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Ag+
-
222.51% activity at 12.5 mM
CaCl2
activates 1.44fold at 10 mM
KCl
-
upon an increase in the KCl concentration from 0 to 100 mM, the OtsA activity decreases by more than 40%, whereas it is not significantly affected when UDP or GDP-glucose is used as the substrate
KHCO3
-
100-300 mM, activation
MgCl2
activates 2fold at 10 mM
NaHCO3
-
100-300 mM, activation
Ca2+
-
activation
Ca2+
-
activates at physiological concentrations
Co2+
-
activation
Co2+
-
1922.04% activity at 12.5 mM
Co2+
the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.91fold activation by 10 mM Co2+
Co2+
1.91fold activation at 10 mM
Cu2+
-
activates 33% at 5 mM
Cu2+
-
124.68% activity at 12.5 mM
Fe2+
-
activation
Fe2+
-
161.13% activity at 12.5 mM
K+
-
activates at 20 mM
K+
-
maximal activation at 400 mM KCl
K+
-
287.73% activity at 12.5 mM
K+
-
activates maximal at 50 mM by 176%, 160% at 400 mM
Mg2+
95% stimulation
Mg2+
-
activates at 20 mM
Mg2+
5 mM used in assay conditions
Mg2+
5 mM used in assay conditions
Mg2+
-
2.5fold activation at 5 mM, best at 70 mM
Mg2+
-
optimal concentration: 3-6 mM MgCl2
Mg2+
-
20 mM, enhances 2fold
Mg2+
-
12.5 mM used in assay conditions
Mg2+
-
most appropriate cation to activate enzyme activity as it increases the activity by 7851fold at 12.5 mM
Mg2+
-
10 mM, required for maximal activity
Mg2+
-
optimal concentration is 1-2 mM
Mg2+
-
2fold stimulation at 5 mM
Mg2+
-
25 mM, 2fold increase of activity
Mg2+
-
activates at low concentration up to 5 mM
Mg2+
the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.33fold activation ba 10 mM Mg2+
Mg2+
2.33fold activation at 10 mM
Mn2+
20% stimulation
Mn2+
-
best divalent cation, 2.6fold activation at 5 mM, best at 70 mM
Mn2+
-
10 mM, 2fold increase of activity
Mn2+
-
475.71% activity at 12.5 mM
Mn2+
the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 1.16fold activation by 10 mM Mn2+
Mn2+
1.16fold activation at 10 mM
NaCl
activates at 10 mM
NaCl
-
an increase in the concentration of NaCl from 0 to 100 mM leads to a decrease in the OtsA activity by more than 35% when ADP-glucose or TDP-glucose is the substrate. When UDP-glucose or GDP-glucose is used as substrate, the OtsA activity is increased by 10–30%
Ni2+
-
activation
Ni2+
-
402.82% activity at 12.5 mM
Zn2+
-
2.2fold activation at 5 mM
Zn2+
-
163.05% activity at 12.5 mM
Zn2+
the enzyme does not require divalent metal ions for catalysis, but Mg2+, Zn2+, Co2+ and Mn2+ can stimulate enzyme activity and maximal activation is found in the presence of Mg2+. 2.26fold activation by 10 mM Zn2+
Zn2+
2.26fold activation at 10 mM
additional information
-
no or poor effects by CoCl2, CaCl2, BaCl2, and FeSO4
additional information
heparin in assays has no effect on the activity of recombinant OtsA1-His10
additional information
heparin in assays has no effect on the activity of recombinant OtsA1-His10
additional information
-
no effect by Na+
additional information
the addition of monovalent metal ions Na+, K+ and Li+ has no effect on the enzyme activity
additional information
-
the addition of monovalent metal ions Na+, K+ and Li+ has no effect on the enzyme activity
additional information
no effect by Li+ at 10 mM
additional information
-
no effect by Li+ at 10 mM
additional information
no requirement for divalent cations for activity