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4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
4-nitrophenyl alpha-D-glucoside + H2O
4-nitrophenol + D-glucose
377% of the activity with isomaltose, wild-type enzyme
-
-
?
4-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
4-nitrophenyl-alpha-isomaltoside + H2O
4-nitrophenol + isomaltose
dextran + H2O
alpha-D-glucose
-
-
-
?
dextran + H2O
beta-D-glucose
dextran + H2O
beta-D-glucose + ?
-
-
-
-
?
dextran + H2O
D-glucose
-
-
-
-
?
dextran + H2O
D-glucose + ?
dextrans + H2O
beta-D-glucose
glycogen + H2O
?
-
-
-
-
?
isomaltodextrins + H2O
beta-D-glucose
isomaltoheptaose + H2O
D-glucose
148% of the activity with isomaltose, wild-type enzyme
-
-
?
isomaltohexaose + H2O
D-glucose
148% of the activity with isomaltose, wild-type enzyme
-
-
?
isomaltooligosaccharide + H2O
D-glucose + ?
isomaltooligosacchrides + H2O
D-glucose
-
-
-
-
?
isomaltopentaose + H2O
beta-D-glucose
-
-
-
?
isomaltopentaose + H2O
D-glucose
148% of the activity with isomaltose, wild-type enzyme
-
-
?
isomaltose + H2O
2 D-glucose
isomaltose + H2O
beta-D-glucose
isomaltotetraose + H2O
beta-D-glucose
-
-
-
?
isomaltotetraose + H2O
D-glucose
148% of the activity with isomaltose, wild-type enzyme
-
-
?
isomaltotriose + H2O
beta-D-glucose
isomaltotriose + H2O
D-glucose
isomaltulose + H2O
D-glucose
kojibiose + H2O
2 D-glucose
4.02% of the activity with isomaltose, wild-type enzyme
-
-
?
maltose + H2O
2 D-glucose
0.0135% of the activity with isomaltose, wild-type enzyme
-
-
?
maltotetraose + H2O
maltotriose + D-glucose
0.0108% of the activity with isomaltose, wild-type enzyme
-
-
?
maltotriose + H2O
maltose + D-glucose
0.146% of the activity with isomaltose, wild-type enzyme
-
-
?
nigerose + H2O
2 D-glucose
1.99% of the activity with isomaltose, wild-type enzyme
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + alpha-D-glucopyranose
panose + H2O
beta-D-glucose
-
-
-
?
panose + H2O
D-glucose + ?
sucrose + H2O
D-fructose + D-glucose
4.29% of the activity with isomaltose, wild-type enzyme
-
-
?
additional information
?
-
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
strong hydrolytic activity
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
strong hydrolytic activity
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucopyranose
-
-
-
?
4-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl-alpha-D-glucopyranoside + H2O
4-nitrophenol + D-glucose
-
-
-
?
4-nitrophenyl-alpha-isomaltoside + H2O
4-nitrophenol + isomaltose
-
-
-
?
4-nitrophenyl-alpha-isomaltoside + H2O
4-nitrophenol + isomaltose
-
-
-
?
dextran + H2O
?
-
-
-
-
?
dextran + H2O
?
-
-
-
-
?
dextran + H2O
beta-D-glucose
-
-
-
-
?
dextran + H2O
beta-D-glucose
-
-
-
-
?
dextran + H2O
beta-D-glucose
-
dextran glucosidase is highly specific to alpha-1,6-glucosidic linkage at the non-reducing end of dextran (i.e., water-soluble alpha-1,6-linked glucan)
-
-
?
dextran + H2O
D-glucose + ?
-
-
-
?
dextran + H2O
D-glucose + ?
catalytic efficiency on dextran and dextran/panose
-
-
?
dextran + H2O
D-glucose + ?
-
-
-
?
dextran + H2O
D-glucose + ?
catalytic efficiency on dextran and dextran/panose
-
-
?
dextran + H2O
glucose
-
-
-
-
?
dextran + H2O
glucose
-
-
-
-
?
