Information on EC 3.2.1.182 - 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase

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The expected taxonomic range for this enzyme is: Eukaryota

EC NUMBER
COMMENTARY hide
3.2.1.182
-
RECOMMENDED NAME
GeneOntology No.
4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl glucoside beta-D-glucosidase
-
REACTION
REACTION DIAGRAM
COMMENTARY hide
ORGANISM
UNIPROT
LITERATURE
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside + H2O = 2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one + D-glucose
show the reaction diagram
(2)
-
-
-
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside + H2O = 2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + D-glucose
show the reaction diagram
(1)
-
-
-
PATHWAY
BRENDA Link
KEGG Link
MetaCyc Link
DIMBOA-glucoside activation
-
-
SYSTEMATIC NAME
IUBMB Comments
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside beta-D-glucosidase
The enzyme from Triticum aestivum (wheat) has a higher affinity for DIMBOA glucoside than DIBOA glucoside. With Secale cereale (rye) the preference is reversed.
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
-
-
-
Manually annotated by BRENDA team
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
evolution
-
the enzyme belongs to the glycoside hydrolase family 1, GH1, phylogenetic analysis, overview
metabolism
-
the enzyme is involved in the benzoxazinoid pathway, overview
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside + H2O
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-ol + D-glucose
show the reaction diagram
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside + H2O
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-ol + D-glucose
show the reaction diagram
2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one beta-D-glucopyranoside + H2O
2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one + beta-D-glucose
show the reaction diagram
-
the maximum activity with DIMBOA-Glc is 10times higher in shoots and 7times higher in roots than that with DIBOA-Glc
-
-
?
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one beta-D-glucopyranoside + H2O
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + beta-D-glucose
show the reaction diagram
-
the maximum activity with DIMBOA-Glc is 10times higher in shoots and 7times higher in roots than that with DIBOA-Glc
-
-
?
2-hydroxy-1,4-benzoxazin-3-one-beta-D-glucoside + H2O
2-hydroxy-1,4-benzoxazin-3-one + beta-D-glucose
show the reaction diagram
-
-
-
-
?
2-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside + H2O
2-hydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one + beta-D-glucose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-glucopyranoside + H2O
2-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
2-nitrophenyl beta-D-glucoside + H2O
2-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-hydroxy-3-oxo-3,4,dihydro-2H-1,4,benzoxazin-2-yl beta-D-gluco-pyranoside + H2O
2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one + beta-D-glucose
show the reaction diagram
-
-
-
?
4-methylumbelliferyl-beta-D-glucoside + H2O
4-methylumbelliferone + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-fucoside + H2O
4-nitrophenol + beta-D-fucose
show the reaction diagram
4-nitrophenyl beta-D-galactoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
4-nitrophenyl beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
4-nitrophenyl beta-D-xylopyranoside + H2O
4-nitrophenol + beta-D-xylose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + beta-D-xylose
show the reaction diagram
4-nitrophenyl-beta-D-cellobioside + H2O
4-nitrophenol + cellobiose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-fucopyranoside + H2O
4-nitrophenol + beta-D-fucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-galactopyranoside + H2O
4-nitrophenol + beta-D-galactose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-glucopyranoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
4-nitrophenyl-beta-D-mannopyranoside + H2O
4-nitrophenol + beta-D-mannose
show the reaction diagram
-
-
-
-
?
7-methoxy-3-oxo-3,4-dihydro-2H-1,4 benzoxazin-2-yl beta-D-glucopyranoside + H2O
2-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4 benzoxazin + beta-D-glucose
show the reaction diagram
-
-
-
-
?
dhurrin + H2O
?
show the reaction diagram
-
-
-
-
?
DIBOA beta-D-glucoside + H2O
DIBOA + beta-D-glucose
show the reaction diagram
-
-
-
-
?
DIBOA-beta-D-glucoside + H2O
DIBOA + beta-D-glucose
show the reaction diagram
-
TaGlu1b hydrolyzes DIMBOA-Glc much better than DIBOA-Glc
-
-
?
DIBOA-glucoside + H2O
DIBOA + beta-D-glucose
show the reaction diagram
DIMBOA beta-D-glucoside + H2O
DIMBOA + beta-D-glucose
show the reaction diagram
-
-
-
-
?
DIMBOA-beta-D-glucoside + H2O
DIMBOA + beta-D-glucose
show the reaction diagram
-
TaGlu1b hydrolyzes DIMBOA-Glc much better than DIBOA-Glc
-
-
?
DIMBOA-glucoside + H2O
DIMBOA + beta-D-glucose
show the reaction diagram
esculin + H2O
esculetin + beta-D-glucose
show the reaction diagram
genistin + H2O
?
show the reaction diagram
-
-
-
?
n-octyl-beta-D-glucopyranoside + H2O
octanol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
salicin + H2O
?
show the reaction diagram
-
-
-
-
?
