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: Poaceae

EC NUMBER
COMMENTARY
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
ORGANISM
UNIPROT ACCESSION NO.
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
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.
SYNONYMS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
benzoxazinone-glucoside beta-D-glucosidase
Q9FYS3
-
benzoxazinone-glucoside beta-D-glucosidase
-
-
beta-glu
-
-
beta-glucosidase
-
-
beta-glucosidase
-
-
beta-glucosidase
Q1XH05
-
beta-glucosidase
-
-
beta-glucosidase
P49235
-
DIMBOA glucosidase
-
-
-
-
DIMBOAGlc hydrolase
-
-
-
-
SbDhr1
-
-
ScGlu
Q9FYS3
-
TaGlu1b
Q1XH05
-
ZmGlu1
-
-
ORGANISM
COMMENTARY
LITERATURE
SEQUENCE CODE
SEQUENCE DB
SOURCE
-
UniProt
Manually annotated by BRENDA team
SUBSTRATE
PRODUCT                      
REACTION DIAGRAM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
(Substrate)
LITERATURE
(Substrate)
COMMENTARY
(Product)
LITERATURE
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
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-3-oxo-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
Q9FYS3
-
-
-
?
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-fucoside + H2O
4-nitrophenol + beta-fucose
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-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-glucoside + H2O
4-nitrophenol + beta-D-glucose
show the reaction diagram
Q1XH05
-
-
-
?
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
-
-
-
-
?
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
-
-
-
-
?
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-2yl 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
-
-
-
-
?
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
Q1XH05
-
-
-
?
DIBOA-glucoside + H2O
DIBOA + beta-D-glucose
show the reaction diagram
-
-
-
-
?
DIBOA-glucoside + H2O
DIBOA + beta-D-glucose
show the reaction diagram
-
-
-
-
?
DIBOA-glucoside + H2O
DIBOA + beta-D-glucose
show the reaction diagram
Q9FYS3
ScGlu shows similar enzyme activity toward DIMBOA-Glc and DIBOA-Glc
-
-
?
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
Q1XH05
-
-
-
?
DIMBOA-glucoside + H2O
DIMBOA + beta-D-glucose
show the reaction diagram
-
-
-
-
?
DIMBOA-glucoside + H2O
DIMBOA + beta-D-glucose
show the reaction diagram
-
-
-
-
?
DIMBOA-glucoside + H2O
DIMBOA + beta-D-glucose
show the reaction diagram
-
-
-
-
?
DIMBOA-glucoside + H2O
DIMBOA + beta-D-glucose
show the reaction diagram
P49235
-
-
-
?
DIMBOA-glucoside + H2O
DIMBOA + beta-D-glucose
show the reaction diagram
Q9FYS3
ScGlu shows similar enzyme activity toward DIMBOA-Glc and DIBOA-Glc
-
-
?
esculin + H2O
esculetin + beta-D-glucose
show the reaction diagram
-
-
-
-
?
esculin + H2O
esculetin + beta-D-glucose
show the reaction diagram
-
-
-
-
?
esculin + H2O
esculetin + beta-D-glucose
show the reaction diagram
Q9FYS3
-
-
-
?
genistin + H2O
?
show the reaction diagram
Q9FYS3
-
-
-
?
n-octyl-beta-D-glucopyranoside + H2O
octanol + beta-D-glucose
show the reaction diagram
-
-
-
-
?
salicin + H2O
?
show the reaction diagram
-
-
-
-
?
