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Co2+
-
-
Co2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity
Co2+
-
less effective than Mg2+ in D-fructose isomerization
Co2+
-
less effective than Mg2+ in D-xylose isomerization
Co2+
-
XI is substantially structurally stabilized in the presence of CO2+
Co2+
-
when the metal ions are added separately the activation is 48-52%. The combination of Mg2+ and Co2+ results in activation of 83%. The combination of Mg2+ and Mn2+ or Co2+ and Mn2+ results in 58-59% activation
Co2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity
Co2+
-
the presence of Co2+ is associated with isozyme T80
Co2+
-
maximal activity in presence of both, 10 mM Mg2+ and 1 mM Co2+
Co2+
-
XI is substantially structurally stabilized in the presence of CO2+
Co2+
-
can only partially substitute for Mg2+
Co2+
-
with D-xylose as substrate, the activity is increased by the addition of 1 mM Co2+ (1.9fold). A mixture of 0.5 mM Co2+ and 0.5 mM Mn2+ increases the enzyme activity 3.2fold. Glucose isomerase activity is maximally enhanced by the addition of 5 mM Co2+
Co2+
-
purified T90 isoform, 100% activity at 10 mM Mn2+ plus 1 mM Co2+
Co2+
Opuntia vulgaris
-
purified T90 isoform, 100% activity at 10 mM Mn2+ plus 1 mM Co2+
Co2+
-
depends on the origin of the enzyme
Co2+
-
the binding sites for Co2+ and Mn2+ are different from each other
Co2+
-
1.0 mM, partial activation, Km: 0.003 mM
Co2+
-
required for activity
Co2+
-
Mg2+ or Co2+ required for activity
Co2+
-
two metal ions bind per subunit to non-identical sites. Mg2+, Mn2+, and Co2+ are of comparable efficiency for the D-xylose isomerization. Co2+ is the most efficient cofactor for D-glucose isomerization
Co2+
D-xylose and D-glucose isomerase activities of XylA are enhanced by Co2+. When 1 mM Co2+ and 10 mM Mg2+ are added together, the activity of XylA is increased by about 10% compared to 1 mM Co2+ only
Co2+
-
XI is substantially structurally stabilized in the presence of CO2+
Co2+
-
required for thermostability
Co2+
-
most effective activator of D-glucose isomerization
Co2+
-
depends on the origin of the enzyme
Co2+
59% activity compared to Mn2+
Co2+
-
the binding sites for Co2+ and Mn2+ are different from each other
Co2+
-
most effectively activates D-glucose isomerization and D-ribose isomerization
Co2+
-
required for D-glucose isomerization
Co2+
-
Co2+ is bound to the enzyme in a molar ratio of 4:1
Fe2+
activates
Mg2+
-
-
Mg2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity
Mg2+
-
best activator of D-fructose isomerization
Mg2+
-
most effective in activation of D-xylose isomerization
Mg2+
-
XI is to a lesser extent structurally stabilized in the presence of Mg2+
Mg2+
-
when the metal ions are added separately the activation is 48-52%. The combination of Mg2+ and Co2+ results in activation of 83%. The combination of Mg2+ and Mn2+ or Co2+ and Mn2+ results in 58-59% activation
Mg2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity
Mg2+
-
stabilzes the enzyme
Mg2+
-
maximal activity in presence of both, 10 mM Mg2+ and 1 mM Co2+
Mg2+
-
XI is to a lesser extent structurally stabilized in the presence of Mg2+
Mg2+
-
included in assay medium
Mg2+
-
preferred metal ion, activates by 15-20%
Mg2+
-
glucose isomerase activity is maximally enhanced by the addition of 5 mM Mg2+
Mg2+
-
depends on the origin of the enzyme
Mg2+
-
the binding sites for Co2+ and Mn2+ are different from each other
Mg2+
-
1.0 mM, strong activation, Km: 0.03 mM
Mg2+
-
required for activity, most effective cation
Mg2+
-
Co2+ or Mg2+ required for activity
Mg2+
used in assay conditions
Mg2+
-
two metal ions bind per subunit to non-identical sites. Mg2+, Mn2+, and Co2+ are of comparable efficiency for the D-xylose isomerization
Mg2+
-
activates, maximal activity at 10 mM
Mg2+
D-xylose and D-glucose isomerase activities of XylA are enhanced by Mg2+
Mg2+
-
XI is to a lesser extent structurally stabilized in the presence of Mg2+
Mg2+
-
activates D-glucose isomerization, D-xylose isomerization and D-ribose isomerization
Mg2+
-
depends on the origin of the enzyme
Mg2+
recombinant XylA requires the addition of Mg2+ for optimum activity (100%)
Mg2+
-
activates D-glucose isomerization, D-xylose isomerization and D-ribose isomerization
Mn2+
-
-
Mn2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity
Mn2+
-
less effective than Mg2+ in activation of D-xylose isomerization
Mn2+
-
less effective than Mg2+ in activation of D-fructose isomerization
Mn2+
-
XI is substantially structurally stabilized in the presence of Mn2+
Mn2+
-
when the metal ions are added separately the activation is 48-52%. The combination of Mg2+ and Co2+ results in activation of 83%. The combination of Mg2+ and Mn2+ or Co2+ and Mn2+ results in 58-59% activation
Mn2+
-
Mg2+, Mn2+ or Co2+ required for maximal activity
Mn2+
-
the presence of Mn2+ is associated with isozyme T80
Mn2+
-
XI is substantially structurally stabilized in the presence of Mn2+
Mn2+
-
specifically required
Mn2+
-
with D-xylose as substrate, the activity is increased by the addition of 1 mM Mn2+ (2.9fold). A mixture of 0.5 mM Co2+ and 0.5 mM Mn2+ increases the enzyme activity 3.2fold. Glucose isomerase activity is maximally enhanced by the addition of 5 mM Mn2+
Mn2+
-
purified T90 isoform, 100% activity at 10 mM Mn2+ plus 1 mM Co2+
Mn2+
Opuntia vulgaris
-
purified T90 isoform, 100% activity at 10 mM Mn2+ plus 1 mM Co2+
Mn2+
-
depends on the origin of the enzyme
Mn2+
-
required for activity
Mn2+
essential for activity, there are two manganese atoms visible in the atomic resolution study
Mn2+
-
two metal ions bind per subunit to non-identical sites. Mg2+, Mn2+, and Co2+ are of comparable efficiency for the D-xylose isomerization
Mn2+
D-xylose isomerase activity of XylA is enhanced by Mn2+
Mn2+
-
XI is substantially structurally stabilized in the presence of Mn2+
Mn2+
-
required for thermostability
Mn2+
-
most effectively activates D-xylose isomerization
Mn2+
-
depends on the origin of the enzyme
Mn2+
maximal activity with 1 mM Mn2+
Mn2+
41% activity compared to Mn2+
Mn2+
-
the binding sites for Co2+ and Mn2+ are different from each other
Mn2+
-
most effectively activates D-xylose isomerization
Mn2+
-
required for D-xylose isomerization
Zn2+
-
weak cofactor for D-glucose isomerization
Zn2+
-
activates D-xylose isomerization
additional information
-
two metal sites: metal site 1 is four-coordinated and tetrahedral in the absence of substrate and is six-coordinated and octahedral in its presence, the O2 and O4 atoms of the linear inhibitors and substrate bind to the metal 1. Metal site 2 is octahedral in all cases, its position changes by 0.7 A when it binds O1 of the substrate and by more than 1 A when it also binds O2
additional information
no activity with Fe2+, Fe3+, Ni2+, and Cu2+
additional information
-
no activity with Fe2+, Fe3+, Ni2+, and Cu2+
additional information
not stimulated by K+, Ni2+ and Zn2+
additional information
-
not stimulated by K+, Ni2+ and Zn2+
additional information
addition of Ca2+, Zn2+, Fe2+, or Cu2+ is not effective
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3
D-glyceraldehyde
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
215
D-Lyxose
mutant enzyme D256R, at pH 7.0 and 85°C
additional information
additional information
-
50
D-fructose
-
D-xylose, mutant E181Q
110
D-fructose
-
with 10-400 mM Mg2+
800
D-fructose
-
with 1-10 mM Mg2+
0.249
D-glucose
-
soluble enzyme
0.297
D-glucose
-
immobilized enzyme
52
D-glucose
-
60°C, pH 7, mutant E372G/V379A
65.2
D-glucose
-
soluble wild type enzyme, at 80°C, pH 7.0
86
D-glucose
-
D-lyxose, 30°C
88.5
D-glucose
-
soluble wild type enzyme, at 90°C, pH 7.0
121.5
D-glucose
-
immobilized CBD-TNX fusion protein, at 80°C, pH 7.0
130
D-glucose
-
D-glucose, mutant enzyme His71Phe
130.8
D-glucose
-
60°C, pH 7, mutant E372G/F163L
138
D-glucose
-
mutant enzyme His101Gln
142
D-glucose
-
glucose, wild-type enzyme
146.8
D-glucose
-
60°C, pH 7, wild-type
148.9
D-glucose
-
immobilized CBD-TNX fusion protein, at 90°C, pH 7.0