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
dextrans + H2O
beta-D-glucose
-
-
-
ir
isomaltodextrins + H2O
beta-D-glucose
-
-
-
ir
isomaltodextrins + H2O
beta-D-glucose
-
-
-
ir
isomaltodextrins + H2O
beta-D-glucose
-
-
-
ir
isomaltodextrins + H2O
beta-D-glucose
-
-
-
ir
isomaltodextrins + H2O
beta-D-glucose
-
-
-
ir
isomaltodextrins + H2O
beta-D-glucose
-
-
-
ir
isomaltodextrins + H2O
beta-D-glucose
-
-
-
ir
isomaltodextrins + H2O
beta-D-glucose
-
-
-
ir
isomaltodextrins + H2O
beta-D-glucose
-
-
-
ir
isomaltodextrins + H2O
beta-D-glucose
-
-
-
ir
isomaltodextrins + H2O
beta-D-glucose
-
-
-
ir
isomaltooligosaccharide + H2O
D-glucose + ?
-
-
-
?
isomaltooligosaccharide + H2O
D-glucose + ?
degradation
-
-
?
isomaltose + H2O
2 D-glucose
-
54.06% hydrolysis
-
-
?
isomaltose + H2O
2 D-glucose
-
54.06% hydrolysis
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
2 D-glucose
-
-
-
?
isomaltose + H2O
beta-D-glucose
-
-
-
?
isomaltose + H2O
beta-D-glucose
-
-
-
?
isomaltotetraose + H2O
?
-
-
-
?
isomaltotetraose + H2O
?
-
-
-
?
isomaltotriose + H2O
?
-
-
-
?
isomaltotriose + H2O
?
-
-
-
?
isomaltotriose + H2O
beta-D-glucose
-
-
-
?
isomaltotriose + H2O
beta-D-glucose
-
-
-
?
isomaltotriose + H2O
D-glucose
-
-
-
?
isomaltotriose + H2O
D-glucose
221% of the activity with isomaltose, wild-type enzyme
-
-
?
isomaltulose + H2O
D-glucose
-
37.3% hydrolysis
-
-
?
isomaltulose + H2O
D-glucose
-
37.3% hydrolysis
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
p-nitrophenyl-alpha-D-glucopyranoside + H2O
p-nitrophenol + alpha-D-glucopyranose
-
-
-
-
?
panose + H2O
D-glucose
-
-
-
-
?
panose + H2O
D-glucose
417% of the activity with isomaltose, wild-type enzyme
-
-
?
panose + H2O
D-glucose + ?
-
-
-
?
panose + H2O
D-glucose + ?
catalytic efficiency on dextran/panose
-
-
?
additional information
?
-
-
the enzyme has no activity with 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-manopyranoside, 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl alpha-D-fucopyranoside, 4-nitrophenyl beta-D-arabinopyranoside, 4-nitrophenyl alpha-D-arabinopyranoside, 4-nitrophenyl alpha-D-maltohexaoside, isomaltrotriose, melibiose, panose and raffinose, trehalose, sucrose, turanose or maltose. The enzyme shows no transglycosylation activity
-
-
?
additional information
?
-
-
the enzyme has no activity with 4-nitrophenyl beta-D-glucopyranoside, 4-nitrophenyl alpha-D-galactopyranoside, 4-nitrophenyl beta-D-galactopyranoside, 4-nitrophenyl alpha-D-manopyranoside, 4-nitrophenyl beta-D-fucopyranoside, 4-nitrophenyl alpha-D-fucopyranoside, 4-nitrophenyl beta-D-arabinopyranoside, 4-nitrophenyl alpha-D-arabinopyranoside, 4-nitrophenyl alpha-D-maltohexaoside, isomaltrotriose, melibiose, panose and raffinose, trehalose, sucrose, turanose or maltose. The enzyme shows no transglycosylation activity
-
-
?
additional information
?
-
no activity with trehalose
-
-
?
additional information
?
-
-
no activity with trehalose
-
-
?
additional information
?
-
dextran glucosidase from Streptococcus mutans catalyzes the hydrolysis of an alpha-1,6-glucosidic linkage at the nonreducing end of isomaltooligosaccharides and dextran
-
-
?
additional information
?