NATURAL SUBSTRATES
NATURAL PRODUCTS
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside + H2O
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-ol + D-glucose
show the reaction diagram
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside + H2O
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-ol + D-glucose
show the reaction diagram
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
Ag+
-
0.2 mM, complete inhibition
Cu2+
-
0.5 mM, strong inhibition
Fe2+
-
0.5 mM, inhibits activity
Mg2+
-
0.5 mM, inhibits activity
Mn2+
-
0.5 mM, inhibits activity
Zn2+
-
0.5 mM, inhibits activity
INHIBITORS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-(1-(4-(2-cyanophenyl)benzyl-1H-indol-3-yl),2,4-dihydro-1H-benzo(d)(1,3))oxazine
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slight inhibition
-
2-(1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
-
-
-
2-(2-butyl-4-chloro-1H-imidazol-5-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
-
-
-
2-(2-methyl-1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
-
-
-
2-fluoro-2-deoxy-beta-D-glucose
3-(2,4-dihydro-1H-benzo[d][1,3]oxazin-2-yl)-4H-chromen-4-one
-
slight inhibition
-
3-(6-chloro-2,4-dihydro-1H-benzo[d][1,3]oxazin-2-yl)-4H-chromen-4-one
-
-
-
3-(6-methyl-2,4-dihydro-1H-benzo[d][1,3]oxazin-2-yl)-4H-chromen-4-one
-
slight inhibition
-
4-(2,4-dihydro-1H-benzo[d][1,3]oxazin-2-yl)phenol
-
-
-
4-(7-chloro-2,4-dihydro-1H-benzo[d][1,3]oxazin-2-yl)phenol
-
anti-hyperglycemic effect via glucose uptake inhibition by the inhibitor in the starved rat model
-
4-Methylumbelliferone
-
-
4-nitrophenol
-
-
6-chloro-2-(2-phenyl-1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
-
-
-
6-methyl-2-(2-methyl-1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
-
-
-
6-methyl-2-(2-phenyl-1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
-
-
-
7-chloro-2-(1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
-
-
-
acarbose
-
-
castanospermine
-
-
D-gluconic acid lactone
-
-
Dhurrin
-
-
DIMBOA
-
-
additional information
-
synthesis of a library of 1,3-benzoxazine scaffold based aglycones by using 2-aminobenzyl alcohols and aldehydes from one-pot reaction in a chloroacetic acid catalytic system via aerobic oxidative synthesis, inhibitory potencies of the compounds, molecular docking studies, overview
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
4.6
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside
-
recombinant enzyme, pH and temperature not specified in the publication
28.4
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside
-
recombinant enzyme, pH and temperature not specified in the publication
1.34
2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one beta-D-glucopyranoside
-
pH 5.5, 30C
0.27
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one beta-D-glucopyranoside
-
pH 5.5, 30C
2
2-hydroxy-1,4-benzoxazin-3-one-beta-D-glucoside
-
pH 5.5, 25C
0.89
2-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside
-
pH 5.5, 25C
1.3 - 1.4
2-Nitrophenyl beta-D-glucoside
1.64
2-Nitrophenyl-beta-D-glucopyranoside
-
pH 5.5, 24C
0.143
4-methylumbelliferyl-beta-D-glucoside
-
pH 5.5, 24C
0.616 - 1.1
4-nitrophenyl beta-D-fucoside
1.3 - 1.78
4-nitrophenyl beta-D-galactoside
2.96
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.9 - 9.28
4-nitrophenyl beta-D-glucoside
3.11 - 3.17
4-nitrophenyl beta-D-xyloside
0.674
4-nitrophenyl-beta-D-cellobioside
-
pH 5.5, 24C
0.648
4-nitrophenyl-beta-D-fucopyranoside
-
pH 5.5, 24C
4.32
4-nitrophenyl-beta-D-galactopyranoside
-
pH 5.5, 24C
0.58
4-nitrophenyl-beta-D-glucopyranoside
-
pH 5.5, 24C
0.769
4-nitrophenyl-beta-D-mannopyranoside
-
pH 5.5, 24C
0.394
4-nitrophenyl-beta-D-xyloside
-
pH 5.5, 24C
2.02
7-methoxy-3-oxo-3,4-dihydro-2H-1,4 benzoxazin-2-yl beta-D-glucopyranoside
-
pH 5.5, 30C
4.8
Dhurrin
-
recombinant enzyme, pH and temperature not specified in the publication
2.8 - 3.3
DIBOA beta-D-glucoside
0.41 - 44.1
DIBOA-glucoside
1.4 - 2.1
DIMBOA beta-D-glucoside
0.07 - 39.3
DIMBOA-glucoside
0.24
esculin
-
pH 5.5, 30C
0.251
n-octyl-beta-D-glucopyranoside
-
pH 5.5, 24C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
32
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside
Consolida orientalis
-
recombinant enzyme, pH and temperature not specified in the publication
4.2
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside
Consolida orientalis
-
recombinant enzyme, pH and temperature not specified in the publication
159 - 204.2
2-Nitrophenyl beta-D-glucoside
66.8 - 86.5