152
D-glucose
-
mutant enzyme His152Phe
157.8
D-glucose
-
unbound CBD-TNX fusion protein, at 80°C, pH 7.0
160
D-glucose
-
60°C, pH 7.3, with Co2+, wild-type
168
D-glucose
-
mutant enzyme His101Asn
171.8
D-glucose
-
60°C, pH 7, mutant E372G
180
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D81A and wild-type
187
D-glucose
in 50 mM sodium phosphate buffer (pH 7.5), at 40°C
190
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D65A
198
D-glucose
-
mutant enzyme His101Asp
200
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q
244
D-glucose
mutant V135N
250
D-glucose
-
D-fructose, 60°C
252
D-glucose
-
mutant enzyme His101Glu
259.6
D-glucose
-
enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
259.6
D-glucose
Opuntia vulgaris
-
enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
290
D-glucose
-
wild-type enzyme
300
D-glucose
-
mutant D257N
310
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutants E221A and D56N
340
D-glucose
-
60°C, pH 7.3, with Co2+, mutant E221A
400
D-glucose
-
D-glucose, mutant H220Q
500
D-glucose
-
mutant H220N
536.1
D-glucose
-
unbound CBD-TNX fusion protein, at 90°C, pH 7.0
1099
D-glucose
-
at pH 5.0 and 65°C
1600
D-glucose
-
mutant F26W
1900
D-glucose
-
wild-type
2400
D-glucose
-
mutant E181D
5800
D-glucose
-
mutant D257E
185
D-mannose
mutant enzyme D256R, at pH 7.0 and 85°C
1005
D-mannose
wild type enzyme, at pH 7.0 and 85°C
77
D-ribose
-
-
0.076
D-xylose
-
-
0.078
D-xylose
-
soluble enzyme
0.104
D-xylose
-
immobilized enzyme
1 - 4
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
1 - 1.2
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
2.25
D-xylose
-
wild-type
2.9
D-xylose
-
with 10 mM Mg2+
3
D-xylose
-
native wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
3.3
D-xylose
-
D-xylose, with 30 mM Mg2+
3.3
D-xylose
-
D-xylose, 30°C
3.3
D-xylose
-
with 1 mM Co2+
3.4
D-xylose
-
mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
3.44
D-xylose
-
60°C, pH 7, wild-type
3.46
D-xylose
-
mutant R202M/Y218D/V275A
3.8
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
4 - 5
D-xylose
-
mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
4.3
D-xylose
-
mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
4.4
D-xylose
-
mutant S388T/K407E
4.8
D-xylose
-
wild-type enzyme
4.9
D-xylose
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
5
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
5.3
D-xylose
-
mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
6
D-xylose
-
mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
6.5
D-xylose
-
mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
7.4
D-xylose
-
mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
7.93
D-xylose
in 50 mM sodium phosphate buffer (pH 7.5), at 40°C
8
D-xylose
-
mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
10
D-xylose
-
mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
11
D-xylose
at 80°C in 100 mM MOPS buffer, pH 7.0
11.7
D-xylose
pH 7.0, 60°C, mutant N91D/D375G
11.8
D-xylose
pH 7.0, 60°C, mutant N91D/K355A
15
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
15.2
D-xylose
pH 7.0, 60°C, mutant N91D
16
D-xylose
-
D-xylose, mutant H220Q
21.1
D-xylose
pH 7.0, 60°C, mutant N91D/D375G/V385A
25.1
D-xylose
-
60°C, pH 7, mutant E372G/V379A
27
D-xylose
-
mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
27.1
D-xylose
pH 7.0, 60°C, mutant N91D/V144A
28.7
D-xylose
-
60°C, pH 7, mutant E372G
33
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
37
D-xylose
-
mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
42
D-xylose
-
mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
46.4
D-xylose
-
enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
46.4
D-xylose
Opuntia vulgaris
-
enzyme isoform T90, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
48
D-xylose
-
mutant D257E
49
D-xylose
-
mutant D257N
49.9
D-xylose
-
pH 7.5, recombinant enzyme
50.18
D-xylose
-
mutant enzyme E129D/V433I/E15D/E114G, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C
54.03
D-xylose
-
in 100 mM Tris-HCl buffer (pH 7.5), 10 mM MgCl2, at 30°C
61.9
D-xylose
-
pH 7.5, native enzyme
66
D-xylose
-
mutant D255N
66
D-xylose
-
pH 7.5, recombinant enzyme
73
D-xylose
-
mutant E181D
83
D-xylose
-
native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
86.97
D-xylose
-
wild type enzyme, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C
89.4
D-xylose
-
60°C, pH 7, mutant E372G/F163L
89.98
D-xylose
-
mutant enzyme E129D/V433I, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C
168.4
D-xylose
-
mutant enzyme E129D/V433I/E15D/E114G/T142S/A177T, in 100 mM Tris-HCl buffer at pH 7.5 and 30°C
177.4
D-xylose
-
at pH 5.0 and 65°C
548
D-xylose
-
mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
605
D-xylose
wild type enzyme, at pH 7.0 and 85°C
8
D-xylulose
-
-
138
L-arabinose
mutant enzyme D256R, at pH 7.0 and 85°C
900
L-arabinose
-
mutant Q256D
1400
L-arabinose
-
mutant F26W
1450
L-arabinose
wild type enzyme, at pH 7.0 and 85°C
1500
L-arabinose
-
wild-type
438
L-ribose
mutant V135N
additional information
additional information
-
-
-
additional information
additional information
-
Km-values for wild-type enzyme and mutants E186D and E186Q, activated by Mg2+, Mn2+ or Co2+
-
additional information
additional information
-
Km-value for D-xylose varies with the concentration Mn2+
-
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0.0001
D-glyceraldehyde
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
additional information
additional information
-
turnover numbers for wild-type enzyme and mutant enzymes E186D and E186Q, activated by Mg2+, Mn2+ or Co2+
-
1.67
D-fructose
-
30°C
0.03 - 0.55
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant E221A
0.031 - 0.51
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D56N
0.04 - 1.97
D-glucose
-
60°C, pH 7.3, with Co2+, mutant E221A
0.2
D-glucose
-
mutant H220N
0.7
D-glucose
-
mutant H220Q
0.7
D-glucose
-
60°C, pH 7, mutant E372G/F163L
0.833
D-glucose
-
60°C, pH 7, wild-type
3 - 6
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q
3 - 6
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D65A
3 - 6
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D81A
3.02
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D163N/E167Q
3.3
D-glucose
-
60°C, pH 7.3, with Co2+, wild-type
3.3
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, wild-type
3.37
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D65A
3.41
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D81A
3.47
D-glucose
mutant V135N
4.53
D-glucose
-
60°C, pH 7.3, with Co2+, wild-type
4.54
D-glucose
in 50 mM sodium phosphate buffer (pH 7.5), at 40°C
5
D-glucose
-
mutant D257N
5.27
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, wild-type
6.99
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant E221A
7.53
D-glucose
-
60°C, pH 7.3, with Mg2+ and Co2+, mutant D56N
9.22
D-glucose
-
60°C, pH 7.3, with Co2+, mutant E221A
9.3
D-glucose
-
mutant E181D
15.5
D-glucose
-
at pH 5.0 and 65°C
16.2
D-glucose
-
soluble wild type enzyme, at 80°C, pH 7.0
16.3
D-glucose
-
60°C, pH 7, wild-type
17.7
D-glucose
-
mutant D257E
19
D-glucose
-
soluble wild type enzyme, at 90°C, pH 7.0
20.5
D-glucose
-
mutant F26W
23.8
D-glucose
-
60°C, pH 7, mutant E372G
24.9
D-glucose
-
wild-type enzyme
25.3
D-glucose
-
wild-type
39.9
D-glucose
-
60°C, pH 7, mutant E372G/V379A
63.3
D-glucose
-
unbound CBD-TNX fusion protein, at 80°C, pH 7.0
66.9
D-glucose
-
60°C, pH 7, mutant E372G/F163L
88.7
D-glucose
-
60°C, pH 7, mutant E372G
96.3
D-glucose
-
immobilized CBD-TNX fusion protein, at 80°C, pH 7.0
116
D-glucose
-
immobilized CBD-TNX fusion protein, at 90°C, pH 7.0
172.6
D-glucose
-
unbound CBD-TNX fusion protein, at 90°C, pH 7.0
0.0617
D-Lyxose
-
30°C
25
D-Lyxose
wild type enzyme, at pH 7.0 and 85°C
38
D-Lyxose
mutant enzyme D256R, at pH 7.0 and 85°C
2 - 8
D-mannose
mutant enzyme D256R, at pH 7.0 and 85°C
18
D-mannose
wild type enzyme, at pH 7.0 and 85°C
0.007
D-xylose
-
mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.05
