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Cr3+
-
140% relative activity at 10 mM
Cs+
-
1 mM, 1.13fold activation of wild-type enzyme
CuCl
-
1 mM, 34% inhibition
HgCl2
-
1 mM, 13% inhibition
KCN
Thermomonospora vulgaris
-
10 mM, 82% inhibition
MoO42-
-
10-100 mM, stimulates
Na2SO4
-
1 M, 4fold increase in activity
PMSF
activates 12% at 1 mM
PO43-
-
100 mM, stimulates
Rb+
1 mM, increases activity by 10%
Urea
-
132% relative activity at 8 mM urea for salivary gland alpha-amylase
ZnCl2
-
5 mM, pH 4.0, 55°C, 104% relative activity
Ag+
-
1 mM, pH 8.0, 24 h at 4°C, slight activation for Amy I and Amy II
Ag+
-
0.5 mM, enhances activity
Al3+
-
1 mM, pH 8.0, 24 h at 4°C, 110% and 73% residual activity for Amy I and Amy II, respectively
Al3+
-
120% relative activity at 10 mM
Ba2+
-
the activity is increased by approximately 15% by 1 mM Ba2+
Ba2+
measured activity about 8090%
Ba2+
-
35% increase of activity at 2 mM
Ba2+
-
1 mM, pH 8.0, 24 h at 4°C, 104% and 95% residual activity for Amy I and Amy II, respectively
Ba2+
-
163% relative activity at 5 mM, at 80°C and pH 5.0
Ba2+
-
1 mM, 2.24fold activation
Ba2+
activates 7.4% at 1 mM
Ba2+
-
5 mM, slight activation
Ba2+
activates 38% at 5 mM
Ca2+
-
-
Ca2+
calcium-dependent alpha-amylase, maximum activity at 2.5 mM CaCl2
Ca2+
Ca2+ ions have effects on the structure and thermal propeties of alpha-amylase (AGXA) from thermophilic Anoxybacillus sp. strain GXS-BL. With calcium ions, the values of Topt, T50, t1/2, Tm and DELTAH in enzyme AGXA are significantly higher than those of enzyme AGXA without calcium ions, showing calcium ions have stabilizing effects on alpha-amylase structure with the increased temperature. Four Ca2+ ions (Ca1-4)are bound to the model structure. Ca1 is in the region between domain A and domain B, coordinated by the N139, D182, H217, and E173 residues and three water molecules. Ca2 and Ca3 are both located in domain A, with Ca2 coordinated by the N44, N46, N49, D50, G63, and D65 residues and a water molecule, and Ca3 coordinated by the N92, E109, and E110 residues and three water molecules. Ca4 is in the region between domain A and domain C, coordinated by the E400 residue and five water molecules
Ca2+
activates slightly at 1-5 mM
Ca2+
-
increases the thermostability of the enzyme, two Ca2+ ions per enzyme molecule
Ca2+
-
stabilizes the partially purified enzyme against thermal inactivation
Ca2+
-
16% activation at 1 mM, although Ca2+ is a good stabilizer it cannot activate the enzyme significantly, Ca2+ shows 41% inhibition of the enzyme at 10 mM
Ca2+
-
1 Ca2+ bound per enzyme molecule
Ca2+
-
increases the thermostability of the enzyme, four Ca2+ ions per enzyme molecule
Ca2+
-
enhances the enzyme activity with 5 mM Ca2+, 120% relative activity, and with 10 mM 96% relative activity, pH 5.0, 50°C
Ca2+
the Ca2+-binding residue Asp233 affects significantly the alpha-amylase specific activity
Ca2+
-
increases the thermostability of the enzyme, five Ca2+ ions per enzyme molecule
Ca2+
presence of an extra Ca2+-binding region between the A and C domains responsible for higher thermostability of this enzyme
Ca2+
-
catalytic and/or structure-stabilizing Ca2+ ions are tightly bound to the enzyme
Ca2+
activates 9% at 1 mM, 59% at 10 mM
Ca2+
-
40 mM calcium acetate, enhances activity of membrane-bound enzyme to 268% of control
