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118
recombinant enzyme in presence of 100 mM phosphate, melting temperature
137
-
melting temperature
139
-
melting temperature in presence of 100 mM phosphate
37
4h, 90% loss of activity
4
4h, 40% loss of activity
73
5 min, 50% residual activity, mutant enzyme C259S/C261S/C262S/C200S/C205S and mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S/C164S
78
5 min, 50% residual activity, mutant enzyme C259S/C261S/C262S/C200S/C205S/C138S
91
5 min, 50% residual activity, mutant enzyme C259S/C261S/C262S
100
Caldariella acidophila
-
1 h, stable
100
-
5 h, 98% remaining activity
100
-
stable for at least 2 h
100
stable for at least 2 h
100
recombinant enzyme, 1 h, 85% remaining activity
100
-
recombinant enzyme, 1 h, 95% remainig activity in presence of 100 mM phosphate
100
1 h, 15% loss of activity of recombinant enzyme, wild-type enzyme remains stable
102
-
apparent Tm, mutant enzyme C259S/C261S
102
5 min, 50% residual activity, mutant enzyme C259S/C261S
106
-
apparent Tm, mutant enzyme C262S
106
5 min, 50% residual activity, mutant enzyme C262S
110
recombinant enzyme, 2 h, stable
110
-
recombinant enzyme, 10 min, 50% remaining activity in absence and 90% remaining activity in presence of 100 mM phosphate
111
recombinant enzyme, melting temperature
111
melting temperature of recombinant enzyme
112
-
apparent Tm, wild-type enzyme
112
5 min, 50% residual activity, wild-type enzyme
120
-
120
-
recombinant enzyme, 10 min, no activity in absence and 50% remaining activity in presence of 100 mM phosphate
130
-
half-life: 43 min
130
half-inactivation time: 15 min
132
-
10 min, melting temperature
132
10 min, melting temperature
140
-
half-life: 13 min
140
half-inactivation time: 5 min
70
-
15 min, complete loss of activity
70
recombinant enzyme, 0.8 M DTT, stable
90
recombinant enzyme, 0.8 M DTT, 2 h, loss of 38% activity
90
-
1 h, wild-type enzyme is completely stable, mutant enzyme C262S loses 32% of its activity, mutant enzyme c259S/C261A loses 63% of its activity
additional information
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resistance to thermal inactivation is increased remarkably by addition of 5'-methylthioadenosine or phosphate
additional information
PfMTAP is a highly thermostable protein
additional information
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PfMTAP is a highly thermostable protein
additional information
-
high degree of thermal stability
additional information
-
disulfide linkages play a key role in thermal stability
additional information
disulfide linkages play a key role in thermal stability
additional information
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the recombinant enzyme, expressed in Escherichia coli, is less thermostable and thermophilic than the native enzyme due to incorrect positioning of disulfide bonds
additional information
the recombinant enzyme, expressed in Escherichia coli, is less thermostable and thermophilic than the native enzyme due to incorrect positioning of disulfide bonds
additional information
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the recombinant 5'-methylthioadenosine phosphorylase is less thermophilic and thermostable than the Sulfolobus solfataricus enzyme, since an incorrect positioning of disulfide bonds within the molecule generates structures less stable to thermal unfolding
additional information
the recombinant 5'-methylthioadenosine phosphorylase is less thermophilic and thermostable than the Sulfolobus solfataricus enzyme, since an incorrect positioning of disulfide bonds within the molecule generates structures less stable to thermal unfolding
additional information
the hexameric hyperthermophilic protein contains in each subunit two pairs of disulfide bridges, a CXC motif, and one free cysteine. All cysteine pairs and especially the CXC motif significantly contribute to the enzyme thermal stability
additional information
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the hexameric hyperthermophilic protein contains in each subunit two pairs of disulfide bridges, a CXC motif, and one free cysteine. All cysteine pairs and especially the CXC motif significantly contribute to the enzyme thermal stability