D-xylose
-
mutant H220N
0.056
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.064
D-xylose
-
mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.07
D-xylose
-
mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.074
D-xylose
-
mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.08
D-xylose
-
mutant E217S
0.1
D-xylose
-
mutant E181Q
0.11
D-xylose
-
mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.14
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.15
D-xylose
-
mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.18
D-xylose
-
mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.19
D-xylose
-
mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.31
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.33
D-xylose
-
mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.41
D-xylose
-
native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.5
D-xylose
-
mutant D255N
0.51
D-xylose
-
mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.6
D-xylose
-
mutant H220Q
0.66
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.8
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.9
D-xylose
-
mutant D257N
0.96
D-xylose
-
mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
1.22
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
1.38
D-xylose
-
mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
1.5
D-xylose
-
mutant E181D
2.3
D-xylose
-
mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
2.4
D-xylose
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
2.8
D-xylose
-
with 1 mM Co2+
3.4
D-xylose
-
mutant D257E
4.15
D-xylose
-
with 10 mM Mg2+
5.52
D-xylose
-
native wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
17.3
D-xylose
-
wild-type enzyme
46.6
D-xylose
-
60°C, pH 7, wild-type
47
D-xylose
in 50 mM sodium phosphate buffer (pH 7.5), at 40°C
50.7
D-xylose
pH 7.0, 60°C, mutant N91D
61.65
D-xylose
pH 7.0, 60°C, mutant N91D/D375G/V385A
68.39
D-xylose
pH 7.0, 60°C, mutant N91D/D375G
70.8
D-xylose
-
60°C, pH 7, mutant E372G/F163L
116
D-xylose
pH 7.0, 60°C, mutant N91D/K355A
124
D-xylose
-
mutant S388T/K407E
142
D-xylose
-
mutant R202M/Y218D/V275A
146.6
D-xylose
-
at pH 5.0 and 65°C
160.5
D-xylose
pH 7.0, 60°C, mutant N91D/V144A
257.5
D-xylose
-
60°C, pH 7, mutant E372G/V379A
258
D-xylose
-
60°C, pH 7, mutant E372G/V379A
0.1
L-arabinose
-
wild-type
0.155
L-arabinose
-
mutant F26W
0.158
L-arabinose
-
mutant Q256D
6.5
L-arabinose
wild type enzyme, at pH 7.0 and 85°C
13
L-arabinose
mutant enzyme D256R, at pH 7.0 and 85°C
0.0226
L-ribose
mutant V135N
0.0252
L-ribose
wild-type
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0.000034
D-glyceraldehyde
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
0.014
D-glucose
-
at pH 5.0 and 65°C
0.024
D-glucose
in 50 mM sodium phosphate buffer (pH 7.5), at 40°C
0.22
D-glucose
-
soluble wild type enzyme, at 90°C, pH 7.0
0.25
D-glucose
-
soluble wild type enzyme, at 80°C, pH 7.0
0.32
D-glucose
-
unbound CBD-TNX fusion protein, at 90°C, pH 7.0
0.4
D-glucose
-
unbound CBD-TNX fusion protein, at 80°C, pH 7.0
0.78
D-glucose
-
immobilized CBD-TNX fusion protein, at 90°C, pH 7.0
0.79
D-glucose
-
immobilized CBD-TNX fusion protein, at 80°C, pH 7.0
0.041
D-Lyxose
wild type enzyme, at pH 7.0 and 85°C
0.17
D-Lyxose
mutant enzyme D256R, at pH 7.0 and 85°C
0.017
D-mannose
wild type enzyme, at pH 7.0 and 85°C
0.15
D-mannose
mutant enzyme D256R, at pH 7.0 and 85°C
0.00013
D-xylose
-
mutant enzyme D57H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0018
D-xylose
-
mutant enzyme N247D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0019
D-xylose
-
mutant enzyme K289E, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0024
D-xylose
-
mutant enzyme K289H, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0037
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0049
D-xylose
-
native wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.007
D-xylose
-
mutant enzyme D57N, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.0094
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.01
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.018
D-xylose
-
mutant enzyme N247D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.019
D-xylose
-
mutant enzyme N215D, in 100 mM MES-NaOH (pH 5.8), 20 mM MgCl2, at 25°C
0.023
D-xylose
-
mutant enzyme Q256D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.024
D-xylose
-
mutant enzyme D57H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.059
D-xylose
-
mutant enzyme E186Q/N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.064
D-xylose
-
mutant enzyme K289E, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.181
D-xylose
-
mutant enzyme D57N, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.211
D-xylose
-
recombinant His12-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.24
D-xylose
-
recombinant His6-tagged wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.321
D-xylose
-
mutant enzyme K289H, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.49
D-xylose
in D2O, 24 mM imidazole buffer, 10 mM MgCl2, at pH 7.5 and 25°C
0.676
D-xylose
-
mutant enzyme N215D, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
0.83
D-xylose
-
at pH 5.0 and 65°C
1.84
D-xylose
-
native wild type enzyme, in 100 mM HEPES-NaOH (pH 7.7), 20 mM MgCl2, at 25°C
2.92
D-xylose
pH 7.0, 60°C, mutant N91D/D375G/V385A
3.35
D-xylose
pH 7.0, 60°C, mutant N91D
5.87
D-xylose
pH 7.0, 60°C, mutant N91D/D375G
5.92
D-xylose
pH 7.0, 60°C, mutant N91D/V144A
5.93
D-xylose
in 50 mM sodium phosphate buffer (pH 7.5), at 40°C
9.8
D-xylose
pH 7.0, 60°C, mutant N91D/K355A
0.008
L-arabinose
wild type enzyme, at pH 7.0 and 85°C
0.09
L-arabinose
mutant enzyme D256R, at pH 7.0 and 85°C
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0.00323
-
Escherichia coli K-12, control, expression analysis
0.006
-
with D-glucose as substrate
0.0076
-
native enzyme in cell extract
0.008
-
with D-glucose as substrate
0.00933
-
Pgap-xylA/xylB-Pgap-tal/tktA, expression analysis
0.00978
-
Pgap-xylA/xylB-Peno-tal/tktA, expression analysis
0.012
-
transformant delta-xyl1No.4(pEc)No.2b
0.013
-
transformant delta-xyl1No.4(pEc)No.2a
0.014
-
transformant delta-xyl1No.4(pScoel)No.4
0.015
-
transformant delta-xyl1No.4(pScoel)No.12
0.034
-
Pseudomonas putida S12 strain xylAB containing xylose isomerase and xylulokinase gene from Escherichia coli
0.0344
-
recombinant enzyme in yeast cell extract
0.04
-
Saccharomyces cerevisiae overexpressing xylose isomerase from Thermus thermophilus, 30°C
0.042
-
+/-0.003, DELTAxyl1 DELTAxyl2-A(EcxylA) No. 1
0.0455
-
Pgap-xylA/xylB-Pgap-tal/tktA, carbon source: glucose
0.047
-
+/-0.003, DELTAxyl1 DELTAxyl2-A(EcxylA) No. 2
0.05
-
+/-0.004, DELTAxyl1 DELTAxyl2-A(EcxylA) No. 4L/3
0.065
-
Escherichia coli wild-type
0.0653
-
Pgap-xylA/xylB-Pgap-tal/tktA, carbon source: xylose
0.151
-
+/-0.009, DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA HpXYL3)
0.152
-
+/-0.009, DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA) No. 1
0.18
-
CRX1, grown on glucose, aerobic
0.188
-
+/-0.010, DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA) No. 2
0.209
-
+/-0.011, Escherichia coli, control strain
0.22
-
enzyme production in the presence of D-glucose
0.26
-
CRX1, grown on xylose, aerobic
0.27
-
CRX2, grown on xylose, anaerobic, aerobic-phase culture Xyl
0.29
-
CRX2, grown on glucose, anaerobic, aerobic-phase culture Xyl
0.3
-
CRX2, grown on xylose, anaerobic, aerobic-phase culture Glc
0.31
-
CRX2, grown on glucose, anaerobic, aerobic-phase culture Glc
0.35
-
CRX2, grown on glucose, aerobic
0.47
-
enzyme production in the presence of D-xylose
0.57
-
using D-glucose as substrate, at pH 5.0 and 65°C
0.71
-
enzyme production in the presence of D-xylose
0.73
-
enzyme production in the presence of sucrose
0.81
-
enzyme production in the presence of D-glucose
0.82
-
+/-0.01, recombinant Saccharomyces cerevisiae strain TMB 3066
1
-
Saccharomyces cerevisiae overexpressing xylose isomerase from Thermus thermophilus, 85°C
132