Ca2+
-
increases the thermostability of the enzyme, three Ca2+ ions per enzyme molecule
Ca2+
-
1 mM, 1.35fold activation of wild-type enzyme, 1.24fold activation of mutant enzyme L134R/S320A
Ca2+
activity not significantly enhanced in presence of 1 mM CaCl2
Ca2+
-
Bacillus subtilis alpha-amylase requires roughly 4times more calcium for full activity than other alpha-amylases of nonbacterial nature
Ca2+
2 ions per enzyme molecule
Ca2+
-
2-mercaptoethanol interfers with activation by Ca2+, glutathione enhances it
Ca2+
-
128% activity at 10 mM
Ca2+
-
the activity of the alpha-amylase AI is increased 1.5fold in the presence of 4 mM Ca2+
Ca2+
-
1 mM, pH 8.0, 24 h at 4°C, 105% and 106% residual activity for Amy I and Amy II, respectively
Ca2+
slightly activating at 5-10 mM
Ca2+
-
2 mM, about 1.2fold activation
Ca2+
-
180% relative activity at 5 mM, at 80°C and pH 5.0
Ca2+
-
200% relative activity at 10 mM
Ca2+
-
Ca2+ at 10 mM has only a slightly stimulating effect, the enzyme is Ca2+-independent
Ca2+
-
contains one gatom of Ca2+ per mol of enzyme
Ca2+
-
slightly improves enzymatic activity
Ca2+
-
stabilizes the enzyme
Ca2+
-
calcium stabilizes the conformation of alpha-amylase and also involved in substrate binding, but inhibits enzyme activity
Ca2+
-
197% relative activity at 20 mM Ca2+ for salivary gland alpha-amylase
Ca2+
-
slight activator at concentrations below 150 mM, activating only a maximum of 3% at 100 mM, and a slight inhibitor at higher concentrations (8% of the initial activity at 200 mM)
Ca2+
-
10 mM, 1.4fold activation
Ca2+
-
10 mM, increase of activity to 140%
Ca2+
-
strictly dependent, retaining below 20% activity in the absence of CaCl2. The optimal concentration is ca. 0.2 mM
Ca2+
-
AMY1 shows the highest activity at 5 mM calcium concentration and maintains its activity at a broad range from 0.1 to 10 mM of calcium ion. AMY2 shows the highest acitivity at 15-20 mM of calcium, compared with the lowest 20% of activity at 0.1 mM of calcium concentration, 37°C, substrate insoluble blue starch. There is no significant difference in hydrolyzing activity on the soluble starch substrate between AMY1 and AMY2, with the increase of calcium concentration. The increase in calcium up to 50 mM causes the decrease by 0-30% in the activity of both AMYs
Ca2+
-
10 mM, 1.35fold activation
Ca2+
-
no effect on enzyme activity by Ca2+, but structural stabilization of the protein molecule by calcium ions
Ca2+
highly activating at 5 mM
Ca2+
-
optimal activation at 15 mM
Ca2+
-
activates, activity profile
Ca2+
-
95% loss of activity after removal of Ca2+ by EDTA, addition of Ca2+ results in the recovery of 12% of the original activity, alpha-amylase III
Ca2+
in the crystal structure, one bound calcium ion is found, coordinated to the side chains of Asn100 and Asp167, the main-chains of Arg158 and His201, and three water molecules
Ca2+
activates 28.2% at 1 mM
Ca2+
in the presence of calcium, the affinity of the enzymes (wild type and mutants) toward starch is increased, the thermostability of the wild type and A53S mutant is calcium dependent at different temperatures, in the presence of 2 mM CaCl2 at 60°C, the percentage of residual activity in both the wild type and A53S mutant changes after 30 min of incubation
Ca2+
