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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 and Organism(s) Triticum aestivum and UniProt Accession Q1XH05

for references in articles please use BRENDA:EC3.2.1.182
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EC Tree
IUBMB Comments
The enzyme from Triticum aestivum (wheat) has a higher affinity for DIMBOA glucoside than DIBOA glucoside. With Secale cereale (rye) the preference is reversed.
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This record set is specific for:
Triticum aestivum
UNIPROT: Q1XH05
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The taxonomic range for the selected organisms is: Triticum aestivum
The enzyme appears in selected viruses and cellular organisms
Synonyms
taglu1b, lgglu1, taglu1a, taglu1c, taglu1, scglu, 4-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2h-1,4-benzoxazin-2-yl glucoside beta-d-glucosidase, more
SYNONYM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
beta-glucosidase
-
benzoxazinone-glucoside beta-D-glucosidase
-
-
beta-glucosidase
-
-
DIMBOA glucosidase
-
-
-
-
DIMBOAGlc hydrolase
-
-
-
-
PATHWAY SOURCE
PATHWAYS
-
-
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.
SUBSTRATE
PRODUCT                       
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate) hide
LITERATURE
(Substrate)
COMMENTARY
(Product) hide
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
4-nitrophenyl beta-D-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
-
-
-
?
DIBOA-glucoside + H2O
DIBOA + beta-D-glucose
show the reaction diagram
-
-
-
?
DIMBOA-glucoside + H2O
DIMBOA + beta-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
-
-
?
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-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
4-nitrophenyl beta-D-xyloside + H2O
4-nitrophenol + beta-D-xylose
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
-
-
-
-
?
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
-
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
-
-
-
-
?
salicin + H2O
?
show the reaction diagram
-
-
-
-
?
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-fluoro-2-deoxy-beta-D-glucose
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2.16
4-nitrophenyl beta-D-glucoside
pH 5.5, 30°C, wild-type
1.44
DIBOA-glucoside
pH 5.5, 30°C, wild-type
0.29
DIMBOA-glucoside
pH 5.5, 30°C, wild-type
1.34
2,4-dihydroxy-2H-1,4-benzoxazin-3(4H)-one beta-D-glucopyranoside
-
pH 5.5, 30°C
0.27
2,4-dihydroxy-7-methoxy-2H-1,4-benzoxazin-3(4H)-one beta-D-glucopyranoside
-
pH 5.5, 30°C
0.67
4-nitrophenyl beta-D-fucoside
-
pH 5.5, 30°C
1.78
4-nitrophenyl beta-D-galactoside
-
pH 5.5, 30°C
1.23 - 9.28
4-nitrophenyl beta-D-glucoside
3.11
4-nitrophenyl beta-D-xyloside
-
pH 5.5, 30°C
2.02
7-methoxy-3-oxo-3,4-dihydro-2H-1,4 benzoxazin-2-yl beta-D-glucopyranoside
-
pH 5.5, 30°C
0.41 - 27.5
DIBOA-glucoside
0.13 - 35.7
DIMBOA-glucoside
0.24
esculin
-
pH 5.5, 30°C
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
128
4-nitrophenyl beta-D-glucoside
pH 5.5, 30°C, wild-type
214
DIBOA-glucoside
pH 5.5, 30°C, wild-type
1201
DIMBOA-glucoside
pH 5.5, 30°C, wild-type
10.7 - 235.9
4-nitrophenyl beta-D-glucoside
4.7 - 137
DIBOA-glucoside
73.3 - 773
DIMBOA-glucoside
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
59.3
4-nitrophenyl beta-D-glucoside
pH 5.5, 30°C, wild-type
149
DIBOA-glucoside
pH 5.5, 30°C, wild-type
4138
DIMBOA-glucoside
pH 5.5, 30°C, wild-type
1.2 - 135
4-nitrophenyl beta-D-glucoside
150
DIBOA-beta-D-glucoside
-
pH and temperature not specified in the publication
0.24 - 131
DIBOA-glucoside
4100
DIMBOA-beta-D-glucoside
-
pH and temperature not specified in the publication
3.1 - 1979
DIMBOA-glucoside
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
isolated from
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HGL1B_WHEAT
569
0
64482
Swiss-Prot
Chloroplast (Reliability: 4)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
59000
calculated from cDNA, native enzyme
60000
SDS-PAGE, native enzyme
64090
mass-spectroscopy, His-tagged TaGlu1a
58000
SDS-PAGE, native enzyme
59160
calculated from cDNA, native enzyme
59250
calculated from cDNA, native enzyme
60000
-
enzyme is found to be present as oligomeric forms with a molecular mass of 260-300 kDa comprising 60- and 58-kDa monomers
64140
mass-spectroscopy, His-tagged TaGlu1a
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
heterohexamer
coexpression of TaGlu1a and TaGlu1b 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
homohexamer
coexpression of TaGlu1a and TaGlu1b give seven bands on a native-PAGE gel, indicating the formation of both homo- and heterohexamers
dimer
minor bands in gel filtration are also observed
heterohexamer
hexamer
major band in gel filtration shows activity with DIMBOA-glucose
homohexamer
monomer
major band in gel filtration shows no activity with DIMBOA-glucose
tetramer
minor bands in gel filtration are also observed
CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
E191A
E407A
mutant shows no activity
E462A
-
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
additional information
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using gel filtration
-
using HisTrap HP column and and Superdex 200 HR
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
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
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
Taglu1b is highly expressed in 48-h-old and 96-h-old wheat shoots
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
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Sue, M.; Ishihara, A.; Iwamura, H.
Purification and characterization of a hydroxamic acid glucoside beta-glucosidase from wheat (Triticum aestivum L.) seedlings
Planta
210
432-438
2000
Triticum aestivum
Manually annotated by BRENDA team
Sue, M.; Yamazaki, K.; Yajima, S.; Nomura, T.; Matsukawa, T.; Iwamura, H.; Miyamoto, T.
Molecular and structural characterization of hexameric beta-D-glucosidases in wheat and rye
Plant Physiol.
141
1237-1247
2006
Secale cereale, Triticum aestivum, Triticum aestivum (Q1XH05)
Manually annotated by BRENDA team
Sue, M.; Nakamura, C.; Miyamoto, T.; Yajima, S.
Active-site architecture of benzoxazinone-glucoside beta-D-glucosidases in Triticeae
Plant Sci.
180
268-275
2011
Secale cereale (Q9FYS3), Triticum aestivum
Manually annotated by BRENDA team