wild type enzyme, with L-arabinose as substrate, at pH 7.0 and 85°C
17
after 6fold purification, at pH 7.0 and 85°C
2.2
-
purified recombinant enzyme
2.44
recombinant overexpressing mutant strain
273
wild type enzyme, with D-mannose as substrate, at pH 7.0 and 85°C
3
crude extract, at pH 7.0 and 85°C
330
mutant enzyme D256R, with L-arabinose as substrate, at pH 7.0 and 85°C
380
wild type enzyme, with D-lyxose as substrate, at pH 7.0 and 85°C
682
mutant enzyme D256R, with D-mannose as substrate, at pH 7.0 and 85°C
950
mutant enzyme D256R, with D-lyxose as substrate, at pH 7.0 and 85°C
0.00001
-
empty vector, carbon source: glucose
0.00001
-
empty vector, expression analysis
0.017
-
Saccharomyces cerevisiae overexprssing five own enzymes of pentose phosphate pathway, deletion of an unspecific aldose reductase, overexpressing xylose isomerase from Piromyces sp., 30°C
0.017
-
with D-xylose as substrate
0.46
-
enzyme production in the presence of D-xylose
1.1
-
Saccharomyces cerevisiae overexprssing xylose isomerase from Piromyces sp., 30°C
1.1
-
Saccharomyces cerevisiae strain CEN.PK overexprssing xylose isomerase (xylA gene) from Piromyces sp., TPI1 promoter, 30°C
1.39
-
enzyme production in the presence of xylitol
266.4
-
enzyme isoform T90 after 39.2fold purification with xylose as a substrate, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
266.4
Opuntia vulgaris
-
enzyme isoform T90 after 39.2fold purification with xylose as a substrate, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
6.4
-
-
6.78
-
enzyme isoform T90 from homogenate with xylose as a substrate, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
6.78
Opuntia vulgaris
-
enzyme isoform T90 from homogenate with xylose as a substrate, in 50 mM Tris-HCl, pH 7.5, containing 1 mM CoCl2, at 90°C
additional information
-
measurement of ethanol production
additional information
-
measurement of the degradation of xylose and glucose
additional information
-
measurement of the degradation of xylose, glucose and a xylose-glucose-mixture
additional information
-
measurement of the production of organic acids
additional information
-
measurement of xylose consumption and ethanol production
additional information
-
modification of established spectrophotometrical activity assay
additional information
-
no activity in: CBS 4732s leu2-2(control strain), DELTAxyl1, DELTAxyl1 DELTAxyl2-A, DELTAxyl1 DELTAxyl2-A DELTAxyl2-B
additional information
-
strains are cultivated under aerobic and anaerobic conditions
additional information
-
measurement of the consumption of xylose, mannose and glucose
additional information
-
measurement of the degradation of xylose and glucose
additional information
-
measurement of the production of ethanol, glycerol and xylitol
additional information
-
measurement of the production of ethanol, glycerol, organic acids, xylitol, CO2
additional information
-
strains are cultivated under aerobic and anaerobic conditions
additional information
-
-
additional information
-
measurement of the degradation of xylose and glucose
additional information
-
measurement of the production of ethanol, glycerol, organic acids, xylitol, CO2
additional information
-
strain is cultivated under aerobic and anaerobic conditions
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structure of a number of binary and ternary complexes involving wild-type and mutant enzymes, the divalent cations Mg2+, Co2+, or Mn2+ and either the substrate xylose or substrate analogs
-
crystal structure of complexes of D-xylose isomerase with deoxysugars
-
structures of the enzyme containing the inhibitors xylitol and D-sorbitol at 2.5 A and 2.3 A resolution respectively
-
wild-type and mutant enzymes
-
sitting drop vapor diffusion method, using 100 mM sodium chloride, 100 mM bicine pH 9.0, 20% (v/v) PEG MME 550
sitting drop vapor diffusion method, using 0.2 M CaCl2, 20% (w/v) polyethylene glycol 3350
sitting drop vapour diffusion method at room temperature, space group 21212 with a: 87.976 A, b: 98.836 and c: 93.927 A
-
3.0 A crystal structure
-
D-threonohydroxamic acid soaked into the crystal, crystallographic structure at 1.6 A resolution
-
X-ray crystallographic structure of the metal-activated enzyme with the substrates D-glucose, 3-O-methyl-D-glucose and in the absence of substrate at 1.96 A, 2.19 A, and 1.81 A
-
analysis of the location of hydrogen atoms by time-of-flight neutron Laue technique. The neutron structure of crystalline XI with bound product, D-xylulose, shows, that O5 of D-xylulose is not protonated but is hydrogen-bonded to doubly protonated His54. Also, Lys289, which is neutral in native XI, is protonated, while the catalytic water in native XI has become activated to a hydroxyl anion which is in the proximity of C1 and C2, the molecular site of isomerization of xylose
cooling crystallization from 0.17 M MgSO4 solution
-
in complex with D-glyceraldehyde, hanging drop vapor diffusion method, using 0.2-0.3 M Mg-formate at pH 7.0 and 22°C
neutron diffraction, largest crystals at 18°C, 95 mg/ml xylose isomerase, 16.9% ammonium sulfate, mathematical analysis to determine optimal conditions for crystallization
-
neutron quasi-Laue diffraction, resolution: 2.2 A - clear visibility of deuterium atoms, clarification of critical residues at the active site and their protonation states
-
structure of E186Q mutant with cyclic glucose bound at the active site, to 2.2 A resolution. Residue His54 is doubly protonated and is poised to protonate the glucose O5 position, while Lys289, which is neutral, promotes deprotonation of the glucose O1H hydroxyl group via an activated water molecule. An extended hydrogen-bonding network connects the conserved residues Lys289 and Lys183 through three structurally conserved water molecules and residue 186
study on the dynamics of solute transport in orthorhombic D-xylose isomerase crystals by means of Brownian dynamics and molecular dynamics simulations and investigation of the diffusion of S-phenylglycine molecules inside XI crystals. The S-phenylglycine molecules mostly interact with residues His54, Asp287, and Lys183. In general, the diffusivities of solute species are found to be 1 to 2 orders of magnitude lower than those of the corresponding free molecules in water
the mechanism of ring-opening for L-arabinose is the same as for the reaction with D-xylose. In the reactive Michaelis complex L-arabinose is distorted to the high-energy 5S1 conformation. Amino acid substitutions in a hydrophobic pocket near C5 of L-arabinose can enhance sugar binding. L-ribulose and L-ribose are found in furanose forms when bound to the enzyme
time-of-flight neutron diffraction at 1.8 A resolution, metal-free enzyme - emphasis on the active site of xylose isomerase, especially of protonation states of His, Lys and H2O
ammonium sulfate as precipitant, orthorhombic space group P212121 with a: 84.35 A, b: 123.6 A, c: 140.24 A
-
ortjorhombic space group P212121 with a: 84.35 A, b: 123.60 A and c: 140.24 A
-
at room temperature with polyethylene glycol 4000 as precipitant, orthorhombic space group P212121 with a: 73.34 A, b: 144.05 A and c 155.07 A
-
ortjorhombic space group P212121 with a: 73.34 A, b: 144.05 A and c: 155.07 A
-
-
-
-
-
-
-
-
-
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E186D
-
mutant enzymes E186D and E186Q are active, and their metal specificity is different from that of the wild type. The E186 enzyme is most active with Mn2+ and has a drastically shifted pH optimum
E186Q
-
mutant enzymes E186D and E186Q are active, and their metal specificity is different from that of the wild type. The E186 enzyme is most active with Mn2+ and has a drastically shifted pH optimum
E253K
-
substitution of Arg for Lys at position 253 at the dimer-dimer interface increases the half-life of the enzyme by 30%. The largest stability gain is achieved in a triple mutant G70S/A73S/G74T
F26W
-
catalytic efficiency with L-arabinose is increased 2fold
H101F
-
