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(CH3CO2)2Pb
-
13.9% residual activity at 1 mM
2-mercaptoethanol
-
90.2% residual activity at 5 mM
2-propanol
-
5% (v/v), about 40% loss of activity, 50% (v/v), about 95% loss of activity
4,7-phenanthroline
-
34% inhibition at 1 mM
4-hydroxymercuribenzoic acid
5,5'-dithiobis(2-nitrobenzoic acid)
8-hydroxyquinoline
-
36% inhibition at 1 mM
acetone
-
30% (v/v), 70% loss of activity
acetonitrile
-
5% (v/v), about 50% loss of activity, 50% (v/v), about 95% loss of activity
Al2(SO4)3
-
complete inhibition at 5 mM
ammonium sulfate
-
75% residual activity at 800 mM
ascorbic acid
-
68% residual activity at 1 mM
BaCl2
-
5 mM, 35% inhibition
benzaldehyde
-
nearly complete inhibition at 10 mM
benzyl bromide
-
strong inhibition at 10 mM
benzylamine
-
65% inhibition at 10 mM
butanol
-
5% (v/v), about 75% loss of activity
Dichloromethane
5% (v/v), 70% inhibition
dimethyl sulfoxide
-
1% (v/v)
DL-cysteine
-
97% residual activity at 1% (w/v)
DMSO
-
5% (v/v), % inhibition
ether
-
5% (v/v), 23% inhibition
ethyl acetate
-
5% (v/v), 35% inhibition
FeCl3
-
5 mM, 23% inhibition
FeSO4
-
5 mM, 47% inhibition
glutathione
-
5 mM, complete inhibition
glycerin
-
5% (v/v), 52% inhibition
GSH
-
slight inhibition at 1 mM
Hg+
-
complete inhibition at 1 mM
jasmonic acid
-
application of jasmonic acid represses protein expression
KCl
-
5 mM, 58% inhibition
MgCl2
-
5 mM, 18% inhibition
n-heptane
-
5% (v/v), 25% inhibition
nicotinic acid
-
inhibition at concentrations greater than 0.2 M
o-phenanthroline
-
complete inhibition at 5 mM
phenylacetonitrile
-
50% inhibition at 10 mM
phenylmethanesulfonyl fluoride
inhibits amide conversion more than 94% and completely suppresses nitrile hydrolysis
phenylmethylsulfonyl fluoride
-
40% inhibition at 1 mM
SDS
-
5% (v/v), 37% inhibition
Triton X-100
-
5% (v/v), 14% inhibition
ZnCl2
-
5 mM, 32% inhibition
3-Cyanopyridine
-
inhibition at concentrations greater than 0.2 M
3-Cyanopyridine
-
inhibitory by substrate inhibition above 400 mM
4-chloromercuribenzoate
-
complete inhibition at 1 mM
4-chloromercuribenzoate
-
91-100% inhibition at 0.1 mM
4-chloromercuribenzoate
-
nearly complete inhibition at 1 mM
4-hydroxymercuribenzoic acid
-
strong inhibition at 1 mM
4-hydroxymercuribenzoic acid
-
50% inhibition at 0.05 mM
4-hydroxymercuribenzoic acid
-
complete inhibition at 0.1 mM, reversal by GSH
4-hydroxymercuribenzoic acid
-
complete inhibition at 0.0005 mM
5,5'-dithiobis(2-nitrobenzoic acid)
-
45% inhibition at 1 mM
5,5'-dithiobis(2-nitrobenzoic acid)
-
complete loss of activity due to modification of Cys165
5,5'-dithiobis(2-nitrobenzoic acid)
-
complete inhibition at 1 mM
5,5'-dithiobis(2-nitrobenzoic acid)
-
complete inhibition at 1 mM
Ag+
-
strong inhibition at 1 mM
Ag+
-
complete inhibition at 0.1 mM
Ag+
-
complete inhibition at 0.1 mM
Ag+
-
complete inhibition at 1 mM
Ag+
1 mM, complete inhibition
Ag+
-
complete inhibition at 0.01 mM
Ag+
-
1.5% residual activity at 1 mM
Ag+
-
1.7% residual activity at 1 mM
Ag+
-
10 mM, complete loss of activity
Ag+
-
complete inhibition between 0.1 and 1 mM
Ag+
-
complete inhibition at 0.01 mM
Ag+
-
complete inhibition at 1 mM
Ag+
-
complete loss of activity
Ag+
-
complete inhibition at 5 mM
Ag+
-
strong inhibition of nitrilase activity. The effect on KCN (0.02 mmol/l) degradation is tested in the presence of Cu2+ and Ag+ ions (0.025 mmol/l to 1.0 mmol/l) and the enzymatic activity is not affected significantly at 0.025 mmol/l, 0.075 mmol/l, and 0.125 mmol/l concentrations. When both ions are combined, the activity of the enzyme decreases significantly
