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AlCl3
-
53% inhibition at 1 mM
Ba(OH)2
-
slightly inhibitory, percentage of inhibition is dependent on substrate
BaCl2
-
28% inhibition at 1 mM
Cd2+
-
2 mM, 25% residual activity
ethylene glycol tetraacetic acid
-
2 mM, 23% residual activity
FeCl2
-
1 mM, 29% remaining activity
FeCl3
-
92% inhibition at 1 mM
glutathione
-
2 mM, 23% residual activity
HgCl2
-
1 mM, 23% remaining activity
Li+
1 mM, 65% of initial activity
Mn3+
-
1 mM, 8% residual activity
NiCl2
-
33% inhibition at 1 mM
NiSO4
-
slightly inhibitory, percentage of inhibition is dependent on substrate
p-chloromercuribenzoate
-
-
Sr2+
-
2 mM, 70% residual activity
trinitrobenzene sulfonic acid
-
-
Triton X-100
slightly activating at 0.001%, slightly inhibitory at 0.01%
Al3+
-
1 mM, 59% residual activity
Al3+
-
1 mM, 47% residual activity
Al3+
1 mM, 83% of initial activity
Ba2+
-
1 mM, 72% residual activity
Ba2+
-
50 mM, isoform A 89%, isoform B 44%, isoform C 42% of initial activity
Ba2+
-
1 mM, 13% residual activity
Ba2+
1 mM, 80% of initial activity
Ca2+
-
2 mM, 95% residual activity
Ca2+
5 mM, 66% inhibition
Ca2+
-
1 mM, 6% residual activity
Ca2+
inhibition at 1-5 mM
Ca2+
-
1 mM, 36% residual activity
Ca2+
1 mM, 18% of initial activity
Co2+
5 mM, almost complete inhibition
Co2+
10 mM, 75% of initial activity
Co2+
-
1 mM, 11% residual activity
Co2+
-
50 mM, isoform A 67%, isoform B 66%, isoform C 29% of initial activity
Co2+
-
1 mM, 12% residual activity
Co2+
1 mM, 71% of initial activity
Co2+
1 mM, about 10% of initial activity
Cu2+
5 mM, almost complete inhibition
Cu2+
1 mM, 65% of initial activity
Cu2+
-
10 mM, complete inhibition
Cu2+
-
1 mM, 10% residual activity
Cu2+
-
1 mM, 8% residual activity
Cu2+
-
1 mM, 3% residual activity
Cu2+
1 mM, 71% of initial activity
Cu2+
1 mM, 81% of initial activity
Cu2+
1 mM, about 10% of initial activity
CuCl2
-
1 mM, 58% remaining activity
CuCl2
-
97% inhibition at 1 mM
EDTA
-
2 mM, 15% residual activity
EDTA
-
complete inhibition at 1 mM concentration, almost completely recovered activity by the addition of 2 mM CaCl2 or partially recovered by the addition of CoCl2 or MnCl2, suggesting that the enzyme conformation is bivalent-cation dependent
EDTA
-
1 mM concentration causes 83% inhibition, the enzyme regains about 90% of the original activity when incubated with 10 mM metal compounds such as MnCl2, MgCl2, NiCl2 or CaCl2, the enzyme is most likely to require the metal ions for the expression of activity
EDTA
-
1 mM, approximately 95% inhibition, enzymatic activity is restored totally by treatment with calcium chloride or partially restored with aluminium chloride or manganese (II) chloride
EDTA
-
1 mM, 50% residual activity
EDTA
1 mM, 37% of initial activity
EDTA
1 mM, 3fold decrease in activity
EDTA
-
1 mM, 48% of initial activity
EDTA
-
1 mM, 8% residual activity
EDTA
1 mM, 75% residual activity
EDTA
-
1 mM, 6% residual activity; 96% inhibition at 1 mM
EDTA
1 mM, 46% of initial activity
EDTA
1 mM, about 30% of initial activity
Fe2+
-
2 mM, 30% residual activity
Fe2+
5 mM, almost complete inhibition
Fe2+
-
50 mM, no residual activity
Fe2+
1 mM, 70% of initial activity
Fe2+
1 mM, about 10% of initial activity
Fe3+
1 mM, 88% of initial activity
Fe3+
-
1 mM, 11% residual activity
Fe3+
-
1 mM, 60% residual activity
Fe3+
-
1 mM, 8% residual activity
Guanidinium chloride
-
concentrations above 3 M cause significant loss of activity
Guanidinium chloride
-
8 M urea causes apparent retention of approximately 50% of enzyme activity
Hg2+
-
2 mM, 10% residual activity
Hg2+
-
10 mM, complete inhibition
Hg2+
1 mM, 34% of initial activity
Mg2+
5 mM, 66% inhibition
Mg2+
-
0.1 M: activation, higher concentrations cause lower activity or precipitation of alginate
Mg2+
inhibition at 1-5 mM
Mg2+
1 mM, 65% of initial activity
Mn2+
5 mM, almost complete inhibition
Mn2+
1 mM, 85% residual activity
Mn2+
1 mM, 75% of initial activity
Mn2+
1 mM, 75% of initial activity
Mn2+
1 mM, 69% of initial activity
N-bromosuccinimide
-
1 mM, no residual activity
Ni2+
-
2 mM, 65% residual activity
Ni2+
1 mM, 87% of initial activity
Ni2+
-
1 mM, 42% residual activity
Ni2+
-
1 mM, 20% residual activity
Ni2+
1 mM, 32% of initial activity
SDS
-
10 mM SDS causes complete loss of activity whereas the ordered beta-structure is created
SDS
1 mM, 23% of initial activity
SDS
1 mM, 29% of initial activity
Urea
-
36% inhibition in the presence of 8 M urea
Urea
-
enzyme preincubated in the presence of 6 M urea, dialyzed and assayed normally retains 90% activity, but if the enzyme is preincubated and assayed in the presence of 6 M urea no activity is measured
Urea
-
8 M urea causes apparent retention of approximately 50% of enzyme activity
Zn2+
5 mM, almost complete inhibition
Zn2+
1 mM, 91% of initial activity
Zn2+
-
1 mM, 32% residual activity
Zn2+
-
50 mM, isoform A 10%, isoform B 14%, isoform C 12% of initial activity
Zn2+
-
1 mM, 42% residual activity
Zn2+
1 mM, 57% of initial activity
Zn2+
1 mM, 66% of initial activity
Zn2+
1 mM, about 30% of initial activity
Zn2+
1 mM, 25% of initial activity
ZnCl2
-
slightly inhibitory, percentage of inhibition is dependent on substrate
ZnCl2
-
58% inhibition at 1 mM
additional information
-
10 mM SDS, protein denaturants or 1 mM urea do not affect enzyme activity
-
additional information
-
iodoacetate, dithiothreitol, 2-mercaptoethanol, sodium dodecyl sulfate or p-chloromercuribenzoate have no inhibitory effects
-
additional information
-
dithiothreitol or 2-mercaptoethanol in concentrations between 0.1 and 6 mM have no influence on intracellular alginate lyase
-
additional information
-
activity is lost at standard sea water salinity, restored in the presence of 1 mM calcium, activity is lost even at low salt concentrations if calcium is removed by a calcium chelator
-
additional information
activity of AlgMytC is stable in the presence of various detergents
-
additional information
-
enzymatic activity is about two times higher in phosphate buffer than in Tris buffer
-
4.2.2.11 guluronate-specific alginate lyase
results (
results (
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