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52
-
recombinant enzyme, pH and temperature not specified in the publication
0.16
-
pH 5.8, 37°C, mutant F205L
0.21
-
pH 5.8, 37°C, mutant M263F
0.55
-
pH 5.8, 37°C, mutant F466S/A467S
0.59
-
pH 5.8, 37°C, mutant F466S
0.7
-
pH 5.8, 37°C, mutant F198V/F205L/P377A
1.13
-
pH 5.8, 37°C, mutant Y473F
1.32
-
pH 5.8, 37°C, chimeric mutant (Chim21) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1
2.23
-
pH 5.8, 37°C, chimeric mutant (Chim16) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1 (with an extra 22 amino acids substitution)
3.6
-
pH 5.8, 37°C, mutant A375P
3.7
-
pH 5.8, 37°C, mutant V196F/L203F
6.52
-
pH 5.8, 37°C, mutant F469Y
13.46
-
pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
14.3
-
pH 5.8, 37°C, wild-type
18.68
-
pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)
22.7
-
pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
23.41
-
pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)
27.17
-
pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
31.83
-
pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
46.02
-
pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
53.96
-
pH 5.8, 37°C, mutant Chim23 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 492-508 of Zea mays)
77.7
-
pH 5.8, 37°C, wild-type
112.5
-
isoform GLU1, at pH 5.5 and 30°C
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4.8
-
recombinant enzyme, pH and temperature not specified in the publication
0.031
-
pH 5.8, 37°C, mutant F205L
0.04
-
pH 5.8, 37°C, mutant Chim23 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 492-508 of Zea mays)
0.047
-
pH 5.8, 37°C, mutant Y473F
0.05
-
pH 5.8, 37°C, wild-type
0.058
-
pH 5.8, 37°C, mutant F198V/F205L/P377A
0.06
-
pH 5.8, 37°C, mutant A375P
0.061
-
pH 5.8, 37°C, wild-type
0.065
-
pH 5.8, 37°C, mutant F466S/A467S
0.065
-
pH 5.8, 37°C, mutant V196F/L203F
0.066
-
pH 5.8, 37°C, mutant M263F
0.076
-
pH 5.8, 37°C, chimeric mutant (Chim21) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1
0.09
-
pH 5.8, 37°C, mutant Chim21 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-473 of Sorghum Dhr1)
0.092
-
pH 5.8, 37°C, mutant F466S
0.1
-
pH 5.8, 37°C, mutant Chim16 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-495 of Sorghum Dhr1)
0.101
-
pH 5.8, 37°C, chimeric mutant (Chim16) bearing a C-terminal octapeptide (466-477) exchanged with the homologous octapeptide of Sorghum Dhr1 (with an extra 22 amino acids substitution)
0.12
-
pH 5.8, 37°C, mutant Chim39 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 466-492 of Zea mays)
0.127
-
pH 5.8, 37°C, mutant F469Y
0.15
-
pH 5.8, 37°C, mutant Chim17 (chimeric construct: parental Sorghum Dhr1 with exchanged domain 462-508 of Zea mays)
0.18
-
pH 5.8, 37°C, mutant Chim22 (chimeric construct: parental Zea mays Glu1 with exchanged domain 481-490 of Sorghum Dhr1)
0.36
-
pH 5.8, 37°C, mutant Chim2 (chimeric construct: parental Zea mays Glu1 with exchanged domain 466-518 of Sorghum Dhr1)
0.4
-
beta-glucosidase C, pH 5, 30°C
0.51
-
pH 5.8, 37°C, mutant Chim15 (chimeric construct: parental Zea mays Glu1 with exchanged domain 496-518 of Sorghum Dhr1)
1.9
-
isoform GLU1, at pH 5.5 and 30°C
2
-
beta-glucosidase B, pH 5, 30°C
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Tissue distributions of dhurrin and of enzymes involved in its metabolism in leaves of Sorghum bicolor
1979
Kojima, M.; Poulton, J.E.; Thayer, S.S.; Conn, E.E.
Plant Physiol.
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Production and properties of the linamarase and amygdalase activities of Penicillium aurantiogriseum P35
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The UDP-glucose:p-hydroxymandelonitrile-O-glucosyltransferase that catalyzes the last step in synthesis of the cyanogenic glucoside dhurrin in Sorghum bicolor. Isolation, cloning, heterologous expression, and substrate specificity
1999
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274
35483-35491
Structural determinants of substrate specificity in family 1 beta-glucosidases: novel insights from the crystal structure of sorghum dhurrinase-1, a plant beta-glucosidase with strict specificity, in complex with its natural substrate
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Verdoucq, L.; Moriniere, J.; Bevan, D.R.; Esen, A.; Vasella, A.; Henrissat, B.; Czjze, M.
J. Biol. Chem.
279
31796-31803
The aglycone specificity-determining sites are different in 2, 4-dihydroxy-7-methoxy-1,4-benzoxazin-3-one (DIMBOA)-glucosidase (Maize beta -glucosidase) and dhurrinase (Sorghum beta -glucosidase)
2000
Cicek, M.; Blanchard, D.; Bevan, D.R.; Esen, A.
J. Biol. Chem.
275
20002-20011
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Substrate specificity of maize beta-glucosidase
1994
Babcock, G.; Esen, A.
Plant Sci.
101
31-39
The mechanism of substrate (aglycone) specificity in beta -glucosidases is revealed by crystal structures of mutant maize beta -glucosidase-DIMBOA, -DIMBOAGlc, and -dhurrin complexes
2000
Czjzek, M.; Cicek, M.; Zamboni, V.; Bevan, D.R.; Henrissat, B.; Esen, A.
Proc. Natl. Acad. Sci. USA
97
13555-13560
Mutational and structural analysis of aglycone specificity in maize and sorghum beta-glucosidases
2003
Verdoucq, L.; Czjzek, M.; Moriniere, J.; Bevan, D.R.; Esen, A.
J. Biol. Chem.
278
25055-25062
-
Characterization of cyanogenic glucosides and beta-glucosidases in Triglochin maritima seedlings
1979
Nahrstedt, A.; Hosel, W.; Walther, A.
Phytochemistry
18
1137-1141
Comparative analysis of benzoxazinoid biosynthesis in monocots and dicots: independent recruitment of stabilization and activation functions
2012
Dick, R.; Rattei, T.; Haslbeck, M.; Schwab, W.; Gierl, A.; Frey, M.
Plant Cell
24
915-928
A promiscuous beta-glucosidase is involved in benzoxazinoid deglycosylation in Lamium galeobdolon
2018
Hannemann, L.; Lucaciu, C.R.; Sharma, S.; Rattei, T.; Mayer, K.F.X.; Gierl, A.; Frey, M.
Phytochemistry
156
224-233