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Information on EC 3.1.1.117 - (4-O-methyl)-D-glucuronate---lignin esterase
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EC Tree
3.1.1.117 (4-O-methyl)-D-glucuronate---lignin esteraseIUBMB Comments
The enzyme occurs in microorganisms and catalyses the cleavage of the ester bonds between glucuronoyl or 4-O-methyl-glucuronoyl groups attached to xylan and aliphatic or aromatic alcohols in lignin polymers.
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Word Map
- 3.1.1.117
-
esterases
- biofuel production
-
lignin-carbohydrate
- biotechnology
-
4-o-methyl-d-glucuronic
- glucuronoxylans
- xylans
-
cellulolytic
-
phanerochaete
-
lignocellulosic
-
schizophyllum
-
uronic
- molecular biology
-
d-glucuronic
-
saccharification
- 4-nitrophenyl
-
white-rot
-
chrysosporium
-
wood-rotting
-
sporotrichum
- cellulases
- xylanases
-
halleri
-
hemicellulases
-
jecorina
- degradation
-
hypocrea
-
hemicellulolytic
-
meglca
-
gemmifera
- synthesis
- industry
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria
Reaction Schemes
a 4-O-methyl-D-glucopyranuronate ester
+
=
+
Synonyms
4-O-methyl-glucuronoyl methylesterase, 4-O-methyl-glucuronoyl methylesterase 1, 4-O-methyl-glucuronoyl methylesterase 2, AaGE1, Acral2 1078265, AfGE, Afu6g14390, AiGE1, AmGE1, BdGE1, 
more
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
4-O-methyl-glucuronoyl methylesterase
4-O-methyl-glucuronoyl methylesterase 1
4-O-methyl-glucuronoyl methylesterase 2
AfGE
Afu6g14390
carbohydrate esterase family 15 domain protein
carbohydrate esterase family 15 protein
CE15 enzyme
Cip2
Cip2_GE
DsGE1
DsGE2
FGE
fungal CE15 enzyme
fungal GE
fungal glucuronoyl esterase
GCE
GCE1
GE Cip2
GE1
Ge2
glucuronoyl esterase
glucuronoyl esterase 1
glucuronoyl esterase 2
glucuronoyl esterase CE15
glucuronoyl methylesterase 1
glucuronoyl methylesterase 2
glucuronoyl-lignin ester hydrolase
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-
-
-
HsGE1
NcGE
PaGE1
PaGE3
PcGCE
PcGE1
PHACADRAFT_157044
PHACADRAFT_247750
PiGE1
PrGE1
ScGE
ScGE1
ScGE2
StGE1
StGE2
SuCE15A
SuCE15B
SuCE15C
TERTU_0517
THITE_2055580
THITE_2117593
TrCip2
TRIREDRAFT_123940
TtCE15A
TtGE1
TtGE2
WcGE1
additional information
4-O-methyl-glucuronoyl methylesterase
-
-
-
-
4-O-methyl-glucuronoyl methylesterase 1
UniProt
carbohydrate esterase family 15 protein
UniProt
-
carbohydrate esterase family 15 protein
UniProt
-
glucuronoyl esterase
-
-
ambiguous
-
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
a 4-O-methyl-D-glucopyranuronate ester + H2O = 4-O-methyl-D-glucuronic acid + an alcohol
-
-
-
-
a 4-O-methyl-D-glucopyranuronate ester + H2O = 4-O-methyl-D-glucuronic acid + an alcohol
The serine and histidine residues of the catalytic triad found in all solved GE structures (fungal and bacterial) are conserved in TtCE15A: Ser281 and His427, only the proposed canonical glutamate of the catalytic triad is absent (similar to MZ0003), and this position is occupied by a serine residue, Ser304. TtCE15A is fine-tuned to utilize Glu374 as the acidic residue in the catalytic mechanism, supporting the enzyme's high turnover rate, and that the utilization of the residue in this position is distinct from CE15 members exhibiting the canonical acidic residue
a 4-O-methyl-D-glucopyranuronate ester + H2O = 4-O-methyl-D-glucuronic acid + an alcohol
The serine and histidine residues of the catalytic triad found in all solved GE structures (fungal and bacterial) are conserved in TtCE15A: Ser281 and His427, only the proposed canonical glutamate of the catalytic triad is absent (similar to MZ0003), and this position is occupied by a serine residue, Ser304. TtCE15A is fine-tuned to utilize Glu374 as the acidic residue in the catalytic mechanism, supporting the enzyme's high turnover rate, and that the utilization of the residue in this position is distinct from CE15 members exhibiting the canonical acidic residue
-
-
a 4-O-methyl-D-glucopyranuronate ester + H2O = 4-O-methyl-D-glucuronic acid + an alcohol
The serine and histidine residues of the catalytic triad found in all solved GE structures (fungal and bacterial) are conserved in TtCE15A: Ser281 and His427, only the proposed canonical glutamate of the catalytic triad is absent (similar to MZ0003), and this position is occupied by a serine residue, Ser304. TtCE15A is fine-tuned to utilize Glu374 as the acidic residue in the catalytic mechanism, supporting the enzyme's high turnover rate, and that the utilization of the residue in this position is distinct from CE15 members exhibiting the canonical acidic residue
-
-
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SYSTEMATIC NAME
IUBMB Comments
(4-O-methyl)-D-glucuronate---lignin ester hydrolase
The enzyme occurs in microorganisms and catalyses the cleavage of the ester bonds between glucuronoyl or 4-O-methyl-glucuronoyl groups attached to xylan and aliphatic or aromatic alcohols in lignin polymers.