-
dextran glucosidase from Streptococcus mutans catalyzes the hydrolysis of an alpha-1,6-glucosidic linkage at the nonreducing end of isomaltooligosaccharides and dextran
-
-
?
additional information
?
-
-
dextran glucosidase from Streptococcus mutans catalyzes the hydrolysis of an alpha-1,6-glucosidic linkage at the nonreducing end of isomaltooligosaccharides and dextran
-
-
?
additional information
?
-
the enzyme also performs transglucosylation
-
-
?
additional information
?
-
the enzyme also performs transglucosylation
-
-
?
additional information
?
-
-
the enzyme also performs transglucosylation
-
-
?
additional information
?
-
dextran glucosidase from Streptococcus mutans catalyzes the hydrolysis of an alpha-1,6-glucosidic linkage at the nonreducing end of isomaltooligosaccharides and dextran
-
-
?
additional information
?
-
the enzyme also performs transglucosylation
-
-
?
additional information
?
-
the enzyme catalyzes both the hydrolysis of substrates such as isomaltooligosaccharides and subsequent transglucosylation to form alpha-(1->6)-glucosidic linkage at the substrate non-reducing ends
-
-
?
additional information
?
-
the enzyme catalyzes both the hydrolysis of substrates such as isomaltooligosaccharides and subsequent transglucosylation to form alpha-(1->6)-glucosidic linkage at the substrate non-reducing ends
-
-
?
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2.38
4-nitrophenyl-alpha-D-glucopyranoside
purified recombinant enzyme, pH 6.0, 37°C
12 - 81.7
isomaltoheptaose
7.88 - 76.9
isomaltohexaose
5.1 - 38.3
isomaltopentaose
5.58 - 20.9
isomaltotetraose
3.17 - 14.1
isomaltotriose
244.52
isomaltulose
-
at pH 5.5 and 37°C
0.549 - 41.4
p-nitrophenyl alpha-D-glucoside
additional information
additional information
-
0.012
Dextran
-
-
29.1
Dextran
purified recombinant enzyme, pH 6.0, 37°C
12
isomaltoheptaose
pH 6.0, 37°C, wild-type enzyme
26.9
isomaltoheptaose
pH 6.0, 37°C, mutant enzyme W238N
43.6
isomaltoheptaose
pH 6.0, 37°C, mutant enzyme W238P
81.7
isomaltoheptaose
pH 6.0, 37°C, mutant enzyme W238A
7.88
isomaltohexaose
pH 6.0, 37°C, wild-type enzyme
19.9
isomaltohexaose
pH 6.0, 37°C, mutant enzyme W238N
27.1
isomaltohexaose
pH 6.0, 37°C, mutant enzyme W238P
76.9
isomaltohexaose
pH 6.0, 37°C, mutant enzyme W238A
5.1
isomaltopentaose
pH 6.0, 37°C, wild-type enzyme
15.1
isomaltopentaose
pH 6.0, 37°C, mutant enzyme W238N
24.6
isomaltopentaose
pH 6.0, 37°C, mutant enzyme W238P
38.3
isomaltopentaose
pH 6.0, 37°C, mutant enzyme W238A
6.22
isomaltose
-
at pH 5.5 and 37°C
8.91
isomaltose
pH 6.0, 37°C, mutant enzyme W238N
9.35
isomaltose
pH 6.0, 37°C, wild-type enzyme
15.8
isomaltose
pH 6.0, 37°C, mutant enzyme W238A
20.5
isomaltose
pH 6.0, 37°C, mutant enzyme W238P
22.5
isomaltose
purified recombinant enzyme, pH 6.0, 37°C
5.58
isomaltotetraose
pH 6.0, 37°C, wild-type enzyme
7.77
isomaltotetraose
pH 6.0, 37°C, mutant enzyme W238N
16.1
isomaltotetraose
pH 6.0, 37°C, mutant enzyme W238P
16.1
isomaltotetraose
purified recombinant enzyme, pH 6.0, 37°C
20.9
isomaltotetraose
pH 6.0, 37°C, mutant enzyme W238A
3.17
isomaltotriose
pH 6.0, 37°C, wild-type enzyme
4.96
isomaltotriose
pH 6.0, 37°C, mutant enzyme W238N
10.2
isomaltotriose
pH 6.0, 37°C, mutant enzyme W238P
11.4
isomaltotriose
pH 6.0, 37°C, mutant enzyme W238A
14.1
isomaltotriose
purified recombinant enzyme, pH 6.0, 37°C
0.549
p-nitrophenyl alpha-D-glucoside
pH 6.0, 37°C, wild-type enzyme
9.92
p-nitrophenyl alpha-D-glucoside
pH 6.0, 37°C, mutant enzyme W238N
19
p-nitrophenyl alpha-D-glucoside
pH 6.0, 37°C, mutant enzyme W238A
41.4
p-nitrophenyl alpha-D-glucoside
pH 6.0, 37°C, mutant enzyme W238P
1.03
panose
pH 6.0, 37°C, wild-type enzyme
2.2
panose
pH 6.0, 37°C, mutant enzyme W238N
3.9
panose
purified recombinant enzyme, pH 6.0, 37°C
4.22
panose
pH 6.0, 37°C, mutant enzyme W238A
6.41
panose
pH 6.0, 37°C, mutant enzyme W238P
additional information
additional information
Michaelis-Menten kinetics
-
additional information