-
5 mM, required for activation
Ca2+
-
5 mM, about 70% activation
Ca2+
-
1 mM, 37°C, 30 min, pH 6.5, 148% relative activity
Ca2+
-
increases the thermostability of the enzyme, one Ca2+ ion per enzyme molecule
Ca2+
-
the enzyme is Ca2+-protein. Removal of Ca2+ by dialysis against water causes irreversible inactivation of the enzyme
Ca2+
activates 55% at 5 mM
Ca2+
1 mM, increases activity by 20%
Ca2+
-
activates 52% at 5 mM
Ca2+
2 mM, 127% of initial activity
CaCl2
-
the reusability of the immobilized enzymes are similar in starch hydrolysis reaction medium containing either 5 mM or 0.25 mM CaCl2
CaCl2
-
5 mM, slight activation
CaCl2
2 mM, pH 6.5, 50°C, 115% relative activity
CaCl2
-
76% activation of isozyme alpha-amylase I at 1 mM
CaCl2
-
maximal activity at 0.1 mM, higher concentrations inhibit activity
CaCl2
-
5 mM, pH 4.0, 55°C, 111% relative activity
CaCl2
-
incubated in different concentrations 0.5-100 mM at 25°C overnight, with 10 mM EDTA, significant activation, with two apparent dissociation constants K1: 0.3 mM and K2: 5.4 mM
chloride
presence of chloride ions is essential for activity. 20 mM NaCl is sufficient for maximum activity. NaCl is not inhibitory below 250 mM
chloride
-
is a weak allosteric enzyme activator
Cl-
Gammarus palustris
-
activates isoenzyme IC and IW
Cl-
-
10-100 mM, activates
Cl-
-
activation above 10 mM
Co2+
5 mM, strong stimulation
Co2+
-
58% activation at 1 mM
Co2+
-
activates the recombinant chimeric mutant amylase
Co2+
-
activates and enhances structural enzyme stability
Co2+
-
activation of isozyme BAA at 10 mM
Co2+
-
162% relative activity at 5 mM, at 80°C and pH 5.0
Co2+
-
1 mM, 3.06fold activation
Co2+
activates the recombinant chimeric mutant amylase
Co2+
-
slight activation of isozyme AI-2, slight inhibition of isozymes AI-1 and AII
Co2+
-
5 mM, about 70% activation
Co2+
1 mM CoCl2, slightly enhances activity
Co2+
-
0.5 mM, enhances activity
Cu2+
-
enhances the enzyme activity with 5 mM Cu2+, 120% relative activity, and with 10 mM 87% relative activity, pH 5.0, 50°C
Cu2+
measured activity about 8090%
Cu2+
-
slightly improves enzymatic activity
Cu2+
-
5 mM, slight activation
Cu2+
-
1 mM, 37°C, 30 min, pH 6.5, 100% relative activity
EDTA
-
112% relative activity at 2 mM EDTA for salivary gland alpha-amylase
EDTA
2 mM, pH 6.5, 50°C, 40% relative activity
Fe2+
-
activates
Fe2+
-
the activity is increased by approximately 15% by 1 mM Fe2+
Fe2+
-
1 mM, 2.72fold activation
Fe2+
-
5 mM, slight activation
Fe2+
activates 22% at 5 mM
Fe2+
-
0.5 mM, enhances activity
Fe3+
activates 152% at 1 mM
Fe3+
-
133% relative activity at 5 mM, at 80°C and pH 5.0
Fe3+
-
activates slightly
K+
activates 10% at 1 mM
K+
slightly activating at 5-10 mM
K+
-
105% relative activity at 10 mM
K+
-
131% relative activity at 5 mM, at 80°C and pH 5.0
K+
-
248% relative activity at 20 mM K+ for midgut alpha-amylase and 223% relative activity at 20 mM K+ for salivary gland alpha-amylase
K+
activity of the enzyme in KCl is equal to that in NACl, indicating that the type of monovalent cation is not critical to the activity
K+
-
slight activation of isozymes AI-1 and AII, slight inhibition of isozyme AI-2
K+
-
optimal activation at 10 mM
K+
-
5 mM, slight activation
K+
1 mM, increases activity by 16%
KCl
2 mM, pH 6.5, 50°C, 105% relative activity