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylitol + H2O
?
3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranonurate
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
3-(4-methoxyphenyl)propan-1-ol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methanol + 3-(4-methoxyphenyl) propyl 4-O-methyl-alpha-D-glucopyranosiduronate
the substrate mimics the ester linkage between lignin and hemicellulose
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-Dglucopyranosiduronate + H2O
methanol + 3-(4-methoxyphenyl)propyl 4-O-methyl-alpha-D-glucopyranosiduronate
3-(4-methoxyphenyl)propyl-methyl-4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 3-(4-methoxyphenyl)propyl-4-O-methyl-alpha-D-glucopyranuronate
3-phenyl-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
4-nitrophenyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
metahnol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-Dglucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
4-nitrophenyl-2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
benzyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
benzyl alcohol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
benzyl methyl alpha-D-glucopyranosiduronate + H2O
benzyl alcohol + methyl alpha-D-glucopyranosiduronic acid
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
methyl (4-nitrophenyl beta-D-glucopyranoside)uronate + H2O
methanol + (4-nitrophenyl beta-D-glucopyranoside)uronate
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-1,4-beta-D-xylopyranoside + H2O
?
methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 4-O-methyl-alpha-D-glucopyranuronate
methyl beta-D-xylopyranosyl-1,4-[2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)]-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl-4-O-methyl-D-glucopyranosyluronate + H2O
methanol + 4-O-methyl-D-glucopyranosyluronic acid
-
-
-
-
?
methylx02betaD-xylopyranosyl-1,4-(3-O-beta-D-xylopyranosyl)-beta-D-xylopyranosyl-1,4-[2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)]-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
O-methyl-alpha-D-glucopyranuronate + H2O
methanol + alpha-D-glucuronic acid
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
1-(4-hydroxy-3-methoxyphenyl)-1-(alpha-D-glucuronate)-2-(2-methoxyphenoxy)-3-propanol + H2O
?
Thermothelomyces thermophilus DSM 1799
-
-
-
?
2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylitol + H2O
?
-
-
-
-
?
2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-(1->4)-beta-D-xylopyranosyl-(1->4)-D-xylitol + H2O
?
-
-
-
-
?
3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranonurate
-
-
-
?
3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranonurate
-
-
-
?
3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranonurate
-
-
-
?
3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranonurate
-
-
-
?
3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-(4-hydroxyphenyl)-propan-1-ol + 4-O-methyl-D-glucopyranonurate
-
-
-
?
3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate + H2O
?
-
-
-
?
3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate + H2O
?
-
-
-
?
3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate + H2O
?
-
-
-
?
3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate + H2O
?
-
-
-
?
3-(4-hydroxyphenyl)-1-propyl D-glucopyranosyluronate + H2O
?
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
3-(4-methoxyphenyl)propan-1-ol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
3-(4-methoxyphenyl)propan-1-ol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
-
-
-
?
3-(4-methoxyphenyl) propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
methyl 4-O-methyl-D-glucuronic acid + 3-(4-methoxyphenyl) propyl alcohol
the substrate mimics the ester linkage of 4-O-methyl-D-glucuronic acid in lignin-carbohydrate complexes (LCCs)
-
-
?
3-(4-methoxyphenyl)propyl D-glucopyranosyluronate + H2O
?
-
-
-
-
?
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
?
-
-
-
-
?
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
?
-
-
-
-
?
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-Dglucopyranosiduronate + H2O
methanol + 3-(4-methoxyphenyl)propyl 4-O-methyl-alpha-D-glucopyranosiduronate
a chromogenic substrate
-
-
?
3-(4-methoxyphenyl)propyl methyl 4-O-methyl-alpha-Dglucopyranosiduronate + H2O
methanol + 3-(4-methoxyphenyl)propyl 4-O-methyl-alpha-D-glucopyranosiduronate
a chromogenic substrate
-
-
?
3-(4-methoxyphenyl)propyl-methyl-4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 3-(4-methoxyphenyl)propyl-4-O-methyl-alpha-D-glucopyranuronate
substrate mimicking the ligninâhemicellulose linkage
-
-
?
3-(4-methoxyphenyl)propyl-methyl-4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 3-(4-methoxyphenyl)propyl-4-O-methyl-alpha-D-glucopyranuronate
substrate mimicking the ligninâhemicellulose linkage
-
-
?