additional information
-
Michaelis-Menten kinetics
-
additional information
additional information
-
KM-value for dextran is 0.031 mg/ml
-
additional information
additional information
detailed steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
detailed steady-state kinetics of wild-type and mutant enzymes, overview
-
additional information
additional information
-
detailed steady-state kinetics of wild-type and mutant enzymes, overview
-
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597
4-nitrophenyl-alpha-D-glucopyranoside
purified recombinant enzyme, pH 6.0, 37°C
9.81 - 449
isomaltoheptaose
0.04 - 419
isomaltopentaose
0.04 - 501
isomaltotetraose
12.2 - 541
isomaltotriose
61.4 - 1202
p-nitrophenyl alpha-D-glucoside
95.2
Dextran
-
-
384
Dextran
purified recombinant enzyme, pH 6.0, 37°C
9.81
isomaltoheptaose
pH 6.0, 37°C, mutant enzyme W238N
33.2
isomaltoheptaose
pH 6.0, 37°C, mutant enzyme W238A
56.5
isomaltoheptaose
pH 6.0, 37°C, mutant enzyme W238P
449
isomaltoheptaose
pH 6.0, 37°C, wild-type enzyme
3 - 6
isomaltohexaose
pH 6.0, 37°C, mutant enzyme W238A
7.8
isomaltohexaose
pH 6.0, 37°C, mutant enzyme W238N
39.6
isomaltohexaose
pH 6.0, 37°C, mutant enzyme W238P
401
isomaltohexaose
pH 6.0, 37°C, wild-type enzyme
0.04 - 1.97
isomaltopentaose
pH 6.0, 37°C, mutant enzyme W238N
9.21
isomaltopentaose
pH 6.0, 37°C, mutant enzyme W238N
22.6
isomaltopentaose
pH 6.0, 37°C, mutant enzyme W238A
42.4
isomaltopentaose
pH 6.0, 37°C, mutant enzyme W238P
419
isomaltopentaose
pH 6.0, 37°C, wild-type enzyme
8.88
isomaltose
pH 6.0, 37°C, mutant enzyme W238N
34.5
isomaltose
pH 6.0, 37°C, mutant enzyme W238A
79.8
isomaltose
pH 6.0, 37°C, mutant enzyme W238P
483
isomaltose
pH 6.0, 37°C, wild-type enzyme
517
isomaltose
purified recombinant enzyme, pH 6.0, 37°C
0.04 - 1.97
isomaltotetraose
pH 6.0, 37°C, mutant enzyme W238N
8.96
isomaltotetraose
pH 6.0, 37°C, mutant enzyme W238N
22.3
isomaltotetraose
pH 6.0, 37°C, mutant enzyme W238A
52.5
isomaltotetraose
pH 6.0, 37°C, mutant enzyme W238P
499
isomaltotetraose
pH 6.0, 37°C, wild-type enzyme
501
isomaltotetraose
purified recombinant enzyme, pH 6.0, 37°C
12.2
isomaltotriose
pH 6.0, 37°C, mutant enzyme W238N
33.1
isomaltotriose
pH 6.0, 37°C, mutant enzyme W238A
77.5
isomaltotriose
pH 6.0, 37°C, mutant enzyme W238P
475
isomaltotriose
purified recombinant enzyme, pH 6.0, 37°C
541
isomaltotriose
pH 6.0, 37°C, wild-type enzyme
61.4
p-nitrophenyl alpha-D-glucoside
pH 6.0, 37°C, mutant enzyme W238N
202
p-nitrophenyl alpha-D-glucoside
pH 6.0, 37°C, mutant enzyme W238A
235
p-nitrophenyl alpha-D-glucoside
pH 6.0, 37°C, wild-type enzyme
1202
p-nitrophenyl alpha-D-glucoside
pH 6.0, 37°C, mutant enzyme W238P
22.4
panose
pH 6.0, 37°C, mutant enzyme W238N
42.1
panose
pH 6.0, 37°C, mutant enzyme W238A
121
panose
pH 6.0, 37°C, mutant enzyme W238P
538
panose
pH 6.0, 37°C, wild-type enzyme
612
panose
purified recombinant enzyme, pH 6.0, 37°C
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evolution
the enzyme belongs to the glycosyl hydrolase family 13
evolution
the enzyme belongs to the glycosyl hydrolase family 13 subfamily 31
evolution
the enzyme belongs to the glycosyl hydrolase family 13, GH13
evolution
-
the enzyme belongs to the glycosyl hydrolase family 13
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 13, GH13
-
evolution
-
the enzyme belongs to the glycosyl hydrolase family 13 subfamily 31
-
physiological function
-
dextran glucosidases is an important enzyme involved in the dental plaque biofilm formation
physiological function
coregulation of alpha-1,6- and alpha-1,4-glucooligosaccharide utilization loci in the organism
physiological function
-
coregulation of alpha-1,6- and alpha-1,4-glucooligosaccharide utilization loci in the organism
-
additional information
phylogenetic and activity motif analysis, overview. Catalytic residues are Asp198 and Glu240, active site structure, overview
additional information
-