substitution of His101 by Phe abolishes the enzyme activity, whereas substitution of other His residues has no effect
H41L
-
substitution of Lys for His41 results in a mutant with near wild-type properties. This mutation completely abolishes adsorption to iminodiacetic acid-Cu(II)
Q256D
-
catalytic efficiency with L-arabinose is increased 3fold, reaction rate with L-ribose is increased 6fold
V135N
no effect on the reaction with D-xylose and L-arabinose, reaction efficiency with L-ribose is increased 2-4fold, reaction with D-glucose is impaired
D189L
-
the Glu140Lys and Asp189Lys mutant proteins are synthesized in the Escherichia coli host, but are incapable of folding correctly. Mutant Trp136Glu does not show any enzyme activity
E140L
-
the Glu140Lys and Asp189Lys mutant proteins are synthesized in the Escherichia coli host, but are incapable of folding correctly. Mutant Trp136Glu does not show any enzyme activity
Y253C
-
a Tyr253 mutant in which a disulfide bridge is introduced at the A-B subunit interface shows reduced thermostability, that is identical in both oxidized and reduced forms and also reduced stability in urea. X-ray-crystallographic analysis of the Mn2+-xylitol form of oxidized Y253C shows a changed conformation of Glu185 and also alternative conformations for Asp254, which is a ligand to the site 2 metal ion. With fructose, Mg2+-Y253C has a similar Km to that of the wild-type, and its maximal velocity is also similar below pH 6.4, but declines thereafter. In presence of Co2+, Y253C has lower activity than wild-type at all pH values, but its activity also declines at alkaline pH
DELTAxyl1
-
deficient in xylose reductase
DELTAxyl1 DELTAxyl2-A
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A
DELTAxyl1 DELTAxyl2-A (EcxylA) No. 1
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A, transformed with xylose isomerase xylA from Escherichia coli, strain 1
DELTAxyl1 DELTAxyl2-A (EcxylA) No. 2
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A, transformed with xylose isomerase xylA from Escherichia coli, strain 2
DELTAxyl1 DELTAxyl2-A (EcxylA) No. 4L/3
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A, transformed with xylose isomerase xylA from Escherichia coli, strain 4L/3
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA HpXYL3)
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B, transformed with xylose isomerase xylA from Escherichia coli and overexpressing endogenous xylulukinase xyl3
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA) No. 1
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B, transformed with xylose isomerase xylA from Escherichia coli, strain 1
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B (EcxylA) No. 2
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B, transformed with xylose isomerase xylA from Escherichia coli, strain 2
H101X
-
selective substitution of His101 or His271 shows that they are essential components of the active site
H271X
-
selective substitution of His101 or His271 shows that they are essential components of the active site
Hansenula polymorpha
-
yeast, strain CBS4732s leu2-2, deficient in beta-isopropyl malate dehydrogenase, deletions of genes encoding xylose reductase (xyl1) and xylitol dehydrogenases (xyl2-A and xyl2-B) - overexpression of xylA gene (Escherichia coli) and endogenous xyl3 gene
DELTAxyl1
-
deficient in xylose reductase
-
DELTAxyl1 DELTAxyl2-A
-
deficient in xylose reductase and xylitol dehydrogenase xyl2-A
-
DELTAxyl1 DELTAxyl2-A DELTAxyl2-B
-
deficient in xylose reductase and xylitol dehydrogenases xyl2-A and xyl2-B
-
Hansenula polymorpha
-
yeast, strain CBS4732s leu2-2, deficient in beta-isopropyl malate dehydrogenase, deletions of genes encoding xylose reductase (xyl1) and xylitol dehydrogenases (xyl2-A and xyl2-B) - overexpression of xylA gene (Escherichia coli) and endogenous xyl3 gene
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E407K
-
2% of strain IO-1 wild-type activity
K407E
-
92% of wild-type activity
R202M
-
9% of strain IO-1 wild-type activity
R202M/V275A
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26% of strain IO-1 wild-type activity
R202M/Y218D
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9% of strain IO-1 wild-type activity
R202M/Y218D/V275A
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62% of strain IO-1 wild-type activity and soluble
S247A
-
97% of wild-type activity
S247A/K407E
-
79% of wild-type activity
S247A/S388T
-
27% of wild-type activity
S388T
-
insoluble and 8% of wild-type activity
S388T/K407E
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soluble and 50% of wild-type activity
T388S
-
11% of strain IO-1 wild-type activity
Y218D
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14% of strain IO-1 wild-type activity
Y218D/V275A
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24% of strain IO-1 wild-type activity
Y275A
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24% of strain IO-1 wild-type activity
E407K
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2% of strain IO-1 wild-type activity
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R202M
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9% of strain IO-1 wild-type activity
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T388S
-
11% of strain IO-1 wild-type activity
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Y218D
-
14% of strain IO-1 wild-type activity
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Y275A
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24% of strain IO-1 wild-type activity
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E407K
-
2% of strain IO-1 wild-type activity
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R202M
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9% of strain IO-1 wild-type activity
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T388S
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11% of strain IO-1 wild-type activity
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Y218D
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14% of strain IO-1 wild-type activity
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Y275A
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24% of strain IO-1 wild-type activity
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E129D/V433I
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the mutation shows an increase in enzymatic activity
E129D/V433I/E15D/E114G
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the mutation shows an increase in enzymatic activity
E129D/V433I/E15D/E114G/T142S/A177T
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the mutant exhibits a 77% increase in enzymatic activity. A yeast strain expressing this mutant enzyme improves its aerobic growth rate by 61fold and both ethanol production and xylose consumption rates by nearly 8fold
Z180L
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one of the metal-binding sites, M-1, is removed by substitution of Glu-180 by Lys. Glu-180 is essential for isomerization but not for ring opening
D163N/E167Q
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40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
D56N
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turnover number increased by 30-40% over that ofwild-type at pH 7.3, lower pH optimum than wild-type, nearly same thermostability as wild-type
D65A
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40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
D81A
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40-60% of wild-type activity, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
E186Q
crystallization data
E221A
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turnover number increased by 30-40% over that from wild-type at pH 7.3, lower pH optimum than wild-type, nearly same tehrmostability as wild-type
H220S
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decreased affinity for Mg2+ and decraesed activity in contrast to wild-type
N185K