3-phenyl-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenyl-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenyl-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenyl-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenyl-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenyl-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenyl-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
3-phenyl-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
3-phenyl-1-propyl 4-O-methyl-D-glucopyranuronate + H2O
3-phenylpropan-1-ol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
3-phenyl-1-propyl D-glucopyranosyluronate + H2O
?
-
-
-
?
4-nitrophenyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
metahnol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
a chromogenic substrate
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
metahnol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
a chromogenic substrate
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
Thermothelomyces thermophilus ATCC 34628
-
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
Thermothelomyces thermophilus DSM 1799
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
methanol + 4-nitrophenyl 2-O-(4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl 2-O-(methyl-4-O-methyl-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl-2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenyl-2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
Phanerochaete chrysosporium ATCC MYA-4764
-
-
-
?
4-nitrophenyl-2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
Phanerochaete chrysosporium FGSC 9002
-
-
-
?
4-nitrophenyl-2-O-(methyl-4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
?
4-nitrophenylacetate + H2O
4-nitrophenol + acetic acid
-
low activity
-
-
?
4-nitrophenylacetate + H2O
4-nitrophenol + acetic acid
-
low activity
-
-
?
4-nitrophenylacetate + H2O
4-nitrophenol + acetic acid
acetylxylan esterase activity
-
-
?
4-nitrophenylacetate + H2O
4-nitrophenol + acetic acid
-
very low activity
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Phanerochaete chrysosporium ATCC MYA-4764
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Phanerochaete chrysosporium FGSC 9002
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Thermothelomyces thermophilus DSM 1799
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer + H2O
?
-
-
-
?
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer + H2O
?
-
-
-
?
4-O-methyl-glucuronic acid gamma-linked to a lignin dimer + H2O
?
-
-
-
?
a 4-O-methyl-D-glucopyranuronate ester + H2O
4-O-methyl-D-glucuronic acid + an alcohol
-
-
-
?
a 4-O-methyl-D-glucopyranuronate ester + H2O
4-O-methyl-D-glucuronic acid + an alcohol
-
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
activity is about 30% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
Phanerochaete chrysosporium ATCC MYA-4764
activity is about 30% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
Phanerochaete chrysosporium FGSC 9002
activity is about 30% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
activity is about 30% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
activity is about 20% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
activity is about 80% compared to the activity with benzyl glucuronic acid
-
-
?
allyl glucuronic acid + H2O
prop-2-en-1-ol + glucuronic acid
activity is about 80% compared to the activity with benzyl glucuronic acid
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
moderate activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
Phanerochaete chrysosporium ATCC MYA-4764
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
Phanerochaete chrysosporium FGSC 9002
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
-
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
moderate activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
moderate activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
low activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
activity is 20% compared to activity with benzyl D-glucuronate
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
low activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
low activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
low activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
high activity
-
-
?
allyl-D-glucuronate + H2O
prop-2-en-1-ol + glucuronic acid
high activity
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl D-glucuronate + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl D-glucuronic acid ester + H2O
?
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
?
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
?
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
Thermothelomyces thermophilus BCRC 31852
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + D-glucuronic acid
Thermothelomyces thermophilus DSM 1799
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl D-glucuronic acid ester + H2O
benzyl alcohol + glucuronic acid
the application of this substrate is described (a) in a Thin Layer Chromatography (TLC) assay for qualitative activity assessment (b) a spectrophotometer-based assay useful for screening, and (c) an HPLC-based assay allowing more precise activity determinations, enabling enzyme kinetics characterization. In addition, TLC and spectrophotometric methods are less costly and time consuming, and there is no need for complicated instruments for the analysis
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
Phanerochaete chrysosporium ATCC MYA-4764
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
Phanerochaete chrysosporium FGSC 9002
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl glucuronic acid + H2O
benzyl alcohol + glucuronic acid
-
-
-
?
benzyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
benzyl alcohol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
-
-
-
?
benzyl methyl 4-O-methyl-alpha-D-glucopyranosiduronate + H2O
benzyl alcohol + methyl 4-O-methyl-alpha-D-glucopyranosiduronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
isozymes SuCE15A or SuCE15C show high activity on BnzGlcA at pH 5.5
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
isozymes SuCE15A or SuCE15C show high activity on BnzGlcA at pH 5.5
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
best substrate
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
best substrate
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
best substrate
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
best substrate
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
isozyme SlCE15A shows high activity on BnzGlcA at pH 5.5
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
Thermothelomyces thermophilus DSM 1799
-
-
-
?
benzyl-D-glucuronate + H2O
benzyl alcohol + D-glucuronic acid
best substrate
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
cinnamyl 4-O-methyl-D-glucopyranuronate + H2O
cinnamyl alcohol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
lignin-rich pellet + H2O
aldotetrauronic acids
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranosid)uronate + H2O
4-nitrophenyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranoside)uronate + H2O
methanol + (4-nitrophenyl beta-D-glucopyranoside)uronate
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranoside)uronate + H2O
methanol + (4-nitrophenyl beta-D-glucopyranoside)uronate
-
-
-
?
methyl (4-nitrophenyl beta-D-glucopyranoside)uronate + H2O
methanol + (4-nitrophenyl beta-D-glucopyranoside)uronate
-
-
-
?