METALS and IONS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
2-fluoro-2-deoxy-beta-D-glucose
Q9FYS3
-
-
2-fluoro-2-deoxy-beta-D-glucose
-
-
-
4-Methylumbelliferone
-
-
4-nitrophenol
-
-
castanospermine
-
-
D-gluconic acid lactone
-
-
DIMBOA
-
-
KM VALUE [mM]
KM VALUE [mM] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
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
-
2-Nitrophenyl beta-D-glucoside
-
pH 5.8, 37C, recombinant protein
1.4
-
2-Nitrophenyl beta-D-glucoside
-
pH 5.8, 37C, native protein
1.64
-
2-Nitrophenyl-beta-D-glucopyranoside
-
pH 5.5, 24C
0.143
-
4-methylumbelliferyl-beta-D-glucoside
-
pH 5.5, 24C
0.616
-
4-nitrophenyl beta-D-fucoside
-
pH 5.5, 25C
0.67
-
4-nitrophenyl beta-D-fucoside
-
pH 5.5, 30C
0.8
-
4-nitrophenyl beta-D-fucoside
-
pH 5.8, 37C, native protein
1.1
-
4-nitrophenyl beta-D-fucoside
-
pH 5.8, 37C, recombinant protein
1.3
-
4-nitrophenyl beta-D-galactoside
-
pH 5.8, 37C, native protein
1.5
-
4-nitrophenyl beta-D-galactoside
-
pH 5.8, 37C, recombinant protein
1.78
-
4-nitrophenyl beta-D-galactoside
-
pH 5.5, 30C
2.96
-
4-nitrophenyl beta-D-glucopyranoside
-
pH and temperature not specified in the publication
0.9
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 25C
0.92
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant F471Y
1.23
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378F
1.33
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378A
1.34
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant Y378F
1.38
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant G464S/S465L
1.7
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C
1.7
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant G464F
1.75
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, wild-type
1.78
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, wild-type
1.85
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, wild-type
2.02
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant Y378A
2.03
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant S465L
2.16
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, wild-type
2.31
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant S464F
2.4
-
4-nitrophenyl beta-D-glucoside
-
pH 5.8, 37C, native protein; pH 5.8, 37C, recombinant protein
2.89
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant G464S
2.93
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant F471Y
3.05
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant F198A
9.28
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant F198A
3.11
-
4-nitrophenyl beta-D-xyloside
-
pH 5.5, 30C
3.17
-
4-nitrophenyl beta-D-xyloside
-
pH 5.5, 25C
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-2yl beta-D-glucopyranoside
-
pH 5.5, 30C
-
2.8
-
DIBOA beta-D-glucoside
-
pH 5.8, 37C, recombinant protein
-
3.3
-
DIBOA beta-D-glucoside
-
pH 5.8, 37C, native protein
-
0.41
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378F
0.52
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant Y378F
0.52
-
DIBOA-glucoside
-
pH and temperature not specified in the publication
0.68
-
DIBOA-glucoside
-
pH and temperature not specified in the publication
0.8
-
DIBOA-glucoside
-
pH 5.5, 30C, wild-type
0.83
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant S465L
1.02
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant G464S
1.05
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
1.19
-
DIBOA-glucoside
-
pH 5.5, 25C
1.4
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
1.44
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
1.55
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant G464S/S465L
1.6
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant G464F
2.03
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant F471Y
2.89
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant S464F
4.21
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F471Y
6.05
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378A
7.99
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant Y378A
27.5
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F198A
44.1
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant F198A
1.4
-
DIMBOA beta-D-glucoside
-
pH 5.8, 37C, recombinant protein
-
2.1
-
DIMBOA beta-D-glucoside
-
pH 5.8, 37C, native protein
-
0.07
-
DIMBOA-glucoside
-
pH and temperature not specified in the publication
0.098
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
0.098
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1); pH 5.8, 37C, wild-type
0.104
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
0.106
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
0.13
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378F
0.16
-
DIMBOA-glucoside
-
pH and temperature not specified in the publication
0.2
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
0.205
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
0.29
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
0.36
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
0.39
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
0.59
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant G464S/S465L
0.617
-
DIMBOA-glucoside
-
pH 5.5, 25C
0.7
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F471Y
0.76
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant S465L
0.94
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant G464S
1.04
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant F471Y
1.07
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant Y378F
1.19
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378A
1.3
-
DIMBOA-glucoside
-
pH 5.5, 30C, wild-type
1.42
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant Y378A
1.42
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant S464F
5.12
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant G464F
35.7