4-nitrophenyl beta-D-fucoside
3.3 - 3.5
4-nitrophenyl beta-D-galactoside
10.7 - 235.9
4-nitrophenyl beta-D-glucoside
52
Dhurrin
Consolida orientalis
-
recombinant enzyme, pH and temperature not specified in the publication
169 - 172
DIBOA beta-D-glucoside
4.7 - 214
DIBOA-glucoside
97.4 - 119
DIMBOA beta-D-glucoside
19.54 - 1201
DIMBOA-glucoside
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
7
(2R)-4-hydroxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside
Consolida orientalis
-
recombinant enzyme, pH and temperature not specified in the publication
15205
0.15
(2R)-4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside
Consolida orientalis
-
recombinant enzyme, pH and temperature not specified in the publication
28523
1.2 - 135
4-nitrophenyl beta-D-glucoside
10.8
Dhurrin
Consolida orientalis
-
recombinant enzyme, pH and temperature not specified in the publication
1121
150
DIBOA-beta-D-glucoside
Triticum aestivum
-
pH and temperature not specified in the publication
169963
0.24 - 150
DIBOA-glucoside
4100
DIMBOA-beta-D-glucoside
Triticum aestivum
-
pH and temperature not specified in the publication
169962
3.1 - 4138
DIMBOA-glucoside
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.973
4-Methylumbelliferone
-
pH 5.5, 24C
1.46
4-nitrophenol
-
pH 5.5, 24C
0.0454
D-gluconic acid lactone
-
pH 5.5, 24C
0.0541
Dhurrin
-
pH 5.5, 24C
0.274
DIMBOA
-
pH 5.5, 24C
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
0.032
2-(1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
Rattus norvegicus
-
pH 6.9, 37C
-
0.0167
2-(2-butyl-4-chloro-1H-imidazol-5-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
Rattus norvegicus
-
pH 6.9, 37C
-
0.0216
2-(2-methyl-1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
Rattus norvegicus
-
pH 6.9, 37C
-
0.0319
3-(6-chloro-2,4-dihydro-1H-benzo[d][1,3]oxazin-2-yl)-4H-chromen-4-one
Rattus norvegicus
-
pH 6.9, 37C
-
0.0171
4-(2,4-dihydro-1H-benzo[d][1,3]oxazin-2-yl)phenol
Rattus norvegicus
-
pH 6.9, 37C
-
0.0115
4-(7-chloro-2,4-dihydro-1H-benzo[d][1,3]oxazin-2-yl)phenol
Rattus norvegicus
-
pH 6.9, 37C
-
0.0278
6-chloro-2-(2-phenyl-1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
Rattus norvegicus
-
pH 6.9, 37C
-
0.0238
6-methyl-2-(2-methyl-1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
Rattus norvegicus
-
pH 6.9, 37C
-
0.0205
6-methyl-2-(2-phenyl-1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
Rattus norvegicus
-
pH 6.9, 37C
-
0.0277
7-chloro-2-(1H-indol-3-yl)-2,4-dihydro-1H-benzo[d][1,3]oxazine
Rattus norvegicus
-
pH 6.9, 37C
-
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
6.9
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
24
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
highest expression
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
additional information
-
no expression in roots
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
putatively localised in chloroplasts
Manually annotated by BRENDA team
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
58000
SDS-PAGE, native enzyme
59000
calculated from cDNA, native enzyme
59160
calculated from cDNA, native enzyme
59250
calculated from cDNA, native enzyme
64090
mass-spectroscopy, His-tagged TaGlu1a
64140
mass-spectroscopy, His-tagged TaGlu1a
67000
-
SDS-PAGE
120000
homodimer
300000
-
native-PAGE, oligomer
SUBUNITS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
dimer
minor bands in gel filtration are also observed
heterohexamer
coexpression of TaGlu1a and TaGlu1b give seven bands on a native-PAGE gel, indicating the formation of both homo- and heterohexamers; coexpression of TaGlu1a and TaGlu1b give seven bands on a native-PAGE gel, indicating the formation of both homo- and heterohexamers; coexpression of TaGlu1b and TaGlu1c give seven bands on a native-PAGE gel, indicating the formation of both homo- and heterohexamers
hexamer
crystal structure, N-terminal region plays an important role in hexamer formation; major band in gel filtration shows activity with DIMBOA-glucose
homodimer
homohexamer
coexpression of TaGlu1a and TaGlu1b give seven bands on a native-PAGE gel, indicating the formation of both homo- and heterohexamers; coexpression of TaGlu1a and TaGlu1b give seven bands on a native-PAGE gel, indicating the formation of both homo- and heterohexamers; coexpression of TaGlu1b and TaGlu1c give seven bands on a native-PAGE gel, indicating the formation of both homo- and heterohexamers
monomer
major band in gel filtration shows no activity with DIMBOA-glucose
oligomer
-
native-PAGE