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl (5-bromo-4-chloro-3-indolyl beta-D-glucopyranosid)uronate + H2O
5-bromo-4-chloro-3-indolyl beta-D-glucopyranosiduronic acid + methanol
-
-
-
?
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-1,4-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl 2-O-(methyl 4-O-methyl-alpha-D-glucopyranosyluronate)-beta-D-xylopyranosyl-1,4-beta-D-xylopyranoside + H2O
?
-
-
-
-
?
methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 4-O-methyl-alpha-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 4-O-methyl-alpha-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 4-O-methyl-alpha-D-glucopyranuronate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
methyl 4-O-methyl-alpha-D-glucopyranuronate + H2O
methanol + 4-O-methyl-alpha-D-glucopyranuronate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
methyl 4-O-methyl-D-glucopyranonate + H2O
methanol + 4-O-methyl-D-glucopyranonate
-
-
-
?
methyl 4-O-methyl-D-glucopyranonate + H2O
methanol + 4-O-methyl-D-glucopyranonate
-
-
-
?
methyl 4-O-methyl-D-glucopyranonate + H2O
methanol + 4-O-methyl-D-glucopyranonate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl 4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methylglucuronic acid
-
-
-
?
methyl 4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methylglucuronic acid
-
-
-
?
methyl 4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methylglucuronic acid
-
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
activity is about 10% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
Phanerochaete chrysosporium ATCC MYA-4764
activity is about 10% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
Phanerochaete chrysosporium FGSC 9002
activity is about 10% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
activity is about 10% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
activity isabout 5% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
activity is about 15% compared to the activity with benzyl glucuronic acid
-
-
?
methyl glucuronic acid + H2O
methanol + glucuronic acid
activity is about 15% compared to the activity with benzyl glucuronic acid
-
-
?
methyl-4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl-4-O-methyl-D-glucopyranuronate + H2O
methanol + 4-O-methyl-D-glucopyranuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
Thermothelomyces thermophilus DSM 1799
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronate
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
Phanerochaete chrysosporium ATCC MYA-4764
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
Phanerochaete chrysosporium FGSC 9002
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
-
-
-
-
?
methyl-4-O-methyl-D-glucuronate + H2O
methanol + 4-O-methyl-D-glucuronic acid
-
-
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
-
-
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
-
-
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
-
poor activity with isozyme OtCE15D
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
-
low activity
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
very low activity
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
very low activity
-
-
?
methyl-D-galacturonate + H2O
methanol + galacturonic acid
very low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
-
low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
-
-
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
-
low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
-
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
very low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
very low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
very low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
very low activity
-
-
?
methyl-D-glucuronate + H2O
methanol + glucuronic acid
low activity
-
-
?
trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate + H2O
?
-
-
-
?
trans-3-phenyl-2-propen-1-yl D-glucopyranosyluronate + H2O
?
-
-
-
?
additional information
?
-
the enzyme is active on the insoluble LCC-rich lignin fraction from birch, i.e. lignin-rich pellet (LRP), showing a clear preference for the insoluble substrate compared with smaller soluble LCC mimicking esters. The LRP fraction contains around 90% lignin and 0.24% 4-O-methyl glucuronic acid. Development of a multi-step assay for experimental determination of enzyme kinetics on the natural insoluble substrate. Product quantification relative to the response of reduced aldotetrauronic acid, products are the aldouronic acids, aldodi-(XylMeGlcA), aldotri-(Xyl2MeGlcA), and aldotetrauronic acid (Xyl3MeGlcA)
-
-
-
additional information
?
-
Lys209 plays an important role in the preference for the substrates containing 4-O-methyl group in the glucopyranose ring. The purified recombinant enzyme displays the ability to degrade the synthetic substrates mimicking the ester linkage between hemicellulose and lignin. Self-degradation of the substrates under high alkaline condition
-
-
-
additional information
?
-
-
Lys209 plays an important role in the preference for the substrates containing 4-O-methyl group in the glucopyranose ring. The purified recombinant enzyme displays the ability to degrade the synthetic substrates mimicking the ester linkage between hemicellulose and lignin. Self-degradation of the substrates under high alkaline condition
-
-
-
additional information
?
-
Lys209 plays an important role in the preference for the substrates containing 4-O-methyl group in the glucopyranose ring. The purified recombinant enzyme displays the ability to degrade the synthetic substrates mimicking the ester linkage between hemicellulose and lignin. Self-degradation of the substrates under high alkaline condition
-
-
-
additional information
?
-
-
no activity is detected with methyl-D-galacturonate, indicating that CkGE15A has a strict preference for GlcA-derived esters
-
-
-
additional information
?
