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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) Secale cereale and UniProt Accession Q9FYS3

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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:
Secale cereale
UNIPROT: Q9FYS3
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The taxonomic range for the selected organisms is: Secale cereale
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
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-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
-
-
-
?
DIBOA-glucoside + H2O
DIBOA + beta-D-glucose
show the reaction diagram
ScGlu shows similar enzyme activity toward DIMBOA-Glc and DIBOA-Glc
-
-
?
DIMBOA-glucoside + H2O
DIMBOA + beta-D-glucose
show the reaction diagram
ScGlu shows similar enzyme activity toward DIMBOA-Glc and DIBOA-Glc
-
-
?
esculin + H2O
esculetin + beta-D-glucose
show the reaction diagram
-
-
-
?
genistin + H2O
?
show the reaction diagram
-
-
-
?
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-glucoside + H2O
2-nitrophenol + 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-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
-
-
-
-
?
DIBOA beta-D-glucoside + H2O
DIBOA + beta-D-glucose
show the reaction diagram
-
-
-
-
?
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-glucoside + H2O
DIMBOA + beta-D-glucose
show the reaction diagram
-
-
-
-
?
esculin + H2O
esculetin + beta-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
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2-fluoro-2-deoxy-beta-D-glucose
-
castanospermine
-
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
2
2-hydroxy-1,4-benzoxazin-3-one-beta-D-glucoside
-
pH 5.5, 25°C
0.89
2-hydroxy-7-methoxy-3-oxo-3,4-dihydro-2H-1,4-benzoxazin-2-yl beta-D-glucopyranoside
-
pH 5.5, 25°C
1.3 - 1.4
2-Nitrophenyl beta-D-glucoside
0.616 - 1.1
4-nitrophenyl beta-D-fucoside
1.3 - 1.5
4-nitrophenyl beta-D-galactoside
0.9 - 3.05
4-nitrophenyl beta-D-glucoside
3.17
4-nitrophenyl beta-D-xyloside
-
pH 5.5, 25°C
2.8 - 3.3
DIBOA beta-D-glucoside
0.52 - 44.1
DIBOA-glucoside
1.4 - 2.1
DIMBOA beta-D-glucoside
0.59 - 39.3
DIMBOA-glucoside
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
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 - 99.2
4-nitrophenyl beta-D-glucoside
169 - 172
DIBOA beta-D-glucoside
4.7 - 84
DIBOA-glucoside
97.4 - 119
DIMBOA beta-D-glucoside
73.3 - 338
DIMBOA-glucoside
kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
IMAGE
150
DIBOA-glucoside
pH and temperature not specified in the publication
120
DIMBOA-glucoside
pH and temperature not specified in the publication
2.72 - 54.6
4-nitrophenyl beta-D-glucoside
5.28 - 148
DIBOA-glucoside
4.94 - 582
DIMBOA-glucoside
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
5.8
-
assay at
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
25
-
optimal reaction at 25-30°C
30
-
assay at
37
-
assay at
ORGANISM
COMMENTARY hide
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
Manually annotated by BRENDA team
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
SOURCE
-
highest expression
Manually annotated by BRENDA team
-
highest expression
Manually annotated by BRENDA team
-
isolated from 48-h-old rye shoots
Manually annotated by BRENDA team
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY hide
GeneOntology No.
LITERATURE
SOURCE
-
putatively localised in chloroplasts
Manually annotated by BRENDA team
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION?
HGGL_SECCE
568
0
64212
Swiss-Prot
Chloroplast (Reliability: 5)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
300000
-
native-PAGE, oligomer
60000
-
SDS-PAGE, monomer
67000
-
SDS-PAGE
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
oligomer
-
native-PAGE
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
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY hide
LITERATURE
G464S/S465L
mutation reduces the reaction efficiency toward DIBOA-Glc to 36% of wild type, whereas it enhances efficiency toward DIMBOA-Glc to 400% of wild type
E191A
-
mutant shows no activity
E407A
-
mutant shows no activity
F198A
-
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
-
kcat values for DIBOA-glucoside increased, Km (DIBOA-glucoside) increased, Km (DIMBOA-glucoside) decreased, kcat values for DIMBOA-glucoside increased
G464F
-
kcat values for DIMBOA-glucoside and DIBOA-glucoside decreased, Km values increased
G464S
-
kcat values for DIMBOA-glucoside and DIBOA-glucoside decreased, Km values increased
G464S/S465L
-
kcat values for DIBOA-glucoside decreased, Km (DIBOA-glucoside) increased, Km (DIMBOA-glucoside) decreased, kcat values for DIMBOA-glucoside increased
S465L
-
kcat values for DIBOA-glucoside decreased, Km (DIBOA-glucoside) increased, Km (DIMBOA-glucoside) decreased, kcat values for DIMBOA-glucoside increased
Y378A
-
kcat values for DIMBOA-glucoside and DIBOA-glucoside increased, Km values increased
Y378F
-
kcat values for DIMBOA-glucoside and DIBOA-glucoside increased, Km values dereased
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
using HisTrap HP column and and Superdex 200 HR
using isoelectric precipitation, anion exchange chromatography, and gel filtration
-
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
expressed in Escherichia coli as His-tagged fusion protein
expressed in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
-
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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
Nikus, J.; Esen, A.; Jonsson, L.
Cloning of a plastidic rye (Secale cereale) beta-glucosidase cDNA and its expression in Escherichia coli
Physiol. Plant.
118
337-345
2003
Secale cereale
-
Manually annotated by BRENDA team
Sue, M.; Ishihara, A.; Iwamura, H.
Purification and characterization of a beta-glucosidase from rye (Secale cereale L.) seedlings
Plant sci.
155
67-74
2000
Secale cereale
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