KCl
-
maximum amylase activity at 4 M NaCl or 4.5 M KCl, 70°C, and pH 8.5
KCl
-
maximum amylase activity at 4 M NaCl or 4.5 M KCl, and retains about 6090% of the optimal activity at 23.5 M. The enzyme is less active in the presence of 0.51.5 M of each salt, and no activity is observed in absence of the salts. The inactivation at low-salt concentrations is reversible by increasing the salt concentration
Li+
slightly activating at 5-10 mM
Li+
-
slight activation of isozymes AI-1 and AI-2, slight inhibition of isozyme AII
Li+
-
5 mM, slight activation
Mg2+
-
required
Mg2+
-
13% activation at 1 mM
Mg2+
-
activates the recombinant chimeric mutant amylase
Mg2+
-
38% activation at 5 mM
Mg2+
-
118% relative activity at 5 mM, at 80°C and pH 6.5
Mg2+
-
the activity is increased by approximately 15% by 10 mM Mg2+
Mg2+
-
40 mM magnesium acetate, enhances activity of the membrane-bound enzyme to 216% of the control
Mg2+
2 ions per enzyme molecule
Mg2+
-
1 mM, pH 8.0, 24 h at 4°C, 111% and 107% residual activity for Amy I and Amy II, respectively
Mg2+
slightly activating at 5-10 mM
Mg2+
-
slightly improves enzymatic activity
Mg2+
-
1 mM, 1.72fold activation
Mg2+
activates the recombinant chimeric mutant amylase
Mg2+
-
inhibitor when added in concentrations from 50 mM to 200 mM. The maximum inhibitory effect is obtained at 100 mM, inhibiting only 10% of the initial activity
Mg2+
-
slight activation of isozymes AI-1 and AI-2, and AII
Mg2+
-
optimal activation at 10 mM
Mg2+
activates 6.9% at 1 mM
Mg2+
-
5 mM, slight activation
Mg2+
-
1 mM, 37°C, 30 min, pH 6.5, 98% relative activity
Mg2+
1 mM MhCl2, slightly enhances activity
Mg2+
activates 13% at 5 mM
Mg2+
-
activates 34% at 5 mM
MgCl2
-
1 mM, 22% inhibition
MgCl2
-
5 mM, pH 4.0, 55°C, 103% relative activity
Mn2+
-
activates
Mn2+
-
activates at 10 mM
Mn2+
measured activity about 8090%
Mn2+
-
1 mM, pH 8.0, 24 h at 4°C, 108% and 102% residual activity for Amy I and Amy II, respectively
Mn2+
-
140% relative activity at 10 mM
Mn2+
-
191% relative activity at 5 mM, at 80°C and pH 5.0
Mn2+
-
slightly improves enzymatic activity
Mn2+
-
1 mM, 1.34fold activation
Mn2+
-
activation of isozymes AI-1 and AI-2, and AII
Mn2+
-
1 mM, 37°C, 30 min, pH 6.5, 96% relative activity
Mn2+
-
0.5 mM, enhances activity
Na+
activates 15% at 1 mM
Na+
-
activation of isozyme BAA at 10 mM
Na+
activates 15% at 1 mM, 61% at 10 mM
Na+
-
activity is promoted by 0.5-2.0% NaCl
Na+
slightly activating at 5-10 mM
Na+
-
142% relative activity at 5 mM, at 80°C and pH 5.0
Na+
-
120% relative activity at 10 mM Na+ for midgut alpha-amylase and 183% relative activity at 20 mM Na+ for salivary gland alpha-amylase
Na+
-
optimal salinity: 10% NaCl
Na+
-
activation of isozymes AI-1 and AI-2, and AII
Na+
-
optimal activation at 5 mM
Na+
-
5 mM, slight activation
NaCl
-
the enzyme is stable against 1.5 M NaCl
NaCl
enzyme AmyD-1 displays extreme salt tolerance, with the highest activity in the presence of 2.0 M NaCl and 60.5% of activity in 5.0 M NaCl, 40% inhibition at 5 M
NaCl
-
the enzyme is resistant to 4.5% NaCl
NaCl
-
the enzyme is resistant to 11% NaCl
NaCl
Amy-E not only is halotolerant but also its activity is stimulated at high salt concentrations in the range of 1-5 M, activates 20% at 2 M
NaCl
2 mM, pH 6.5, 50°C, 100% relative activity
NaCl
-