-
-
methylation of the C4 hydroxyl moiety is crucial for enzymatic activity. To investigate putative lignin- and xylan-binding sites in the solved structures, docking simulations of SuCE15C with a benzyl ester of 4-O-methyl-glucuronoxylotriose (glucuronoate alpha-1,2 linked to the middle xylose residue) are performed
-
-
-
additional information
?
-
-
methylation of the C4 hydroxyl moiety is crucial for enzymatic activity. To investigate putative lignin- and xylan-binding sites in the solved structures, docking simulations of SuCE15C with a benzyl ester of 4-O-methyl-glucuronoxylotriose (glucuronoate alpha-1,2 linked to the middle xylose residue) are performed
-
-
-
additional information
?
-
the enzyme catalyze removal of all glucuronoxylan associated with lignin. This is a direct result of enzymatic cleavage of the ester bonds connecting glucuronoxylan to lignin via 4-O-methyl glucuronoyl-ester linkages
-
-
?
additional information
?
-
a lignin-enriched substrate is prepared from raw birchwood by thermal ethanol extraction, the generated lignin-rich precipitate (LRP) serves as substrate for CuGE. The chemical composition of LRP and raw birchwood is determined by acid hydrolysis and confirmes an enrichment of glucuronoyl substituted xylan and lignin with practically no structural glucan in comparison to the raw birchwood substrate. CuGE catalyzes the release of a mixture of acetylated aldouronic acids upon reaction on LRP. The enzyme shows no endoxylanase or acetyl xylan esterase activity. Glucuronoyl esterases are capable of hydrolyzing ester-linked LCCs of glucuronoxylan and lignin. LC-MS analysis shows that the product profiles contain a mixture of acetylated aldouronic acids containing 4-O-methyl-glucuronosyl (MeGlcA) ranging from DP 3 to DP 5. Substrate specificity, detailed overview
-
-
-
additional information
?
-
analysis of the interactions between CuGE and the alpha-1,2-linked 4-O-methyl-D-glucuronoyl moieties on xylo-oligomers, the binding of the 4-O-methyl-alpha-D-glucuronoyl moiety is not influenced by the nature of the attached xylo-oligosaccharide. Enzyme-substrate binding analysis, overview
-
-
-
additional information
?
-
-
analysis of the interactions between CuGE and the alpha-1,2-linked 4-O-methyl-D-glucuronoyl moieties on xylo-oligomers, the binding of the 4-O-methyl-alpha-D-glucuronoyl moiety is not influenced by the nature of the attached xylo-oligosaccharide. Enzyme-substrate binding analysis, overview
-
-
-
additional information
?
-
the enzyme is active on the insoluble LCC-rich lignin fraction from birch, i.e. lignin-rich pellet (LRP), showing a clear preference for the insoluble substrate compared with smaller soluble LCC mimicking esters. The LRP fraction contains around 90% lignin and 0.24% 4-O-methyl glucuronic acid. Development of a multi-step assay for experimental determination of enzyme kinetics on the natural insoluble substrate. Product quantification relative to the response of reduced aldotetrauronic acid, products are the aldouronic acids, aldodi-(XylMeGlcA), aldotri-(Xyl2MeGlcA), and aldotetrauronic acid (Xyl3MeGlcA)
-
-
-
additional information
?
-
UDH-coupled spectrophotometric assaying of GE enzymatic reaction, hydrolysis of BnGlcA catalyzed by GE and spectrophotometric assaying by NAD+-dependent oxidation of GlcA using uronate dehydrogenase (UDH), overview
-
-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
-
methylation of the C4 hydroxyl moiety is crucial for enzymatic activity. Isozyme OtCE15B shows lower activity compared to the other isozymes. To investigate putative lignin- and xylan-binding sites in the solved structures, docking simulations of OtCE15A with a benzyl ester of 4-O-methyl-glucuronoxylotriose (glucuronoate alpha-1,2 linked to the middle xylose residue) are performed
-
-
-
additional information
?
-
-
the enzyme is active with the glucuronoxylan oligosaccharide (XUX). The oligosaccharide is produced from beech xylan and contains the 4-O-methyl-alpha-D-glucuronate moiety. Docking study, structure analysis of enzyme OtCE15A in complex with glucuronoxylooligosaccharide 23-(4-O-methyl-alpha-D-glucuronyl)-xylotriose (commonly referred to as XUX). The structure of the enzyme with the disaccharide xylobiose reveals a surface binding site that possibly indicates a recognition mechanism for long glucuronoxylan chains
-
-
-
additional information
?
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcoholesters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcoholesters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
Phanerochaete chrysosporium ATCC MYA-4764
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
Phanerochaete chrysosporium ATCC MYA-4764
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
Phanerochaete chrysosporium ATCC MYA-4764
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
Phanerochaete chrysosporium ATCC MYA-4764
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
Phanerochaete chrysosporium ATCC MYA-4764
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
Phanerochaete chrysosporium FGSC 9002
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
Phanerochaete chrysosporium FGSC 9002
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
Phanerochaete chrysosporium FGSC 9002
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
Phanerochaete chrysosporium FGSC 9002
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
Phanerochaete chrysosporium FGSC 9002
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
the substrate and the reaction product 4-O-methyl-D-glucuronic acid are visualized with N-(1-naphthyl)ethylenediamine dihydrochloride reagent
-
-
-
additional information
?