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decreased affinity for Mg2+ and decraesed activity in contrast to wild-type
W139A
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replacement of W139 with F, M, or A results in increased catalytic efficience proportional to the decrease in hydrophobicity of the side chain of the substituted amino acid
W139F/V186S
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double mutants, W139F/V186T and W139F/V186S have 5fold and 2fold higher catalytic efficiency, respectively, than does the wild-type
W139F/V186T
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double mutants, W139F/V186T and W139F/V186S have 5fold and 2fold higher catalytic efficiency, respectively, than does the wild-type
W139M
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replacement of W139 with F, M, or A results in increased catalytic efficience proportional to the decrease in hydrophobicity of the side chain of the substituted amino acid
D309K
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no activity, Tm of 95.5°C in the presence of 5 mM Mg2+ and 0.5 mM Co2+
E232K
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no activity, Tm of 100.7°C in the presence of 5 mM Mg2+ and 0.5 mM Co2+
E232K/D309K
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no activity, Tm of 96.5°C in the presence of 5 mM Mg2+ and 0.5 mM Co2+
V185T
mutation increases catalytic efficiency on glucose
D254R/D256R
complete loss of activity
D256R
the mutant shows an increase in the specificity on D-lyxose, L-arabinose and D-mannose
E372G
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broader pH range and nine times higher turnover for D-xylose at 60°C than wild-type
E372G/F163L
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broader pH range and nine times higher turnover for D-xylose at 60°C than wild-type
E372G/V379A
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broader pH range and nine times higher turnover for D-xylose at 60°C than wild-type
N91D/D375G
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
N91D/D375G/V385A
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
N91D/K355A
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
N91D/V144A
site-directed mutagenesis, the mutant shows increased activity but reduced thermostability compared to the wild-type enzyme
D254R/D256R
-
complete loss of activity
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D256R
-
the mutant shows an increase in the specificity on D-lyxose, L-arabinose and D-mannose
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N91D
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the mutant shows increased substrate specificity for D-xylose compared to the wild type enzyme
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H101F
-
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H101F
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substitution of His101 by Phe completely abolishes enzyme activity. When His101 is changed to Glu, Gln, Asn, or Asp, approximately 10-16% of wild-type enzyme activity is retained by the mutant enzymes. The His101Gln mutant enzyme is resistant to diethyldicarbonate inhibition which completely inactivates the wild-type enzyme
W139F
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replacement of W139 with F, M, or A results in increased catalytic efficience proportional to the decrease in hydrophobicity of the side chain of the substituted amino acid
W139F
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the W139F substitution reduces the Km and increases the turnover number of the mutant towards glucose, while the reverse effect towards xylose is observed
N91D
site-directed mutagenesis
N91D
-
the mutant shows increased substrate specificity for D-xylose compared to the wild type enzyme
additional information
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metabolic engineering of Corynebacterium glutamicum to broaden substrate utilization range
additional information
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co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
additional information
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co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
-
additional information
overexpression of the polyhydroxybutyrate producing enzyme in an enzyme-deficient knockout strain of Burkholderia sacchari restoring the ability of the cells to produce polyhydroxybutyrate, overview. Expression in a wild-type strain does not lead to increased polyhydroxybutyrate repoduction and cell growth, overview
additional information
-
overexpression of the polyhydroxybutyrate producing enzyme in an enzyme-deficient knockout strain of Burkholderia sacchari restoring the ability of the cells to produce polyhydroxybutyrate, overview. Expression in a wild-type strain does not lead to increased polyhydroxybutyrate repoduction and cell growth, overview
additional information
-
overexpression of the polyhydroxybutyrate producing enzyme in an enzyme-deficient knockout strain of Burkholderia sacchari restoring the ability of the cells to produce polyhydroxybutyrate, overview. Expression in a wild-type strain does not lead to increased polyhydroxybutyrate repoduction and cell growth, overview
-
additional information
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Saccharomyces cerevisiae: five enzymes of non-oxidative pentose-phosphate-pathway are induced, a unspecific aldose reductase is deleted
additional information
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the overexpressing Saccharomyces cerevisiae strain RWB 218 shows sensitivity to inhibitor acetic acid, kinetics and stoichiometry, detailed overview. At pH 3.5 acetic acid had a strong and specific negative impact on xylose consumption rates, which, after glucose depletion, slowed down dramatically, leaving 50% of the xylose unused after 48 h of fermentation
additional information
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establishing and optimization of ethanol production from hotcompressed water treatment of Japanese beech by bioconversion of D-xylose via xylose isomerase, production enhancement by process integration of saccharifi cation, isomerization, and fermentation, process schemes, overview
additional information
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Saccharomyces cerevisiae: five enzymes of non-oxidative pentose-phosphate-pathway are induced, a non-specific aldose reductase is deleted
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109
in the presence of Mg2+ plus Co2+, the enzyme shows a biphasic inactivation time course and two melting transitions at 99°C and 109°C
25
-
stable for more than 1 month
40
-
10 min, stable up to
40 - 90
thermostability of recombinant mutant enzymes, overview
45
-
purified recombinant enzyme, rapid inactivation
50 - 70
the enzyme is stable up to 50°C for 20 min. However, only 34% of the maximal activity is observed after preincubation at 60°C for 20 min, and no activity is observed after preincubation at 70°C for 20 min
50 - 80
-
30 min, in presence of Co2+, stable
53
-
half life in presence of Co2+: 7 days, half-life in presence of Mg2+: 9 days, in presence of Mn2+ the enzyme activity remains constant for at least 10 days
70 - 80
-
pH 7.8, 2 h, after following 2 h incubation at 80°C 37.6% loss of activity, 70-75% loss of activity at 80°C
97 - 112
-
chitin-binding domain-D-xylose isomerase fusion protein (CBD-TNXI) bound to chitin has a half-life approximately 3times longer than the soluble wild type xylose isomerase (19.9 h vs. 6.8 h, respectively). The unbound soluble CBD-TNXI has a significantly longer half-life (56.5 h) than the immobilized enzyme. TNXI-apo enzyme melts at 97.5°C, while transitions at 100°C and 112°C are observed in the presence of Co2+ (0.5 mM) and Mn2+ (5.0 mM). The apo version of the immobilized enzyme melts at 104°C, with transitions at 87°C and 110°C for the halo enzyme
99
