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BaCl2
-
stimulates activity, relative activity: 198%
Fe3+
-
147% relative activity at 1 mM
KCl
-
stimulates activity, relative activity: 109%
Na2HPO4
-
optimal at 1% w/v
NaN3
-
1 mM, 20% activation
sulfate
-
sulfate binding site structure
Ba2+
-
1 mM, 55% activation
Ba2+
-
1mM, 143% of initial activity
Ba2+
2 mM, 130% of initial activity
Ba2+
1 mM, 4.2fold increase in activity
Ba2+
1 mM, 116% of initial activity
Ba2+
1 mM, 113% of initial activity
Ca2+
at 1 mM, strain 4A1M
Ca2+
-
the activity of isoform AlyA3 is stimulated by Ca2+, an increase by 5fold is observed upon increasing the concentration of Ca2+ from 0.02 mM to 6.3 mM
Ca2+
required for activity
Ca2+
-
optimal activity in presence of Ca2+
Ca2+
1 mM, 174% of initial activity, 10 mM, 135% of initial activity
Ca2+
-
7.5 mM CaCl2 stimulates
Ca2+
-
136% relative activity at 1 mM
Ca2+
-
1mM, 136% of initial activity
Ca2+
-
50 mM, isoform A 117%, isoform B 131% of initial activity
Ca2+
1 mM, 2.5fold increase in activity
Ca2+
1 mM, 116% of initial activity
Ca2+
required for activity, activates at 1 mM
Ca2+
-
cations are required
Ca2+
1 mM, 125% of initial activity
Ca2+
1 mM, 135% of initial activity
Ca2+
1 mM, 1.2fold increase in enzymatic activity
Ca2+
1 mM, 1.5fold increase in enzymatic activity
Ca2+
at least 2 mM Ca2+ in the reaction mixture is essential for the activity
CaCl2
-
stimulates activity, relative activity: 176%
CaCl2
-
optimal at 5-10 mM
CaCl2
-
20% activation at 1 mM
Co2+
-
-
Co2+
-
activates 5% at 2 mM
Co2+
-
1 mM, 80% activation
Co2+
-
1mM, 123% of initial activity
Co2+
2 mM, 148% of initial activity
Co2+
1 mM, 156% of initial activity
Cs+
Alginovibrio aquatilis
-
-
Cs+
-
1 mM, 40% activation
Cs+
0.2 M, 2500% of initial activity
Cu2+
-
activates 4% at 2 mM
Cu2+
2 mM, 133% of initial activity
Cu2+
1 mM, 18% of initial activity
Fe2+
-
stimulates
Fe2+
1 mM, 148% of initial activity
K+
Alginovibrio aquatilis
-
-
K+
highly activating, activation is synergistic with Mg2+
K+
-
optimum activity at 0.25 M. At 2 M, about 70% residual activity
K+
-
maximal activation at 0.05 M
K+
-
cations are required for activity
K+
-
maximal activation at 0.05 M
K+
-
1 mM, 15% activation
K+
-
the addition of K+ at a concentration of 50 mM results in a 10% increase in activity level
K+
-
117% relative activity at 50 mM
K+
-
1mM, 117% of initial activity
K+
-
50 mM, isoform A 132%, isoform B 110% of initial activity
K+
1 mM, 4.2fold increase in activity
K+
1 mM, 121% of initial activity
K+
activates at over 50 mM
K+
0.2 M, 2500% of initial activity
K+
1 mM, 136% of initial activity
Li+
Alginovibrio aquatilis
-
-
Li+
-
1 mM, 12% activation
Li+
0.2 M, 1880% of initial activity
Mg2+
-
slightly activating
Mg2+
slightly activating, activation is synergistic with K+
Mg2+
-
maximal activation at 0.06-0.08 M
Mg2+
-
cations are required for activity
Mg2+
-
maximal activation at 0.06-0.08 M
Mg2+
1 mM, 168% of initial activity, 10 mM, 119% of initial activity
Mg2+
-
1 mM, 40% activation
Mg2+
-
the addition of 50 mM Mg2+ leads to a 2fold increase in activity level
Mg2+
extracellular isozyme
Mg2+
-
1mM, 126% of initial activity
Mg2+
2 mM, 146% of initial activity
Mg2+
-
50 mM, isoform A 116%, isoform B 121%, isoform C 114% of initial activity
Mg2+
1 mM, 3.1fold increase in activity
Mg2+
1 mM, 126% of initial activity
MgCl2
-
stimulates activity, relative activity: 156%
MgCl2
-
15% activation at 1 mM
Mn2+
-
slightly activating
Mn2+
-
maximal activation at 0.06-0.08 M
Mn2+
-
cations are required for activity
Mn2+
-
maximal activation at 0.06-0.08 M
Mn2+
-
150% relative activity at 1 mM
Mn2+
-
1mM, 116% of initial activity
Mn2+
2 mM, 125% of initial activity
Mn2+
1 mM, 3.2fold increase in activity
MnCl2
-
stimulates activity, relative activity: 121%
MnCl2
-
12% activation at 1 mM
Na+
Alginovibrio aquatilis
-
-
Na+
-
optimum activity at 0.25 M. At 2 M, about 70% residual activity
Na+
-
maximal activation at 0.05 M
Na+
-
cations are required for activity
Na+
-
maximal activation at 0.05 M