-
UDH-coupled spectrophotometric assaying of GE enzymatic reaction, hydrolysis of BnGlcA catalyzed by GE and spectrophotometric assaying by NAD+-dependent oxidation of GlcA using uronate dehydrogenase (UDH), overview
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
the enzyme is active on the insoluble LCC-rich lignin fraction from birch, i.e. lignin-rich pellet (LRP), showing a clear preference for the insoluble substrate compared with smaller soluble LCC mimicking esters. The LRP fraction contains around 90% lignin and 0.24% 4-O-methyl glucuronic acid. Development of a multi-step assay for experimental determination of enzyme kinetics on the natural insoluble substrate. Product quantification relative to the response of reduced aldotetrauronic acid, products are the aldouronic acids, aldodi-(XylMeGlcA), aldotri-(Xyl2MeGlcA), and aldotetrauronic acid (Xyl3MeGlcA)
-
-
-
additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. The deesterification of 4-O-methyl-D-glucuronosyl residues in both substrates proceeds at a similar rate, pointing to the same or a very similar specific activity of the enzyme for high and low molecular mass substrates. 1H NMR spectra of glucuronoxylan methyl ester, overview
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
enzyme substrate specificity, overview. The glucuronoyl esterase attacks exclusively the esters of MeGlcA. The methyl ester of free or glycosidically linked MeGlcA is not hydrolysed by other carbohydrate esterases
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-
-
additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. 1H NMR spectra of glucuronoxylan methyl ester, overview
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
-
enzyme substrate specificity, overview. The glucuronoyl esterase attacks exclusively the esters of MeGlcA. The methyl ester of free or glycosidically linked MeGlcA is not hydrolysed by other carbohydrate esterases
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. 1H NMR spectra of glucuronoxylan methyl ester, overview
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. 1H NMR spectra of glucuronoxylan methyl ester, overview
-
-
-
additional information
?
-
the enzyme hydrolyses glucuronic acid esters present in LCC fractions from spruce and birch
-
-
?
additional information
?
-
-
the enzyme hydrolyses glucuronic acid esters present in LCC fractions from spruce and birch
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-
?
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
lignin-carbohydrate complexes (LCCs) fractions from spruce and birch are treated with a recombinantly produced glucuronoyl esterase (GE) originating from Acremonium alcalophilum (AaGE1). A combination of size exclusion chromatography and 31P NMR analyses of phosphitylated LCC samples, before and after AaGE1 treatment, provide evidence for cleavage of the lignin-carbohydrate (LC) ester linkages existing in wood by the enzyme. Structures of gamma and alpha ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid residues of glucuronoxylans are the proposed target bonds of enzyme AaGE1. Estimation of hydroxyl groups in LCCs before and after GE treatment. 31Phosphorous NMR and 2D HSQC NMR analysis confirming the GE activity on LC ester bonds and AaGE1 specificity, respectively
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-
-
additional information
?
-
-
lignin-carbohydrate complexes (LCCs) fractions from spruce and birch are treated with a recombinantly produced glucuronoyl esterase (GE) originating from Acremonium alcalophilum (AaGE1). A combination of size exclusion chromatography and 31P NMR analyses of phosphitylated LCC samples, before and after AaGE1 treatment, provide evidence for cleavage of the lignin-carbohydrate (LC) ester linkages existing in wood by the enzyme. Structures of gamma and alpha ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid residues of glucuronoxylans are the proposed target bonds of enzyme AaGE1. Estimation of hydroxyl groups in LCCs before and after GE treatment. 31Phosphorous NMR and 2D HSQC NMR analysis confirming the GE activity on LC ester bonds and AaGE1 specificity, respectively
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-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides. The recombinant GE from Acremonium alcalophilum reduces the molecular mass of isolated lignin-carbohydrate complexes from spruce and birch
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-
-
additional information
?
-
-
methylation of the C4 hydroxyl moiety is crucial for enzymatic activity
-
-
-
additional information
?
-
glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds, enzyme-substrate interaction analysis, two aromatic residues, Phe174 and Trp376, conserved in bacterial GEs, interact with aromatic and carbohydrate structures of these substrates in the enzyme active site, respectively. The substrate affinity decreases drastically for glucuronoate esters with smaller alcohol portions (allyl and methyl) as compared to benzyl-D-glucuronate. Poor activity with 4-nitrophenylacetate
-
-
-
additional information
?
