosaccharides generated from birchwood glucuronoxylan by a family 10 endoxylanase and on a mixture of aldouronic acids. No activity with birchwood glucuronoxylan
-
-
-
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
-
-
-
additional information
?
-
-
the enzyme functions synergistically with a GH10 endoxylanase enzyme to hydrolyze the substrate
-
-
-
additional information
?
-
-
the enzyme functions synergistically with xylanase in the hydrolysis of xylan substrate. The main products of the hydrolysis reaction are xylotriose, xylotetraose, and xylopentaose
-
-
-
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
?
-
Bacteroides sp. J-37
-
no activity with baicalin
-
-
-
additional information
?
-
-
alpha-glucuronidases act on xylan side-chains and release methyl glucuronic acid residues. The enzyme is active on xylooligosaccharides generated from birchwood glucuronoxylan by a family 10 endoxylanase and on a mixture of aldouronic acids. No activity with birchwood glucuronoxylan
-
-
-
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
-
-
-
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
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
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
?
-
B3PC73
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
?
-
A7M022
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
?
-
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
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
Mn2+
-
17% activation at 1 mM
Na+
-
2 mM, slight activation
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
4-O-Methyl-D-glucuronic acid
-
-
Ag+
-
1 mM, 90% inhibition
Ag+
-
1 mM, 58% inhibition
Ca2+
-
14% inhibition at 1 mM
Cd2+
-
1 mM, strong inhibition
Cu2+
-
1 mM, strong inhibition
Cu2+
-
0.1 mM, complete inhibition
Cu2+
-
1 mM, complete inhibition
CuCl2
Clostridium stercorarium, Thermoanaerobacterium saccharolyticum
-
-
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+
-
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
PCMB
-
-
SDS
-
2 mM, 48% inhibition
Zn2+
-
1 mM, strong inhibition
Zn2+
-
1 mM, 55% inhibition
Zn2+
-
1 mM, 43% inhibition
ZnCl2
Clostridium stercorarium
-
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
2-mercaptoethanol
maximal activation at 150 mM
NAD+
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
maximal activation at 0.6 mM, 15% of the activation with 2-mercaptoethanol
additional information
-
glutaraldehyde stabilizes
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
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
-
-
0.4
beechwood xylan
recombinant wild-type enzyme, pH 6.5, 37C
-
0.9
beechwood xylan
recombinant wild-type enzyme, pH 6.5, 37C
-
0.3
birchwood xylan
recombinant wild-type enzyme, pH 6.5, 37C, GH30 glucuronoxylan-specific xylanase treated substrate
-
1.1
birchwood xylan
recombinant wild-type enzyme, pH 6.5, 37C, GH30 glucuronoxylan-specific xylanase treated substrate
-
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
-
1
p-nitrophenyl-alpha-D-glucuronopyranoside
-
-
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
Cellvibrio japonicus
-
37C, pH 7.0, mutant enzyme K288A
0.09
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
Cellvibrio japonicus
-
37C, pH 7.0, mutant enzyme W160A
0.2
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
Cellvibrio japonicus
-
37C, pH 7.0, mutant enzyme K360A
0.38
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
Cellvibrio japonicus
-
37C, pH 7.0, mutant enzyme W543A
127
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
Cellvibrio japonicus
-
37C, pH 7.0, mutant enzyme V210G
143
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
Cellvibrio japonicus
-
37C, pH 7.0, wild-type enzyme
220
4-nitrophenyl-2-O-(4-O-methyl-alpha-D-glucuronosyl)-beta-D-xylopyranoside
Cellvibrio japonicus
-
37C, pH 7.0, mutant enzyme V210A
69.2
aldobiouronic acid
Cellvibrio japonicus
-
-
131.9
aldopentaouronic acid
Cellvibrio japonicus
-
-
54.9
aldotetraouronic acid
Geobacillus stearothermophilus
-
55C
102.5
aldotetraouronic acid
Cellvibrio japonicus
-
-
96
aldotriouronic acid
Cellvibrio japonicus
-
-
11.6
beechwood xylan
Bacteroides ovatus
A7M022
recombinant wild-type enzyme, pH 6.5, 37C
-
13.95
beechwood xylan
Bacteroides ovatus
A7M022
recombinant wild-type enzyme, pH 6.5, 37C
-
11.08
birchwood xylan
Bacteroides ovatus
A7M022
recombinant wild-type enzyme, pH 6.5, 37C, GH30 glucuronoxylan-specific xylanase treated substrate
-
0.28
p-nitrophenyl alpha-D-glucuronopyranoside
Thermotoga maritima
P96105
-
0.0018
p-nitrophenyl-alpha-D-glucuronopyranoside
Thermotoga maritima
-
-
14.37
birchwood xylan
Bacteroides ovatus
A7M022
recombinant wild-type enzyme, pH 6.5, 37C, GH30 glucuronoxylan-specific xylanase treated substrate
-
additional information
additional information
Thermoanaerobacterium sp.