phylogenetic and activity motif analysis, overview. Catalytic residues are Asp198 and Glu240, active site structure, overview
additional information
the enzyme has an Asp194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys129 and Cys532
additional information
the enzyme has an Asp194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys129 and Cys532
additional information
-
the enzyme has an Asp194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys129 and Cys532
additional information
the enzyme has an Asp194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys129 and Cys532. Asp194 is essential for enzyme activity
additional information
the enzyme has an Asp194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys129 and Cys532. Asp194 is essential for enzyme activity
additional information
-
the enzyme has an Asp194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys129 and Cys532. Asp194 is essential for enzyme activity
additional information
-
the enzyme has an Asp194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys129 and Cys532
-
additional information
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the enzyme has an Asp194 catalytic nucleophile and two catalytically unrelated Cys residues, Cys129 and Cys532. Asp194 is essential for enzyme activity
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additional information
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phylogenetic and activity motif analysis, overview. Catalytic residues are Asp198 and Glu240, active site structure, overview
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E458Q
-
mutant enzyme shows 0.0005% of the wild-type activity
E656Q
-
mutant enzyme shows 0.0003% of the wild-type activity
E458Q
-
mutant enzyme shows 0.0005% of the wild-type activity
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E656Q
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mutant enzyme shows 0.0003% of the wild-type activity
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D318A
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shows an activity level identical to that of the wild-type
E94A
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shows a relatively minor change in the alpha-1,6-glucosidase activity, but a sharply increased alpha-1,4-transferase activity compared with the wild-type
C129S/C532S
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme, the mutant predominantly catalyzes hydrolysis
D194A/C129S/C532S
site-directed mutagenesis
D194C/C129S/C532S
site-directed mutagenesis, the mutant shows highly reduced activity compared with the wild-type enzyme and mutant C129S/C532S, oxidation with KI activates the mutant by 330fold which is 0.27% activity of the activity of mutant C129S/C532S, the oxidized mutant Ox-D194C-2CS catalyzes both hydrolysis and transglucosylation
E236Q
catalysis is compromised in complex with isomaltotriose
W238A
mutant shows lower preference for kojibiose, nigerose, and sucrose and higher preference for maltooligosaccharides, trehalose, and p-nitrophenyl alpha-D-glucoside. Altough trehalose is not a substrate for the wild-type, the mutant enzyme hydrolyzes trehalose
W238N
mutant shows lower preference for kojibiose, nigerose, and sucrose and higher preference for maltooligosaccharides, trehalose, and p-nitrophenyl alpha-D-glucoside. Altough trehalose is not a substrate for the wild-type, the mutant enzyme hydrolyzes trehalose
W238P
mutant shows lower preference for kojibiose, nigerose, and sucrose and higher preference for maltooligosaccharides, trehalose, and p-nitrophenyl alpha-D-glucoside. Altough trehalose is not a substrate for the wild-type, the mutant enzyme hydrolyzes trehalose
C129S/C532S
-
site-directed mutagenesis, the mutant shows unaltered activity compared to the wild-type enzyme, the mutant predominantly catalyzes hydrolysis
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D194A/C129S/C532S
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site-directed mutagenesis