-
-
glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds, enzyme-substrate interaction analysis, two aromatic residues, Phe174 and Trp376, conserved in bacterial GEs, interact with aromatic and carbohydrate structures of these substrates in the enzyme active site, respectively. The substrate affinity decreases drastically for glucuronoate esters with smaller alcohol portions (allyl and methyl) as compared to benzyl-D-glucuronate. Poor activity with 4-nitrophenylacetate
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds, enzyme-substrate interaction analysis, two aromatic residues, Phe174 and Trp376, conserved in bacterial GEs, interact with aromatic and carbohydrate structures of these substrates in the enzyme active site, respectively. The substrate affinity decreases drastically for glucuronoate esters with smaller alcohol portions (allyl and methyl) as compared to benzyl-D-glucuronate. Poor activity with 4-nitrophenylacetate
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
glucuronoyl esterase from Teredinibacter turnerae interacts with carbohydrates and aromatic compounds, enzyme-substrate interaction analysis, two aromatic residues, Phe174 and Trp376, conserved in bacterial GEs, interact with aromatic and carbohydrate structures of these substrates in the enzyme active site, respectively. The substrate affinity decreases drastically for glucuronoate esters with smaller alcohol portions (allyl and methyl) as compared to benzyl-D-glucuronate. Poor activity with 4-nitrophenylacetate
-
-
-
additional information
?
-
enzyme is active on substrates containing glucuronic acid methyl ester
-
-
?
additional information
?
-
-
enzyme is active on substrates containing glucuronic acid methyl ester
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-
?
additional information
?
-
no substrate: 3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate
-
-
?
additional information
?
-
-
no substrate: 3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate
-
-
?
additional information
?
-
-
the enzyme hydrolyzes the ester linkage between the 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
molecular docking of model substrates in the catalytic site of StGE2
-
-
-
additional information
?
-
-
molecular docking of model substrates in the catalytic site of StGE2
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme is active on substrates containing glucuronic acid methyl ester
-
-
-
additional information
?
-
-
the enzyme is active on substrates containing glucuronic acid methyl ester
-
-
-
additional information
?
-
Thermothelomyces thermophilus ATCC 34628
-
the enzyme hydrolyzes the ester linkage between the 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols
-
-
-
additional information
?
-
enzyme is active on substrates containing glucuronic acid methyl ester
-
-
?
additional information
?
-
the enzyme is active on substrates containing glucuronic acid methyl ester
-
-
-
additional information
?
-
no substrate: 3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate
-
-
?
additional information
?
-
molecular docking of model substrates in the catalytic site of StGE2
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
enzyme is active on substrates containing glucuronic acid methyl ester
-
-
?
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
the enzyme is active on substrates containing glucuronic acid methyl ester
-
-
-
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
no substrate: 3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate
-
-
?
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
molecular docking of model substrates in the catalytic site of StGE2
-
-
-
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
Thermothelomyces thermophilus BCRC 31852
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
Thermothelomyces thermophilus DSM 1799
enzyme is active on substrates containing glucuronic acid methyl ester
-
-
?
additional information
?
-
Thermothelomyces thermophilus DSM 1799
the enzyme is active on substrates containing glucuronic acid methyl ester
-
-
-
additional information
?
-
Thermothelomyces thermophilus DSM 1799
no substrate: 3-(4-hydroxyphenyl)-1-propyl 4-O-methyl-D-glucopyranuronate
-
-
?
additional information
?
-
Thermothelomyces thermophilus DSM 1799
molecular docking of model substrates in the catalytic site of StGE2
-
-
-
additional information
?
-
Thermothelomyces thermophilus DSM 1799
design of BnGlcA-based glucuronoyl esterase (GE) assays for different applications: a thin-layer chromatography assay for qualitative activity detection, a coupled-enzyme spectrophotometric assay that can be used for high-throughput screening or general activity determinations and a HPLC-based detection method allowing kinetic determinations. The three-level experimental procedure not merely facilitates routine, fast and simple biochemical characterizations but it can also give rise to the discovery different GEs through an extensive screening of heterologous genomic and metagenomic expression libraries
-
-
-
additional information
?
-
Thermothelomyces thermophilus DSM 1799
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
the enzyme is slightly active on the insoluble LCC-rich lignin fraction from birch, i.e. lignin-rich pellet (LRP), showing a clear preference for the insoluble substrate compared with smaller soluble LCC mimicking esters. The LRP fraction contains around 90% lignin and 0.24% 4-O-methyl glucuronic acid. Development of a multi-step assay for experimental determination of enzyme kinetics on the natural insoluble substrate. Product quantification relative to the response of reduced aldotetrauronic acid, products are the aldouronic acids, aldodi-(XylMeGlcA), aldotri-(Xyl2MeGlcA), and aldotetrauronic acid (Xyl3MeGlcA). TtGE shows low overall activity
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2
-
-
-
additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. 1H NMR spectra of glucuronoxylan methyl ester, overview
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
two substrates of glucuronoyl esterase are utilized, substrate I: methyl ester of 4-O-methyl-D-glucuronic acid; substrate II: methyl ester of 4-O-methyl-D-glucuronic acid linked alpha-1,2 to 4-nitrophenyl-beta-D-xylopyranoside
-
-
-
additional information
?
-
-
two substrates of glucuronoyl esterase are utilized, substrate I: methyl ester of 4-O-methyl-D-glucuronic acid; substrate II: methyl ester of 4-O-methyl-D-glucuronic acid linked alpha-1,2 to 4-nitrophenyl-beta-D-xylopyranoside
-
-
-
additional information
?