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F198A
39.3
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant F198A
0.24
-
esculin
-
pH 5.5, 30C
0.251
-
n-octyl-beta-D-glucopyranoside
-
pH 5.5, 24C
TURNOVER NUMBER [1/s]
TURNOVER NUMBER MAXIMUM[1/s]
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
159
-
2-Nitrophenyl beta-D-glucoside
-
pH 5.8, 37C, native protein
204.2
-
2-Nitrophenyl beta-D-glucoside
-
pH 5.8, 37C, recombinant protein
66.8
-
4-nitrophenyl beta-D-fucoside
-
pH 5.8, 37C, native protein
86.5
-
4-nitrophenyl beta-D-fucoside
-
pH 5.8, 37C, recombinant protein
3.3
-
4-nitrophenyl beta-D-galactoside
-
pH 5.8, 37C, recombinant protein
3.5
-
4-nitrophenyl beta-D-galactoside
-
pH 5.8, 37C, native protein
10.7
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant F198A
10.7
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant F198A
25.1
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant Y378A
25.1
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378A
31.2
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant S464F
31.2
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant S464F
46.1
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant Y378F
46.1
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378F
52
-
4-nitrophenyl beta-D-glucoside
-
pH 5.8, 37C, native protein
54.6
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant F471Y
54.6
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant F471Y
72.8
-
4-nitrophenyl beta-D-glucoside
-
pH 5.8, 37C, recombinant protein
99.2
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, wild-type
99.2
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, wild-type
128
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, wild-type
235.9
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, wild-type
169
-
DIBOA beta-D-glucoside
-
pH 5.8, 37C, recombinant protein
-
172
-
DIBOA beta-D-glucoside
-
pH 5.8, 37C, native protein
-
4.7
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant Y378F
4.7
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378F
6.7
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant F198A
6.7
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F198A
26.4
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant Y378A
26.4
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378A
48.8
-
DIBOA-glucoside
-
pH 5.5, 30C, wild-type
48.8
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
83.5
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant F471Y
83.5
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F471Y
84
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant S464F
84
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant S464F
137
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
214
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
97.4
-
DIMBOA beta-D-glucoside
-
pH 5.8, 37C, recombinant protein
-
119
-
DIMBOA beta-D-glucoside
-
pH 5.8, 37C, native protein
-
19.54
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
20.15
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
24.02
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
25.67
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
29.16
-
DIMBOA-glucoside
-
pH 5.8, 37C, wild-type
43.33
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
73.3
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant S464F
73.3
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant S464F
85.1
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant Y378F
85.1
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378F
110
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant F198A
110
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F198A
124
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant Y378A
124
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378A
192
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant F471Y
192
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F471Y
338
-
DIMBOA-glucoside
-
pH 5.5, 30C, wild-type
338
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
773
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
1201
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
kcat/KM VALUE [1/mMs-1]
kcat/KM VALUE [1/mMs-1] Maximum
SUBSTRATE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
IMAGE
1.2
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant F198A
4738
2.72
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant F198A
4738
12.5
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, wild-type
4738
13.5
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant S464F
4738
15
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant G464F
4738
18.6
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant F471Y
4738
18.9
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378A
4738
37.2
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant S465L
4738
37.5
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378F
4738
42.9
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant G464S
4738
47
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant Y378F
4738
50.3
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant F471Y
4738
50.5
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant Y378A
4738
53.6
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, wild-type
4738
54.6
-
4-nitrophenyl beta-D-glucoside
-
pH 5.5, 30C, mutant G464S/S465L
4738
59.3
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, wild-type
4738
135
-
4-nitrophenyl beta-D-glucoside
Q1XH05
pH 5.5, 30C, wild-type
4738
150
-
DIBOA-beta-D-glucoside
-
pH and temperature not specified in the publication
0
0.24
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F198A
296817
4.36
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378A
296817
5.28
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant F198A
296817
11.5