Al3+
-
0.3% residual activity at 5 mM
Al3+
-
0.5% residual activity at 5 mM
Al3+
-
strong inhibition of nitrilase activity
Ba2+
-
about 76% residual activity at 1 mM
Ba2+
1 mM, 45% inhibition
Benzamide
-
66% residual activity at 25 mM
Benzamide
-
competitive inhibition of benzonitrile hydrolysis, Ki: 16.6 mM
Ca2+
-
Ca2+
-
96% residual activity at 5 mM
Ca2+
-
about 77% residual activity at 1 mM
Ca2+
-
1 mM, 48% loss of activity
CaCl2
-
inhibition at 50 mM
CaCl2
-
5 mM, 34% inhibition
Co2+
-
Co2+
-
62% residual activity at 5 mM
Co2+
-
1 mM decreases the enzyme activity to about 90%
Co2+
1 mM, 35% inhibition
Co2+
-
46.3% residual activity at 5 mM
Co2+
-
75.8% residual activity at 1 mM
Co2+
-
97% inhibition at 0.1 mM
Co2+
-
1 mM, 84% loss of activity
Co2+
-
44.9% residual activity at 1 mM
Co2+
-
complete inhibition at 1 mM
Cr3+
-
7% residual activity at 5 mM
Cr3+
-
27.8% residual activity at 1 mM
Cu2+
-
Cu2+
-
benzonitrilase A: 30% inhibition at 0.1 mM, benzonitrilase B: 83% inhibition at 0.1 mM
Cu2+
-
1% residual activity at 0.1 mM
Cu2+
-
about 75% residual activity at 1 mM
Cu2+
1 mM, 30% inhibition
Cu2+
-
13.4% residual activity at 1 mM
Cu2+
-
88.3% residual activity at 1 mM
Cu2+
-
10 mM, 94% loss of activity
Cu2+
-
complete inhibition at 1 mM
Cu2+
-
complete inhibition at 0.01 mM
Cu2+
-
1 mM, 61% loss of activity
Cu2+
-
19.7% residual activity at 1 mM
Cu2+
-
strong inhibition of nitrilase activity. The effect on KCN (0.02 mmol/l) degradation is tested in the presence of Cu2+ and Ag+ ions (0.025 mmol/l to 1.0 mmol/l) and the enzymatic activity is not affected significantly at 0.025 mmol/l, 0.075 mmol/l, and 0.125 mmol/l concentrations. When both ions are combined, the activity of the enzyme decreases significantly
dithiothreitol
-
slight inhibition at 1 mM
dithiothreitol
-
58% residual activity at 1 mM
dithiothreitol
-
55% residual activity at 1 mM
dithiothreitol
-
79% residual activity at 1 mM
dithiothreitol
-
5 mM, 37% inhibition
dithiothreitol
-
5 mM, complete inhibition
DTT
-
1 mM, 15% loss of activity
EDTA
-
EDTA
-
93% residual activity at 15 mM
EDTA
-
87% residual activity at 1 mM
EDTA
-
84.1% residual activity at 5 mM
EDTA
-
10 mM, 20% loss of activity
EDTA
-
1 mM, 7% loss of activity
EDTA
-
93.2% residual activity at 1 mM
ethanol
-
a relative activity of 49% is detected in 5% (v/v) of ethanol
ethanol
5% (v/v), 45% inhibition
ethanol
-
30% (v/v), about 25% loss of activity
Fe2+
-
slight inhibition at 1 mM
Fe2+
-
60% residual activity at 5 mM
Fe2+
-
about 79% residual activity at 1 mM
Fe2+
-
10 mM, 59% loss of activity
Fe2+
-
37% inhibition at 0.001 mM
Fe2+
-
75.4% residual activity at 1 mM
Fe3+
-
Fe3+
-
71% residual activity at 5 mM
Fe3+
-
5% residual activity at 5 mM
Fe3+
-
43.7% residual activity at 5 mM
Fe3+
-
1 mM, 48% loss of activity
Fe3+
-
53.3% residual activity at 1 mM
H2O2
-
4% residual activity at 5 mM
H2O2
-
1 mM, 73% loss of activity
H2O2
-
strong inhibition of nitrilase activity
hexane
5% (v/v), 80% inhibition
hexane
-
50% (v/v), 60% loss of activity
Hg2+
-
strong inhibition at 1 mM
Hg2+
-
complete inhibition at 0.1 mM
Hg2+
-
complete inhibition at 0.1 mM
Hg2+
-
complete inhibition at 0.01 mM
Hg2+
-
complete loss of activity at 1 mM
Hg2+
-
0.1% residual activity at 1 mM
Hg2+
-
10 mM, complete loss of activity
Hg2+
-
complete inhibition between 0.1 and 1 mM
Hg2+
-
complete inhibition at 0.01 mM
Hg2+
-
5 mM, 98% loss of activity