-
substrate preparation, beechwood glucuronoxylan, isolated by alkaline extraction from delignified holocellulose, is converted to its methyl ester. 1H NMR spectra of glucuronoxylan methyl ester, overview
-
-
-
additional information
?
-
two substrates of glucuronoyl esterase are utilized, substrate I: methyl ester of 4-O-methyl-D-glucuronic acid; substrate II: methyl ester of 4-O-methyl-D-glucuronic acid linked alpha-1,2 to 4-nitrophenyl-beta-D-xylopyranoside
-
-
-
additional information
?
-
the enzyme GE enzymes are active on alkyl and alkyl aryl alcohol esters of MeGlcA and GlcA or their glycosides. The GEs do not differentiate esters of alpha- or beta-glucuronides
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuronoxylan methyl ester + H2O
4-O-methyl-D-glucuronoxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Phanerochaete chrysosporium ATCC MYA-4764
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Phanerochaete chrysosporium FGSC 9002
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Thermothelomyces thermophilus BCRC 31852
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
Thermothelomyces thermophilus DSM 1799
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
4-O-methyl-D-glucuroxylan methyl ester + H2O
4-O-methyl-D-glucuroxylan + methanol
-
-
-
?
a 4-O-methyl-D-glucopyranuronate ester + H2O
4-O-methyl-D-glucuronic acid + an alcohol
-
-
-
?
a 4-O-methyl-D-glucopyranuronate ester + H2O
4-O-methyl-D-glucuronic acid + an alcohol
-
-
-
?
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme cleaves the ester linkage between lignin alcohols and xylan-bound 4-O-methyl-D-glucuronic acid of hemicellulose
-
-
-
additional information
?
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
the enzyme can target ester linkages that contribute to lignin-carbohydrate complexes that form in plant cell walls. Glucuronoxylan is characterized by a beta-1,4 linked xylose backbone that can be substituted by alpha-(1,2)-glucopyranosyl uronic acid (GlcA) or 4-O-methyl-alpha-D-glucopyranosyl uronic acid (MeGlcA) side groups. In gymnosperms, glucuronoxylan can be substituted with alpha-(1,2)-L-arabinose, while glucuronoxylans in angiosperms is acetylated
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
Phanerochaete chrysosporium ATCC MYA-4764
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
Phanerochaete chrysosporium FGSC 9002
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
the enzyme hydrolyzes the ester linkage between the 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols
-
-
-
additional information
?
-
Thermothelomyces thermophilus ATCC 34628
-
the enzyme hydrolyzes the ester linkage between the 4-O-methyl-D-glucuronic acid of glucuronoxylan and lignin alcohols
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
additional information
?
-
in nature, the enzyme hydrolyses ester bonds between aliphatic alcohols in lignin and the 4-O-methyl-D-glucuronic acid side chains of xylan
-
-
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
additional information
additional information
the enzyme is not affected by Zn2+ at 1 mM. AfGE activity is not affected by EDTA, indicating that this enzyme is not a metalloenzyme
additional information
-
the enzyme is not affected by Zn2+ at 1 mM. AfGE activity is not affected by EDTA, indicating that this enzyme is not a metalloenzyme
additional information
divalent metal ions, such as Mg2+ and Ca2+, are not necessary for the enzyme to exert its activity
additional information
poor effects on enzyme activity at 1 mM by Mn2+ and Fe2+, and by 5 mM EDTA, 10 mM acetic anhydride, 10 mM ascorbic acid, and 10 mM glycerol
additional information
-
poor effects on enzyme activity at 1 mM by Mn2+ and Fe2+, and by 5 mM EDTA, 10 mM acetic anhydride, 10 mM ascorbic acid, and 10 mM glycerol
additional information
divalent metal ions, such as Mg2+ and Ca2+, are not necessary for the enzyme to exert its activity
additional information
-
the enzyme does not loose activity on addition of 1 mM EDTA as an evidence that it is not a metal-dependent enzyme
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
dimethyl sulfoxide
10 mM, 14% loss of activity; 16% inhibition at 10 mM
reduced 23-(4-O-methyl-D-glucuronyl)-alpha-D-xylotetraitol
XUXXR, inhibits the wild-type, mutant F174D, and mutant F174A, but not mutant W376A
-
2-mercaptoethanol
10 mM, 16% loss of activity; 16% inhibition at 10 mM
EDTA
10 mM, 30°C, 20 min, about 15% loss of activity; 15% inhibition at 10 mM
EDTA
10 mM, 30°C, 20 min, about 15% loss of activity; 15% inhibition at 10 mM
glycerol
46% inhibition at 5% glycerol; 5%, 30°C, 20 min, about 45% loss of activity
glycerol
46% inhibition at 5% glycerol; 5%, 30°C, 20 min, about 45% loss of activity
imidazole
5 mM, 30°C, 20 min, about 30% loss of activity
PMSF