AmyH is very halophilic, but is also active in absence of salt, denaturation by urea occurs only in absence of NaCl
NaCl
maximal activity at 2.6 M NaCl. 83% and 95% of the maximum activity are observed at 0.6 and 4.2 M NaCl, respectively
NaCl
-
optimal NaCl concentration in the absence of chloroform is 4.3 M. No activity is detected below 1.7 M NaCl. In the presence of chloroform, optimal NaCl concentration is 4.3 M, and activity is not detected below 0.9 M
NaCl
-
the enzyme is resistant against 4.5% NaCl
NaCl
-
maximal activity at 3 M NaCl
NaCl
-
maximum amylase activity at 4 M NaCl or 4.5 M KC, 70°C, and pH 8.5
NaCl
-
maximum amylase activity at 4 M NaCl or 4.5 M KCl, and retains about 6090% of the optimal activity at 23.5 M. The enzyme is less active in the presence of 0.51.5 M of each salt, and no activity is observed in absence of the salts. The inactivation at low-salt concentrations is reversible by increasing the salt concentration
NaCl
activates, optimal at 2 M for highest enzyme activity, profile overview
NaCl
-
the enzyme is active over a broad range of salt concentrations, with optimum activity at 0.9 M. At 1.7, 2.6, and 4.3 M NaCl AmyB ist 80, 60, and 12% active, respectively. AmyB is a halophilic enzyme, but is still above 45% active in the absence of salt
NaCl
-
18% activation of isozyme alpha-amylase I at 1 mM, 21% at 10 mM
NaCl
-
activation above 10 mM, 28% activation at 250 mM
NaCl
-
the enzyme is stable against 3.5 M NaCl
NaCl
-
the enzyme is stable against 11-17%
NaCl
the enzyme is stable against 10-17%
NaCl
-
the enzyme is stable against 12%
NaCl
-
the enzyme is stable against 0.5-4.0 M, a salt-tolerant alpha-amylase
Ni2+
measured activity about 8090%
Ni2+
-
1 mM, 1.23fold activation
Ni2+
-
1 mM, 37°C, 30 min, pH 6.5, 100% relative activity
Ni2+
activates 19% at 5 mM
Pb2+
-
1 mM, pH 8.0, 24 h at 4°C, 101% and 87% residual activity for Amy I and Amy II, respectively
Pb2+
-
5 mM, slight activation
Pb2+
-
1 mM, 37°C, 30 min, pH 6.5, 91% relative activity
Pb2+
-
activates slightly
Sr2+
-
1 mM, 1.11fold activation of wild-type enzyme, no activation of mutant enzyme L134R/S320A
Sr2+
-
1 mM, 37°C, 30 min, pH 6.5, 92% relative activity
Zn2+
-
22% activation at 5 mM
Zn2+
-
5 mM, slight activation
additional information
-
alpha-amylase requires metal ions for activity and structural stability
additional information
Li+, Na+, K+, Co2+, Cu2+, Mg2+, Zn2+, and Fe3+ have no stimulatory effect on activity
additional information
-
no requirement for Ca2+
additional information
-
poor effects by Mg2+, Na+, Ni2+, Zn2+, Cu2+, Fe2+, and Ba2+
additional information
-
the recombinant chimeric mutant amylase activity is not significantly affected by EGTA, Ca2+, Na+, and K+. The enzymes are Ca2+-independent
additional information
-
the enzyme is poorly affected by Ca2+, Mg2+, Li+, Cu2+, Ba2+, and Mn2+
additional information
-
BH072 alpha-amylase is a Ca2+-independent enzyme
additional information
-
the enzyme shows Ca2+-independency, no effect by Ca2+ at 1-5 mM. Poor effects by 1-5 mM of Na+, K+, and Mg2+
additional information
-
activity is not stimulated by the presence of Ca2+, Fe2+, Ba2+, K+, and Mn2+
additional information
-
no stimulation by Ca2+, no or poor effect on activity by Mn2+, Fe2+, and K+
additional information
-
the enzyme is Ca2+-independent