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D194C/C129S/C532S
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site-directed mutagenesis, the mutant shows highly reduced activity compared with the wild-type enzyme and mutant C129S/C532S, oxidation with KI activates the mutant by 330fold which is 0.27% activity of the activity of mutant C129S/C532S, the oxidized mutant Ox-D194C-2CS catalyzes both hydrolysis and transglucosylation
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F262A
the mutant enzyme has a stronger preference for transglucosylation than that of the wild type enzyme
F262W
the mutant enzyme has a weaker preference for transglucosylation than that of the wild type enzyme
F262A
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the mutant enzyme has a stronger preference for transglucosylation than that of the wild type enzyme
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F262W
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the mutant enzyme has a weaker preference for transglucosylation than that of the wild type enzyme
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additional information
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construction of deletion mutants in regions A and B, all mutants enzymatically active, analysis of substrate chain-length, kinetics. Lack of the extension of loop 4 leads to higher relative activities toward dextran and long-chain isomaltooligosaccharides
additional information
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construction of deletion mutants in regions A and B, all mutants enzymatically active, analysis of substrate chain-length, kinetics. Lack of the extension of loop 4 leads to higher relative activities toward dextran and long-chain isomaltooligosaccharides
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304
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brenda
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brenda
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Thermostable alpha-1,4- and alpha-1,6-glucosidase enzymes from Bacillus sp. isolated from a marine environment
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Structural elements in dextran glucosidase responsible for high specificity to long chain substrate
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Streptococcus mutans (Q2HWU5), Streptococcus mutans
brenda
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X-ray crystallographic study of glucodextranase from a Gram-positive bacterium, Arthrobacter globiformis I42
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52
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-
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Crystallization and preliminary X-ray analysis of Streptococcus mutans dextran glucosidase
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Streptococcus mutans
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Streptococcus mutans (Q99040), Streptococcus mutans
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Calcium ion-dependent increase in thermostability of dextran glucosidase from Streptococcus mutans
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Streptococcus mutans
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Dextran glucosidase: a potential target of iminosugars in caries prevention
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Streptococcus mutans
brenda
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Enzymology and structure of the GH13_31 glucan 1,6-alpha-glucosidase that confers isomaltooligosaccharide utilization in the probiotic Lactobacillus acidophilus NCFM
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Streptococcus mutans serotype c (Q99040), Streptococcus mutans serotype c ATCC 700610 (Q99040)
brenda
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Lactiplantibacillus plantarum, Lactiplantibacillus plantarum LL441
brenda