in the presence of Mg2+ plus Co2+, the enzyme shows a biphasic inactivation time course and two melting transitions at 99°C and 109°C
50
-
pH 7.5, 30 min, stable up to
60
-
pH 7.5, 30 min, about 35% loss of activity
60
-
10 min, 20% loss of activity
60
-
30 days, stable in presence of 1 mM Co2+ or 10 mM Mg2+
65
-
mutant Q256D remains fully active for 60 min at 65°C, whereas the activity is rapidly lost at 80°C
65
-
purified recombinant enzyme, 1 h, complete inactivation
65
-
30 min, about 50% loss of activity
65
-
pH 6.5, stable for more than 5 h
70
-
about 65% loss of activity
70
-
in the presence of CO2+, cell-free xylose isomerase retains 100% activity without loss of activity for 7 days
70
-
30 min, about 70% loss of activity
70
-
10 min, stable up to
70
-
in presence of Mn2+, 50% loss of activity after 5 days
70
-
half-life in absence of divalent cations: 4 d. In presence of Mn2+ or Co2+ stable for at least 1 month
75
-
wild-type enzyme remains fully active for 60 min at 75°C
75
-
60 min, stable up to
80
-
mutant F26W remains fully active for 60 min at 80°C
80
-
at least 10 min stable
80
-
the melting temperature at xylose isomerase isoform T80 is at about 80°C
80
-
2 h leads to 30.1% loss of activity
80
-
2 h leads to 30.5% loss of activity
80
-
10 min, 80% loss of activity in absence of metal ions, 50% loss of activity in presence of 1 mM Mg2+, no loss of activity in presence of 1 mM Co2+
85
-
in the presence of CO2+, cell-free xylose isomerase retains 50% residual activity for 13.5 h
85
the enzyme has a half-life of 1 h at 85°C
85
-
with Mg2+, half-life: 20 h
90
-
the melting temperature of the native enzyme isoform T90 is at 90°C
90
Opuntia vulgaris
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the melting temperature of the native enzyme isoform T90 is at 90°C
90
-
after 1 h incubation the recombinant and the wild-type enzymes retain 25 and 34% of their activity, respectively
90
-
in the presence of CO2+, cell-free xylose isomerase retains 50% residual activity for 126 min
additional information
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Tm: 50.3°C (apoenzyme), 53.3°C (in the presence of 5 microM Mg2+), 73.4°C (in the presence of 5 microM Co2+), 73.6°C (in the presence of 5 microM Mn2+)
additional information
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Tm: 50.8°C (apoenzyme), 56.2°C (in the presence of 5 microM Mg2+), 56.2°C (in the presence of 5 microM Co2+), 57.3°C (in the presence of 5 microM Mn2+)
additional information
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Co2+ is superior as protector against thermal inactivation at 80°C
additional information
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Mn2+ and Co2+ increase thermal stability
additional information
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Tm: 64.1°C (apoenzyme), 83.0°C (in the presence of 5 microM Mg2+), 86.0°C (in the presence of 5 microM Co2+), 86.1°C (in the presence of 5 microM Mn2+)
additional information
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Tm: 96.4°C (apoenzyme), 97.6°C (in the presence of 5 microM Mg2+), 97.5°C (in the presence of 5 microM Co2+), 96.9°C (in the presence of 5 microM Mn2+), 100.4°C (in the presence of 5 mM Mg2+), 100.0°C (in the presence of 5 mM Co2+), 100.5°C (in the presence of 5 mM Mn2+), 100.9°C (in the presence of 5 mM Ni2+), 100.5°C (in the presence of 5 mM Ca2+), half-lives: 83.2 min in the presence of 2 mM Mn2+ at 99°C, 6.9 min in the presence of 2 mM Mn2+ at 102°C, 4.2 min in the presence of 2 mM Mn2+ at 104°C, 2.3 min in the presence of 2 mM Mn2+ at 106°C, 59.5 min in the presence of 2 mM Co2+ at 96°C, 14 min in the presence of 2 mM Co2+ at 99°C, 5.8 min in the presence of 2 mM Co2+ at 102°C, 2.9 min in the presence of 2 mM Co2+ at 104°C, 12 min in the presence of 2 mM Mg2+ at 92°C, 2.3 min in the presence of 2 mM Mg2+ at 96°C, 1.9 min in the presence of 2 mM Mg2+ at 99°C, 1.3 min in the presence of 2 mM Mg2+ at 102°C, 30 min in the absence of metal ions at 87°C, 11.3 min in the absence of metal ions at 90°C, 7.5 min in the presence of 5 mM Mg2+ and 0.5 mM Co2+ at 100°C, 3.0 min in the presence of 0.5 mM Co2+ at 100°C
additional information
-
stability is also strongly influenced by the addition of divalent cations. The addition of Mn2+ gives the highest thermostability, Mg2+ has a smaller stabilizing effect, while other metals have no effect
additional information
-
Mn2+, Co2+ and Ni2+ strongly protect the enzyme from heat denaturation
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cloning and functional expression of enzymes from Escherichia coli in Pseudomonas putida
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co-overexpression of genes encoding xylose isomerase (EcxylA, Escherichia coli) and xylulokinase (XYL3, Hansenula polymorpha), expression of both genes is driven by Hansenula polymorpha GAP-DH promoter
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Corynebacterium glutamicum is transformed with: xylose isomerase (xylA, Escherichia coli) and xylulokinase (xylB, Escherichia coli)-two recombinant strains of Corynebacterium glutamicum are obtained: CRX1 (xylA) and CRX2 (xylA/xylB)
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expressed in Escherichia coli BL21 (DE3) cells
expressed in Escherichia coli BL21 Star (DE3) cells and in Lactobacillus plantarum
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expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli DH10B cells
expressed in Escherichia coli Rosetta2 (DE3)pLysS cells
expressed in Saccharomyces cerevisiae
expressed in Saccharomyces cerevisiae strain BY4741-S1
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expression in Escherichia coli
expression in Escherichia coli (DH5-alpha) and Saccharomyces cerevisiae
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expression in Escherichia coli BL21(DE3)
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expression in Escherichia coli HB101
expression in Escherichia coli JM105
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expression in Escherichia coli or Bacillus subtilis
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expression in Escherichia coli, sequence homology with enzymes from other sources
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expression in Hansenula polymorpha
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expression in Pseudomonas putida S12
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expression in Saccharomyces cerevisiae
expression in the yeast Hansenula polymorpha
expression of mutant enzymes in Escherichia coli strain BL21 (DE3)
gene XYL1, subcloning in Escherichia coli strain MC1061, functional expression in Corynebacterium glutamicum, ATCC13032. Biotransformation of xylose into xylitol appears to be influenced by xylose transport, which is in turn affected by the glucose concentration in the reaction medium
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gene xylA, expression in Saccharomyces cerevisiae
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gene xylA, expression of the polyhydroxybutyrate producing enzyme in an enzyme-deficient knockout strain of Burkholderia sacchari restoring the ability of the cells to produce polyhydroxybutyrate and increasing cell growth, overview
overexpression in Escherichia coli strain BL21(DE3) from vector pRAC
-
phylogenetic analysis and enzyme sequence comparisons, functional expression of codon-optimized enzyme in Saccharomyces cerevisiae confers on the yeast cells the ability to metabolize D-xylose and to use it as the sole carbon and energy source. The recombinant enzyme shows reduced sensitivity to inhibition by xylitol
phylogenetic analysis, enzyme expression in Escherichia coli strain BL21(DE3)
-
Saccharomyces cerevisiae is transformed with a gene encoding xylose isomerase (Thermus thermophilus)
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Saccharomyces cerevisiae is transformed with a gene encoding xylose isomerase originating from Piromyces sp.