-
-
-
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
15.5
beechwood xylan
Bacteroides ovatus
A7M022
recombinant wild-type enzyme, pH 6.5, 37C
11539
119
beechwood xylan
Bacteroides ovatus
A7M022
recombinant wild-type enzyme, pH 6.5, 37C
11539
13.06
birchwood xylan
Bacteroides ovatus
A7M022
recombinant wild-type enzyme, pH 6.5, 37C, GH30 glucuronoxylan-specific xylanase treated substrate
1733
36.95
birchwood xylan
Bacteroides ovatus
A7M022
recombinant wild-type enzyme, pH 6.5, 37C, GH30 glucuronoxylan-specific xylanase treated substrate
1733
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
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]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
0.07
-
crude extract
0.29
-
recombinant His-tagged enzyme from Pichia pastoris, pH 5.0, 28C
1.09
-
fungus native culture supernatant, pH 5.0, 28C
1.647
Clostridium stercorarium
-
-
2.8
-
after 41.5fold purification
11.7
-
purified recombinant enzyme, pH 8.0, 45C
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 RANGE
ORGANISM
UNIPROT
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
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
Clostridium stercorarium, Thermoanaerobacterium saccharolyticum
-
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
pH 5: 20% of maximal activity, pH 8: about 60% of maximal activity
5.5 - 9.5
-
activity range, profile overview
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
35
-
mutant enzyme W328E/R329T/R665N
40
-
immobilized TreDCase
40
-
at pH 6.0, using methylglucuronoxylose as substrate
60
Clostridium stercorarium
-
-
60
protein unstable at this temperature with 50% activity loss in 30 min
65
-
wild-type enzyme
TEMPERATURE RANGE
ORGANISM
UNIPROT
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
30 - 60
-
activity range, profile overview
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
60C: about 50% of maximal activity, 90C: about 80% of maximal activity
pI VALUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
4
isoelectrofocusing on Multiphor II system using SEVALYT PRECOTES gels and markers from 3-10
4.6
calculated from sequence
5.34
-
calculated from sequence
6.1
-
sequence analysis
SOURCE TISSUE
ORGANISM
UNIPROT
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
additional information
-
growth substrate is birchwood xylan
Manually annotated by BRENDA team
additional information
-
growth substrate is birchwood xylan
-
Manually annotated by BRENDA team
PDB
SCOP
CATH
ORGANISM
UNIPROT
Thermotoga maritima (strain ATCC 43589 / MSB8 / DSM 3109 / JCM 10099)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
80000
-
-
26102
91600
-
sequence analysis
679583
91730
-
recombinant mature enzyme, sequence calculation
731869
100000
-
-
26101
100000 - 300000
-
MW ranging from 100000 to 300000, the fraction with the highest activity has a MW of 103000, gel filtration
26104
115000
-
native AUH-I, gel filtration
703044
118000
-
gel filtration
26103
118000
-
gel filtration
26107
120000
-
gel filtration
664379
120000
SDS-PAGE with 2 sets of protein markers: Fermentas no. SM0431, SERVA no. 39216
697944
124000
Clostridium stercorarium
-
gel filtration
26103
130000
-
gel filtration, native PAGE
26108
150000
-
gel filtration
26100
150000
gel filtration
665367
160000
-
gel filtration
26101
161000
-
gel filtration
664345
180000
-
gel filtration
26106, 26111
199000
analytical ultracentrifugation, recombinant wild-type enzyme
732167
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
?