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378F
296817
19.8
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F471Y
296817
23.1
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant Y378F
296817
29.1
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant S464F
296817
34.1
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant G464F
296817
34.6
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
296817
53.9
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant G464S/S465L
296817
56.1
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant S465L
296817
85.2
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant G464S
296817
120
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant F471Y
296817
131
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
296817
137
-
DIBOA-glucoside
-
pH 5.5, 30C, mutant Y378A
296817
148
-
DIBOA-glucoside
-
pH 5.5, 30C, wild-type
296817
149
-
DIBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
296817
150
-
DIBOA-glucoside
Q9FYS3
pH and temperature not specified in the publication
296817
4100
-
DIMBOA-beta-D-glucoside
-
pH and temperature not specified in the publication
0
3.1
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F198A
296820
4.94
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant F198A
296820
23.6
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant G464F
296820
51.6
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant S464F
296820
97.7
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
296820
104
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378A
296820
120
-
DIMBOA-glucoside
Q9FYS3
pH and temperature not specified in the publication
296820
122
-
DIMBOA-glucoside
-
pH 5.5, 30C, wild-type
296820
182
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant Y378F
296820
195.2
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
296820
211
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
296820
226
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
296820
244
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant G464S
296820
261.9
-
DIMBOA-glucoside
-
pH 5.8, 37C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
296820
274
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant F471Y
296820
296
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant S465L
296820
297.5
-
DIMBOA-glucoside
-
pH 5.8, 37C, wild-type
296820
309
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant F471Y
296820
488
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant G464S/S465L
296820
582
-
DIMBOA-glucoside
-
pH 5.5, 30C, mutant Y378A
296820
655
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, mutant Y378F
296820
939
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
296820
1979
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
296820
4138
-
DIMBOA-glucoside
Q1XH05
pH 5.5, 30C, wild-type
296820
Ki VALUE [mM]
Ki VALUE [mM] Maximum
INHIBITOR
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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
pH OPTIMUM
pH MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
5.5
-
-
assay at
5.5
-
Q1XH05
assay at; assay at
5.5
-
-
assay at
5.5
-
Q9FYS3
assay at
5.5
-
-
assay at
5.8
-
-
assay at
5.8
-
-
assay at
TEMPERATURE OPTIMUM
TEMPERATURE OPTIMUM MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
24
-
-
assay at
25
-
-
assay at 25C, substrates: 2-nitrophenyl-beta-D-glucopyranoside and 4-nitrophenyl-beta-D-glucopyranoside
25
-
-
optimal reaction at 25-30C
30
-
-
assay at
30
-
Q1XH05
assay at; assay at
30
-
Q9FYS3
assay at
30
-
-
assay at
37
-
-
assay at 37C, substrates: dhurrin and DIMBOA-glucoside
37
-
-
assay at
SOURCE TISSUE
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
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 ACCESSION NO.
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
-
putatively localised in chloroplasts
Manually annotated by BRENDA team
MOLECULAR WEIGHT
MOLECULAR WEIGHT MAXIMUM
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
58000
-
Q1XH05
SDS-PAGE, native enzyme
59000
-
Q1XH05
calculated from cDNA, native enzyme
59160
-
Q1XH05
calculated from cDNA, native enzyme
59250
-
Q1XH05
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
60000
-
Q1XH05
SDS-PAGE, native enzyme
60000
-
-
monomer
60000
-
-
SDS-PAGE, monomer
64090
-
Q1XH05
mass-spectroscopy, His-tagged TaGlu1a
64140
-
Q1XH05
mass-spectroscopy, His-tagged TaGlu1a
67000
-
-
SDS-PAGE
120000
-
P49235
homodimer
300000
-
-
native-PAGE, oligomer
SUBUNITS
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
dimer
Q1XH05
minor bands in gel filtration are also observed
heterohexamer
Q1XH05
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
Q1XH05
crystal structure, N-terminal region plays an important role in hexamer formation; major band in gel filtration shows activity with DIMBOA-glucose
homodimer
-
2 * 60000 Da
homodimer
P49235
crystal structure
homohexamer
Q1XH05
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
Q1XH05
major band in gel filtration shows no activity with DIMBOA-glucose
oligomer
-
native-PAGE
tetramer
Q1XH05
minor bands in gel filtration are also observed
Crystallization/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
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
Q9FYS3
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
Q1XH05
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
P49235
Purification/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
using HisTrap HP column and and Superdex 200 HR
Q9FYS3
using isoelectric precipitation, anion exchange chromatography, and gel filtration
-
using Ni-NTA chromatography
-
using gel filtration
-
using HisTrap HP column and and Superdex 200 HR
-
cryoprecipitation followed by cation-exchange chromatography and gel filtration
-
using Ni-NTA chromatography
-
Cloned/COMMENTARY
ORGANISM
UNIPROT ACCESSION NO.