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the production of the cloned gene in Escherichia coli and Bacillus brevis are compared expression in Escherichia coli and Bacillus brevis. Bacillus brevis is able to produce the isomerase efficiently (more than 1 g/l)
-
transformants bearing the fused lac-xylA or tac-xylA gene, cloned into various high copy-number plasmids
-
wild-type and mutant enzymes, expression in Escherichia coli
-
wild-type and mutant enzymes, overexpression in Escherichia coli
-
xylose isomerase gene (Piromyces sp.) is overexpressed in Saccharomyces cerevisiae strain TMB3044 resulting in strain TMB 3066
-
Zymobacter palmae is transformed with: xylose isomerase (xylA, Escherichia coli), xylulokinase (xylB, Escherichia coli), transaldolase (tal, Escherichia coli), transketolase (tktA, Escherichia coli). Different promotors from Zymomonas mobilis ATCC 29191 are used: gap-dh (Pgap), enolase (Peno)
-
-
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
-
expressed in Escherichia coli BL21(DE3) cells
expressed in Escherichia coli BL21(DE3) cells
expressed in Saccharomyces cerevisiae
-
expressed in Saccharomyces cerevisiae
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
-
expression in Escherichia coli
expression in Escherichia coli HB101
-
expression in Escherichia coli HB101
-
expression in Escherichia coli HB101
-
expression in Escherichia coli HB101
expression in Saccharomyces cerevisiae
-
expression in Saccharomyces cerevisiae
expression in the yeast Hansenula polymorpha
-
expression in the yeast Hansenula polymorpha
-
phylogenetic analysis and enzyme sequence comparisons, functional expression of codon-optimized enzyme in Saccharomyces cerevisiae confers on the yeast cells the ability to metabolize D-xylose and to use it as the sole carbon and energy source. The recombinant enzyme shows reduced sensitivity to inhibition by xylitol
-
phylogenetic analysis and enzyme sequence comparisons, functional expression of codon-optimized enzyme in Saccharomyces cerevisiae confers on the yeast cells the ability to metabolize D-xylose and to use it as the sole carbon and energy source. The recombinant enzyme shows reduced sensitivity to inhibition by xylitol
-
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biotechnology
-
putative use of lignocellulosic biomass as feedstock for the chemical industry
degradation
enzyme additionally displays xylose fermenting activity. A Saccharomyces cerevisae strain coexpressing xylose isomerase and endo-1,4-beta-xylanase Xyn11B from Saccharophagus degradans, and beta-xylosidase XlnD from Aspergillus niger is able to produce 6.0 g/l ethanol from xylan
degradation
-
enzyme additionally displays xylose fermenting activity. A Saccharomyces cerevisae strain coexpressing xylose isomerase and endo-1,4-beta-xylanase Xyn11B from Saccharophagus degradans, and beta-xylosidase XlnD from Aspergillus niger is able to produce 6.0 g/l ethanol from xylan
-
energy production
-
bioethanol
energy production
-
engineering of Saccharomyces cerevisiae for alcoholic fermentation of D-xylose
energy production
-
engineering Saccharomyces cerevisiae for alcoholic fermentation of D-xylose
energy production
-
genetic engineering of Saccharomyces cerevisiae in order to increase ethanol production by fermentation of D-xylose
energy production
-
genetic engineering of the yeast Hansenula polymorpha in order to increase ethanol production by D-xylose fermentation
energy production
-
genetic engineering of Zymobacter palmae in order to produce ethanol from xylose fermentation
energy production
-
genetic engineering of the yeast Hansenula polymorpha in order to increase ethanol production by D-xylose fermentation
-
food industry
-
thermophilic xylose isomerase from Opuntia vulgaris can serve as a good alternate source of enzyme for use in the production of high fructose corn syrup
food industry
Opuntia vulgaris
-
thermophilic xylose isomerase from Opuntia vulgaris can serve as a good alternate source of enzyme for use in the production of high fructose corn syrup
food industry
-
xylose isomerase is widely used for production of glucose fructose syrup, a natural sweetener in dietary and preventive nutrition
food industry
-
xylose isomerase isozyme T80 serves as potential alternate catalytic converter of glucose in the production of high-fructose corn syrup for the sweetener industry and for ethanol production
food industry
industrial production of high fructose corn syrup
food industry
-
xylose isomerase is widely used for production of glucose fructose syrup, a natural sweetener in dietary and preventive nutrition
-
nutrition
-
high fructose corn syrups
nutrition
-
industrial manufacture of high-fructose corn syrups
nutrition
-
industrial manufacture of high-fructose corn syrups
-
synthesis
-
used in industry for the production of high-fructose corn syrups
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
synthesis
-
commercial importance in the production of high-fructose corn syrup, potential application in the production of ethanol from hemicelluloses
synthesis
-
production of high fructose corn syrup
synthesis
-
production of fructose, which is used as an alternate sugar to sucrose or invert sugar in the food and beverage industries, it is also used in the baking and dairy industry
synthesis
-
production of fructose, which is used as an alternate sugar to sucrose or invert sugar in the food and beverage industries, it is also used in the baking and dairy industry
synthesis
-
production of fructose, which is used as an alternate sugar to sucrose or invert sugar in the food and beverage industries, it is also used in the baking and dairy industry
synthesis
-
production of fructose, which is used as an alternate sugar to sucrose or invert sugar in the food and beverage industries, it is also used in the baking and dairy industry
synthesis
-
higher rates of xylose utilization by further improved strains make alcoholic fermentation of hemicellulose fractions of plant biomass a realistic enterprise
synthesis
alcohol fermentation of xylose and mixed sugars by Saccharomyces cerevisiae constitutively overexpressing of the Orpinomyces sp. xylose isomerase, the Saccharomyces cerevisiae xylulokinase, and the Pichia stipitis SUT1 sugar transporter genes. A strain adapted for enhanced growth on xylose by serial transfer in xylose-containing minimal medium under aerobic conditions can ferment 20 g per l of xylose to ethanol with a yield of 0.37 g per g and production rate of 0.026 g per l and h. Raising the fermentation temperature from 30°C to 35°C results in a substantial increase in the ethanol yield and production as well as a significant reduction in the xylitol yield. Ethanol production from xylose and a mixture of glucose and xylose is achieved in complex medium containing yeast extract, peptone, and borate with a considerably high yield of 0.48 g per g
synthesis
-
co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
synthesis
-
expression of Escherichia coli xylose isomerase and xylulokinase in Pseudomonas putida S12 for efficient utilization of D-xylose and L-arabinose. After laboratory evolution of strains by repeated transfer to fresh minimal medium with xylose, a strain that efficiently utilizes xylose at a considerably improved growth rate can be obtained. The high yield can be attributed in part to glucose dehydrogenase inactivity, whereas the improved growth rate may be connected to alterations in the primary metabolism. The evolved D-xylose-utilizing strain metabolizes L-arabinose as efficiently as D-xylose, while its ability to utilize glucose is not affected
synthesis
the combination of TxyA, XloA, and XylA is useful tool for the D-xylulose production from beta-1,3-xylan
synthesis
-
co-overexpression of xylose isomerase and endogenous xylulokinase in a Hansenula polymorpha strain lacking NAD(P)H-dependent xylose reductase and NAD-dependent xylitol dehydrogenases activities. Recombinant strain displays improved ethanol production during the fermentation of xylose
-
synthesis
-
the combination of TxyA, XloA, and XylA is useful tool for the D-xylulose production from beta-1,3-xylan
-