Na+
100 mM, 126% of initial activity, 500 mM, 203% of initial activity
Na+
-
0.2 M NaCl stimulates
Na+
-
1 mM, 115% of initial activity
Na+
0.8-1.4 M NaCl required for maximum activity
Na+
-
the addition of Na+ at a concentration of 50 mM results in a 10% increase in activity level
Na+
extracellular isozyme
Na+
-
280% relative activity at 100 mM
Na+
-
1mM, 143% of initial activity
Na+
activity in 0.5-1.2 M NaCl is sixfold higher than that in absence of NaCl. The Km value in 0.5 M NaCl decreases more than 20fold compared to that in absence of NaCl
Na+
-
is essential for the activity of all the three lyases
Na+
1 mM, 120% of initial activity
Na+
activates at over 50 mM
Na+
0.2 M, 2200% of initial activity
Na+
50 mM, 124% of initial activity
Na+
optimum concentration 0.3 M, about 2fold increase in activity compared to absence of NaCl
Na+
up to 10fold increase in activity, optimum concentration 1 M
Na+
up to 3fold increase in activity, optimum concentration 400 mM
NaCl
-
AkAly28 shows practically no activity in the absence of NaCl and the maximal activity at NaCl concentrations higher than 0.2 M, whereas AkAly33 shows about 20% of maximal activity despite the absence of NaCl and the maximal activity at around 0.1 M NaCl
NaCl
-
2 mM, 110% of initial activity, 100 mM, 193% of initial activity
NaCl
-
activates 10% at 2 mM,96% at 150 mM
NaCl
activity is optimal at 0.35 M
NaCl
-
0.05-0.075 M required for activity
NaCl
-
0.1-0.2 M required for activity
NaCl
-
required for activity
NaCl
-
stimulates activity, relative activity: 113%
NaCl
-
aly-SJ02 shows the highest activity in 0.2 M NaCl, and retains more than 75% activity in 1 M NaCl, exhibiting salt-tolerance ability
NaCl
-
0.05-0.075 M required for activity
NaCl
-
0.05-0.075 M required for activity
NH4+
-
1 mM, 12% activation
NH4+
0.2 M, 2270% of initial activity
Ni2+
-
activates
Ni2+
-
1mM, 110% of initial activity
Rb+
Alginovibrio aquatilis
-
-
Rb+
0.2 M, 2500% of initial activity
Sr2+
-
activates
Sr2+
-
1mM, 124% of initial activity
Zn2+
111% relative activity at 1 mM
Zn2+
-
activates 5% at 2 mM
Zn2+
1 mM ZnCl2, 92% loss of activity
Zn2+
1 mM, 114% of initial activity
Zn2+
relevance of this zinc ion in catalytic activity, metal-binding protein ligands are His533, Gln551, and Lys573. The metal ion establishes the orientation of His415 and Arg438, which would otherwise be mobile, to set these residues for interactions with substrate
Zn2+
1 mM, enhances activity by 66%
additional information
Alginovibrio aquatilis
-
no requirement for divalent cations
additional information
-
no metal ion requirement
additional information
-
no or poor effects by Mn2+ and Zn2+
additional information
not affected by Ca2+, Co2+, Mn2+, and Zn2+
additional information
-
not affected by Ca2+, Co2+, Mn2+, and Zn2+
additional information
no requirement for divalent cations
additional information
no requirement for divalent cations
additional information
-
the activities of isoforms AlyA1 and AlyA2 are not affected by addition of similar concentrations of Ca2+
additional information
no or poor effects by CaCl2 and NaCl at 1 mM
additional information
-
no or poor effects by CaCl2 and NaCl at 1 mM
additional information
-
Zn2+ has no effect on aly-SJ02 activity
additional information
-
no effect by Li+ at 50 mM
additional information
-
no effect on activity by K+
additional information
-
requires significant levels of salt for maximal activity. Optimal activity at approximately 0.05 M with divalent cation and between 0.3 and 0.4 M with monovalent cation
additional information
-
Sn2+, Ca2+, Mn2+, and Mg2+ do not influence enzyme activity of isoform A9mT
additional information
Sn2+, Ca2+, Mn2+, and Mg2+ do not influence enzyme activity of isoform A9mT
additional information
Sn2+, Ca2+, Mn2+, and Mg2+ do not influence enzyme activity of isoform A9mT
additional information
Sn2+, Ca2+, Mn2+, and Mg2+ do not influence enzyme activity of isoform A9mT
additional information
-
no effect on enzyme activity by SDS, K+, Li+, and NH4+