-
x * 91000, SDS-PAGE
?
-
x * 97000, SDS-PAGE
?
-
x * 78480, calculated from sequence
?
-
x * 91000, calculated from sequence
?
x * 120000, SDS-PAGE
?
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
-
?
-
x * 91000, SDS-PAGE
-
dimer
Clostridium stercorarium
-
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
-
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
-
homodimer
2 * 85000, about, sequence calculation
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
-
additional information
the enzyme consists of four distinct domains, which are connected by extended loops, structure overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
twenty putative N-glycosylation sites and four O-glycosylation sites
additional information
Rasamsonia emersonii CBS 814.70
-
twenty putative N-glycosylation sites and four O-glycosylation sites
-
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
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
pH STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
2 - 4
-
immobilized TreDCase
680401
2 - 4.5
-
30C, stable
664379
3 - 7
-
30C, 2 h, stable
26106
3.5
-
50C, in absence of substrate, inactivated in 2 h
26105
4 - 12
30 min, stable between pH 4 and pH 12
664349
4 - 9
-
almost no enzyme activity appears at pHs lower than 4.0 and higher than 9.0
703044
4.5 - 7
-
50C, 1 h, stable
26100
4.8 - 5.5
-
40C, 24 h, stable
26109
5
-
AguA exhibits 85% of its maximal activity at pH 5.0
701796
5 - 11
-
room temperature, 30 min, stable
664926
5.5
-
40C, absence of substrate, 20% loss of activity; 50C, absence of substrate, 15 min, 79% loss of activity
26104
5.5
-
50C, in absence of substrate, 58% loss of activity in 24 h
26105
6.2 - 7.9
-
60C, stable for 1 h
26108
6.6
-
40C, 24 h, 22% loss of activity
26109
11.5
-
room temperature, 30 min, 50% loss of activity
664926
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
10 - 40
-
AUH-I is stable at 10-40C, but starts to lose the activity above 40C
703044
30
-
pH 4.0, 24 h, stable below
664379
40
-
pH 5.5, in absence of substrate, 15 min, 20% loss of activity
26104
40
-
pH 6.2-7.9, stable for 1 h
26109
40
stable for at least 3 h, at optimal temperature loss of 50% activity after 30 min
697944
45
-
4 h, 20% loss of activity
664345
50
-
pH 4.5-7.0, 1 h, stable
26100
50
Clostridium stercorarium
-
pH 6.0, 4 h, stable
26103
50
-
pH 5.5, absence of substrate, 15 min, 79% loss of activity
26104
50
-
-
26105
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
26105
50
-
stable up to
26106
50
-
in absence of substrate, 6 h, 15% loss of activity
26107
50
-
pH 4.8, 24 h, 50% loss of activity
26109
50
-
half-life: 50 min
664345
50
-
AguA shows 54% of the maximal activity at 50C
701796
55
rapid inactivation above
665367
55 - 75
-
partial inactivation, but thereafter the residual activity remains nearly constant for several days
26110
60
Clostridium stercorarium
-
half-life: 14 h
26103
60
-
half-life: 2-3 h
26103
60
-
in absence of substrate, 6 h, 58% loss of activity; in absence of substrate, t1/2: 192 min
26107
60
-
pH 6.2-7.9, stable for 1 h
26108
62
-
half-life: 1 h
26108
70
-
in absence of substrate, t1/2: 28 min
26107
70
-
20 min, no less of activity
646735
70
30 min, stable up to
664349
70
-
20 min, wild-type enzyme and mutant enzyme W328E/R329T/R665N, about 10% loss of activity
665378
73
-
melting temperature of mutant enzyme W328E/R329T/R665N is 72.9C, melting temperature of wild-type enzyme is 73.4C
665378
73.4
-
denaturation at
646735
75
-
20 min, 70% loss of activity
646735
75
-
20 min, wild-type enzyme loses 70% of its activity, mutant enzyme W328E/R329T/R665N copletely loses activity
665378
80
30 min, 10% loss of activity
664349
90
30 min, complete inactivation
664349
additional information
-
1 mg/ml of substrate protects against heat inactivation
26107
additional information
-