LITERATURE
expressed in Escherichia coli
-
expressed in Escherichia coli as a His-tagged fusion protein
-
expressed in Escherichia coli as His-tagged fusion protein
Q9FYS3
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
Q1XH05
expressed in Escherichia coli as His-tagged fusion protein
-
expressed in Escherichia coli
P49235
expressed in Escherichia coli as a His-tagged fusion protein
-
EXPRESSION
ORGANISM
UNIPROT ACCESSION NO.
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
Q1XH05
ENGINEERING
ORGANISM
UNIPROT ACCESSION NO.
COMMENTARY
LITERATURE
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
G464S/S465L
Q9FYS3
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
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
E191A
Q1XH05
mutant shows no activity
E191A
-
crystals of the enzymatically inactive mutant E191A are soaked in a solution containing DIMBOA-Glc as substrate and 3.5M sodium formate as cryoprotectant, the structure is solved at a resolution of 2.2 A and the DIMBOA-Glc molecule is clearly defined. In the structure, the aglycone moiety is shown to be stabilized by interaction with the aromatic ring of W379 and by a hydrogen bond with T194
E407A
Q1XH05
mutant shows no activity
E462A
-
inactive mutant, E462 plays a crucial role in hydrolysis of the substrate
F198A
Q1XH05
Km increased compared to wild-type, kcat decreased compared to wild-type
S464F
Q1XH05
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
Q1XH05
Km increased compared to wild-type, kcat decreased compared to wild-type
Y378F
Q1XH05
Km decreased compared to wild-type, kcat decreased compared to wild-type
Y378F
-
kcat values for DIMBOA-glucoside and DIBOA-glucoside increased, Km values dereased
additional information
-
to study the mechanism of substrate specificity further, eight chimeric beta-glucosidases are constructed by replacing peptide sequences within the C-terminal region of Zea mays Glu1 with the homologous peptide sequences of Sorghum Dhr1 or vice versa. Replacing the peptide 466FAGFTERY473 of Zea mays Glu1 with the homologous peptide 462SSGYTERF469 of Sorghum Dhr1 or replacing the peptide 481NNNCTRYMKE490 in Glu1 with the homologous peptide 477ENGCERTMKR486 of Dhr1 is sufficient to confer to Zea mays Glu1 the ability to hydrolyze dhurrin
F471Y
Q1XH05
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
additional information
Q1XH05
the N-terminal 25 residues of the mature TaGlu1a and TaGlu1b are replaced with the corresponding residues of Zea mays ZmGlu1, considering that this enzyme is known to exist as a dimer. The chimeric glucosidases (Zm-TaGlu1a and Zm-TaGlu1b) completely loses their ability to form a hexamer, which is confirmed by gel filtration chromatography; the N-terminal 25 residues of the mature TaGlu1a and TaGlu1b are replaced with the corresponding residues of Zea mays ZmGlu1, considering that this enzyme is known to exist as a dimer. The chimeric glucosidases (Zm-TaGlu1a and Zm-TaGlu1b) completely loses their ability to form a hexamer, which is confirmed by gel filtration chromatography
E191D
P49235
catalytically inactive mutant is used for crystal structure determination
additional information
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to study the mechanism of substrate specificity further, eight chimeric beta-glucosidases are constructed by replacing peptide sequences within the C-terminal region of Zea mays Glu1 with the homologous peptide sequences of Sorghum Dhr1 or vice versa. Replacing the peptide 466FAGFTERY473 of Zea mays Glu1 with the homologous peptide 462SSGYTERF469 of Sorghum Dhr1 or replacing the peptide 481NNNCTRYMKE490 in Glu1 with the homologous peptide 477ENGCERTMKR486 of Dhr1 is sufficient to confer to Zea mays Glu1 the ability to hydrolyze dhurrin