Hg2+
-
complete inhibition at 0.25 mM, also inhibition of enzyme association to decamers
Hg2+
-
43% inhibition at 1 mM
Hg2+
-
nearly complete inactivation at 1 mM
iodoacetamide
-
slight inhibition at 1 mM
iodoacetamide
-
67% residual activity at 1 mM
iodoacetamide
-
slight inhibition at 0.05 mM
iodoacetamide
-
5% residual activity at 4.6 mM
iodoacetamide
-
complete inhibition at 0.5 mM
iodoacetamide
-
56.6% residual activity at 1 mM
iodoacetamide
-
5 mM, 82% loss of activity
iodoacetic acid
-
slight inhibition at 1 mM
iodoacetic acid
-
slight inhibition at 1 mM
Li+
-
Li+
-
about 70% residual activity at 1 mM
methanol
-
the enzyme is relatively active in 5% (v/v) methanol with 60% of the enzyme activity remaining
methanol
5% (v/v), 30% inhibition
methanol
-
5% (v/v), 29% inhibition
methanol
-
30% (v/v), about 25% loss of activity
Mg2+
-
Mg2+
-
91% residual activity at 5 mM
Mg2+
-
46% residual activity at 5 mM
Mg2+
-
85.3% residual activity at 5 mM
Mg2+
-
10 mM, 15% loss of activity
Mn2+
-
79.3% residual activity at 1 mM
Mn2+
-
10 mM, 24% loss of activity
Mn2+
-
complete inhibition at 0.1 mM
Mn2+
-
1 mM, 59% loss of activity
Mn2+
-
67.4% residual activity at 1 mM
N-ethylmaleimide
-
slight inhibition at 0.05 mM
N-ethylmaleimide
-
30% inhibition at 1 mM
N-ethylmaleimide
-
complete inhibition at 0.005 mM
N-ethylmaleimide
-
57.3% residual activity at 1 mM
NaCl
-
5 mM, 26% inhibition
NaCl
the enzyme loses more than 75% of its activity at NaCl concentrations higher than 2.0 mol/l
NaN3
-
88% residual activity at 5 mM
NaN3
-
38% residual activity at 5 mM
Ni2+
-
Ni2+
-
44% residual activity at 5 mM
Ni2+
-
1 mM decreases the enzyme activity to about 90%
Ni2+
1 mM, 40% inhibition
Ni2+
-
7% residual activity at 5 mM
Ni2+
-
62% residual activity at 1 mM
Ni2+
-
10 mM, 83% loss of activity
Ni2+
-
21.6% residual activity at 1 mM
p-hydroxymercuribenzoate
-
complete inhibition at 1 mM
p-hydroxymercuribenzoate
-
12% residual activity at 1 mM
Pb2+
-
Pb2+
-
52% residual activity at 0.1 mM
Pb2+
-
about 78% residual activity at 1 mM
Pb2+
-
6% residual activity at 1 mM
Pb2+
-
10 mM, 15% loss of activity
phenylhydrazine
-
slight inhibition at 1 mM
phenylhydrazine
-
43% residual activity at 1 mM
Phenylmercuriacetate
-
complete inhibition at 1 mM
Phenylmercuriacetate
-
complete inhibition at 0.005 mM
Propanol
-
a relative activity of 6% is detected in 5% (v/v) of propanol
Propanol
5% (v/v), 80% inhibition
Toluene
5% (v/v), 95% inhibition
Toluene
-
5% (v/v), about 65% loss of activity, 50% (v/v), about 85% loss of activity
Zn2+
-
Zn2+
-
complete inhibition at 5 mM
Zn2+
-
1 mM decreases the enzyme activity to about 90%
Zn2+
-
6% residual activity at 5 mM
Zn2+
-
8.2% residual activity at 1 mM
Zn2+
-
10 mM, 20% loss of activity
Zn2+
-
complete inhibition at 1 mM
Zn2+
-
complete inhibition at 0.01 mM
Zn2+
-
1 mM, 20% loss of activity; 1 mM, 24% loss of activity
Zn2+
-
57% residual activity at 1 mM
Zn2+
-
complete inhibition at 1 mM
Zn2+
-
strong inhibition of nitrilase activity
additional information
-
not inhibited by L-glutathione, L-cysteine, dithiothreitol, and 8-hydroxyquinoline
-
additional information
-
-
-
additional information
the enzyme retains near maximal activity even in the presence of high concentrations of ZnCl2, MgSO4 and MnSO4
-
additional information
-
gibberellic acid, kinetin, abscisic acid, or epi-brassinolide have no obvious influence on activity
-
3.5.5.1 nitrilase
results (
results (
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