additional information
-
no activation by Ca2+ or other divalent cations
additional information
no or poor effects by Mg2+, K+, and Zn2+ at 1-10 mM
additional information
-
no or poor effects by Mg2+, K+, and Zn2+ at 1-10 mM
additional information
-
the enzyme shows no requirement for metals
additional information
-
not affected by Mg2+ and Cu2+
additional information
-
Li+ has negligible effect on activity
additional information
-
isozyme Amy3 is a chloride-independent alpha-amylase
additional information
isozyme Amy3 is a chloride-independent alpha-amylase
additional information
no or poor effects by 5-10 mM of Mn2+, Cu2+, Zn2+, and Fe2+
additional information
-
not stimulated by Na+
additional information
-
the enzyme is Ca2+-independent
additional information
-
the activity of the purified enzyme is Ca2+-independent
additional information
-
Ca2+-independent
additional information
-
does not require Ca2+ for its stability or activity
additional information
-
no quantitative change in the activity even at high concentrations of acrylamide, 0.05 to 0.6 mM. The addition of CsCl decreases the fluorescence quenching with no influence on enzyme activity
additional information
the recombinant chimeric mutant amylase activity is not significantly affected by EGTA, Ca2+, Na+, and K+. The enzymes are Ca2+-independent
additional information
-
the recombinant chimeric mutant amylase activity is not significantly affected by EGTA, Ca2+, Na+, and K+. The enzymes are Ca2+-independent
additional information
when the enzyme is assayed in the presence of CaCl2 or EDTA at 5, 10, and 25 mM, neither increase nor decrease of activity is observed suggesting that Ca2+ is not required for the enzyme action, and EDTA is not inhibitory
additional information
-
when the enzyme is assayed in the presence of CaCl2 or EDTA at 5, 10, and 25 mM, neither increase nor decrease of activity is observed suggesting that Ca2+ is not required for the enzyme action, and EDTA is not inhibitory
additional information
-
alpha-amylase I is no affected by NaNO3, BaCl2, and MgCl2
additional information
-
no effect by 1 mM EGTA
additional information
-
no effect on isozymes by Ca2+
additional information
no effect by Mg2+ at 5 mM
additional information
-
not activated by several metal ions tested, including Ca2+ up to 10 mM
additional information
-
the enzyme is not affected by Mn2+ at 1-100 mM
additional information
poor effects by 1 mM of K+ and Na+
additional information
-
does not require Ca2+
additional information
the enzyme does not require Ca2+ for activity
additional information
-
the enzyme does not require Ca2+ for activity
additional information
-
does not require Ca2+
additional information
-
additional provision of Cl- (up to 30 mM NaCl) in the reaction mixture does not affect significantly the activity of alpha-amylases
additional information
calcium ions show neither inhibitory nor potentiating activity on alpha-amylase activity, alpha-amylase extracted from marine Streptomyces strain A3 is mainly calcium independent
additional information
-
no requirement for Ca2+
additional information
Ni2+ and Ca2+ do not stimulate the activity of AmyB
additional information
-
Ni2+ and Ca2+ do not stimulate the activity of AmyB
additional information
-
no effect by 5 mM Ni2+