tetramer
minor bands in gel filtration are also observed
Crystallization/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
crystal structures of an inactive mutant of the wheat glucosidase complexed with the natural substrate DIMBOA-Glc, wheat and rye glucosidases complexed with an aglycone DIMBOA, and wheat and rye glucosidases complexed with an inhibitor 2-fluoro-2- deoxy-beta-D-glucose are analyzed
crystal structure of hexameric TaGlu1b is determined at a resolution of 1.8 A in complex with DOMBOA. The N-terminal region is located at the dimer-dimer interface and plays a crucial role in hexamer formation
crystal structures of an inactive mutant of the wheat glucosidase complexed with the natural substrate DIMBOA-Glc, wheat and rye glucosidases complexed with an aglycone DIMBOA, and wheat and rye glucosidases complexed with an inhibitor 2-fluoro-2- deoxy-beta-D-glucose are analyzed
-
crystal structure of inactive mutant E191D Glu1 in complex with DIMBO-glucoside, the free aglycone DIMBOA, and competitive inhibitor dhurrin is solved at 2.1, 2.1, 2.0 A resolution, respectively. The free enzyme is solved at 2.2 A resolution
Purification/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
cryoprecipitation followed by cation-exchange chromatography and gel filtration
-
using gel filtration
-
using HisTrap HP column and and Superdex 200 HR
using isoelectric precipitation, anion exchange chromatography, and gel filtration
-
using Ni-NTA chromatography
Cloned/COMMENTARY
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli
expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli as a His-tagged fusion protein; expressed in Escherichia coli as a His-tagged fusion protein
expressed in Escherichia coli as His-tagged fusion protein
phylogenetic analysis, heterologus expression
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EXPRESSION
ORGANISM
UNIPROT
LITERATURE
compared to Taglu1a and Taglu1b mRNA level of Taglu1c is much lower in 48-h-old and 96-h-old wheat shoots; Taglu1a is most highly expressed (67%) in 48-h-old wheat; Taglu1b is highly expressed in 48-h-old and 96-h-old wheat shoots
ENGINEERING
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E191A
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mutant shows no activity
E407A
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mutant shows no activity
F198A
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kcat/Km values of ScGlu-F198A for DIMBOA-glucoside and DIBOA-glucoside decrease by a factor of 24- to 28fold as compared to wild-type ScGlu due to an increased Km, whereas the kcat value increases
F471Y
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kcat values for DIBOA-glucoside increased, Km (DIBOA-glucoside) increased, Km (DIMBOA-glucoside) decreased, kcat values for DIMBOA-glucoside increased
G464F
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kcat values for DIMBOA-glucoside and DIBOA-glucoside decreased, Km values increased
G464S
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kcat values for DIMBOA-glucoside and DIBOA-glucoside decreased, Km values increased
G464S/S465L
S465L
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kcat values for DIBOA-glucoside decreased, Km (DIBOA-glucoside) increased, Km (DIMBOA-glucoside) decreased, kcat values for DIMBOA-glucoside increased
Y378A
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kcat values for DIMBOA-glucoside and DIBOA-glucoside increased, Km values increased
Y378F
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kcat values for DIMBOA-glucoside and DIBOA-glucoside increased, Km values dereased
E407A
mutant shows no activity
E462A
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inactive mutant, E462 plays a crucial role in hydrolysis of the substrate
F198A
Km increased compared to wild-type, kcat decreased compared to wild-type
F471Y
Km increased compared to wild-type, kcat (DIBOA-glucoside) increased compared to wild-type, kcat (DIMBOA-glucoside or 4-nitrophenyl beta-D-glucoside) increased compared to wild-type
S464F
Km increased compared to wild-type, kcat (DIBOA-glucoside) increased compared to wild-type, kcat (DIMBOA-glucoside or 4-nitrophenyl beta-D-glucoside) increased compared to wild-type
Y378A
Km increased compared to wild-type, kcat decreased compared to wild-type
Y378F
Km decreased compared to wild-type, kcat decreased compared to wild-type
E191D
catalytically inactive mutant is used for crystal structure determination
additional information