below 40C, immobilized TreDCase, treatment with glutaraldehyde does not affect thermostability
680401
GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
susceptible to proteinase attack, inactivation by trypsin is similar to the inactivation rate for the intracellular enzyme malate dehydrogenase
STORAGE STABILITY
ORGANISM
UNIPROT
LITERATURE
-18C, 4 months, complete inactivation
-
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
recombinant His-tagged enzyme from Pichia pastoris by nickel affinity chromatography
-
2 enzym forms: CM-I and CM-II
-
partially purified by gel filtration
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3) to homogeneity by immobilized metal ion affinity chromatography and gel filtration
-
Clostridium stercorarium
-
soluble phase onto HisTrap HP column, eluted with imidazole gradient in sodium phosphate buffer, pH 8, and 300 mM sodium chloride
HiTrap column chromatography
-
Toyopearl SuperQ column chromatography, Toyopearl phenyl column chromatography, Resource Q column chromatography, and TSKgel G3000SWXL gel filtration
-
recombinant enzyme from Saccharomyces cerevisiae strain MH1000pbk by ultrafiltration
-
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
Ni-NTA agarose column chromatography, DEAE-Sepharose column chromatography, and Superose 12 gel filtration
recombinant enzyme
-
recombinant His6-tagged enzyme from Escherichia coli strain BL21(DE3)pLysE by immobilized metal affinity chromatography and gell filtration
-
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
from strain A1163, DNA and amino acid sequence determination and analysis, sequence comparisons, recombinant expression of His-tagged enzyme in Pichia pastoris
-
expression in Saccharomyces cerevisiae
-
recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)
Escherichia coli BL21(DE3)pLysE, Luria-Bertani broth, 37°C, plasmid pET29-Gste-AG-his-S
expression in Escherichia coli
-
overexpression in Escherichia coli using the T7 polymerase expression system
-
expressed in Escherichia coli Rosetta(DE3) cells
-
into pGEM-T Easy vector, plasmids maintained in Escherichia coli JM109
-
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
recombinant expression in Saccharomyces cerevisiae strain MH1000pbk, optimisation and scale-up of enzyme production in aerobic fed-batch culture with constant growth rate, strain growth parameters at at 30C and pH 5.5, and growth and production profiles , overview. The enzyme is secreted into the culture supernatant
-
expressed in Escherichia coli Tuner (DE3) cells
expression in Escherichia coli
-
gene deg75-AG, DNA and amino acid sequence determination and analysis, recombinant expression of His6-tagged enzyme in Escherichia coli strain BL21(DE3)pLysE
-
the gene is isolated from a rumen metagenomic library
-
ENGINEERING
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
D332A
site-directed mutagenesis, inactive mutant
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
H275A/H422A
site-directed mutagenesis, inactive mutant
H422A
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
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
-
K374A
site-directed mutagenesis, the mutant shows highly reduced activity compared to the wild-type enzyme
additional information
deletion of C-terminal residues 1-526, 1-639, and 1-665 results in inactive enzyme mutants
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
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
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
-
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
-
synthesis
-
hydrolysis of amylouronate to glucuronate by AUH-I
synthesis
-
hydrolysis of amylouronate to glucuronate by AUH-I
-
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
-
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
-
additional information
-
immobilized enzyme is effective in high yield production of D-glucuronic acid