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1,10-phenanthroline
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relative activity: 95%
1-cyclohexyl-3-(2-morpholinoethyl)carbodiimide metho-p-toluenesulfonate
-
reacts with Asp and Glu residues, causes a slight decrease in activity
2,4,6-Trinitrobenzene sulfonate
-
reacts with Lys residues, causes a slight decrease in activity
AgNO3
-
relative activity: 28%
AlCl3
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53% inhibition at 1 mM
BaCl2
-
28% inhibition at 1 mM
Butane-2,3-dione
-
reacts with Arg residues, causes a slight decrease in activity
CoCl2
-
relative activity: 717
CuCl2
-
97% inhibition at 1 mM
CuSO4
7% inhibition at 1 mM
ethylene glycol tetraacetic acid
-
2 mM, 23% residual activity
FeCl3
-
92% inhibition at 1 mM
FeSO4
10% inhibition at 1 mM
glutathione
-
2 mM, 23% residual activity; 77% inhibition at 2 mM
K+
-
67% residual activity at 100 mM
KCl
weak inhibition at 1 mM
Li+
1 mM, 65% of initial activity
Methyl-4-nitrobenzenesulfonate
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40% reduced activity with recombinant wild-type enzyme, no effect on mutant H192A
Methylmercury chloride
-
-
MgCl2
weak inhibition at 1 mM
MgSO4
weak inhibition at 1 mM
N-bromosuccimide
-
complete loss of activity, reacts with Trp residues
NaCl
in the presence of 0.2 M NaCl, the residual activities of isoform A9mL from pH 6 to 10 are decreased 40-75% of those observed in the absence of NaCl
NiCl2
-
33% inhibition at 1 mM
Pb2+
1 mM, 82% inhibition
Pd2+
95% inhibition at 1 mM
PMSF
-
relative activity: 95%
Tetranitromethane
-
reacts with Tyr residues, causes a slight decrease in activity
TritonX-100
1 mM, 83% of initial activity
Tween 20
1 mM, 75% of initial activity
Urea
1 mM, 86% of initial activity
ZnCl2
-
58% inhibition at 1 mM
ZnSO4
-
relative activity: 78%
(NH4)2SO4
-
96% residual activity at 1 mM
Al3+
-
1 mM, 59% residual activity
Al3+
1 mM, 83% of initial activity
Ba2+
-
-
Ba2+
-
1 mM, 72% residual activity
Ba2+
-
79% residual activity at 1 mM
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+
95% inhibition at 1 mM
Ca2+
-
2 mM, 95% residual activity; 5% inhibition at 2 mM
Ca2+
-
1 mM, 6% residual activity
Ca2+
-
1 mM, 36% residual activity
Ca2+
1 mM, 18% of initial activity
Cd2+
-
-
Cd2+
-
2 mM, 25% residual activity; 75% inhibition at 2 mM
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, 59% of initial activity
Co2+
-
1 mM, 12% residual activity
Co2+
1 mM, 50% inhibition
Co2+
isoform A9mT is inhibited by 14% at 1 mM
Co2+
1 mM, 71% of initial activity
Co2+
1 mM, about 20% of initial activity
Cu2+
-
CuCl2
Cu2+
1 mM, 65% of initial activity
Cu2+
-
1 mM, 10% residual activity
Cu2+
-
slightly inhibiting
Cu2+
1 mM, 18% inhibition
Cu2+
1 mM, 84% of initial activity
Cu2+
-
1 mM, 8% residual activity
Cu2+
1 mM, more than 95% inhibition
Cu2+
isoform A9mT is inhibited by 16% at 1 mM
Cu2+
1 mM, 71% of initial activity
Cu2+
1 mM, 81% of initial activity
EDTA
86%inhibition at 5 mM
EDTA
-
2 mM, 15% residual activity; 85% inhibition at 2 mM
EDTA
25% inhibition at 1 mM
EDTA
-
1 mM, 50% residual activity
EDTA
-
1 mM, 37% of initial activity
EDTA
-
the addition of 50 mM EDTA leads to a 3fold decrease in activity level
EDTA
-
relative activity: 48%
EDTA
-
56% residual activity at 1 mM
EDTA
-
1 mM, 48% of initial activity; 51.7% inhibition at 1 mM
EDTA
1 mM, 75% of initial activity
EDTA
-
1 mM, 8% residual activity
EDTA
-
96% inhibition at 1 mM
EDTA
1 mM, 46% of initial activity
EGTA
86% inhibition at 5 mM
EGTA
-
77% inhibition at 2 mM
EGTA
-
relative activity: 71%
Fe2+
-
2 mM, 30% residual activity; 70% inhibition at 2 mM
Fe2+
1 mM, 69% inhibition
Fe2+
-
50 mM, no residual activity; complete inhibition of all isozymes at 50 mM
Fe2+
1 mM, 68% of initial activity
Fe2+
1 mM, 70% of initial activity
Fe3+
1 mM, 88% of initial activity
Fe3+
-
1 mM, 11% residual activity
Fe3+
1 mM, 86% inhibition
Fe3+
1 mM, complete inhibition
Fe3+
-
1 mM, 60% residual activity
Hg2+
80% inhibition at 1 mM
Hg2+
-
1 mM, 96% inhibition
Hg2+
-
2 mM, 10% residual activity; 90% inhibition at 2 mM
Hg2+
-
40% inhibition at 1 mM of isozyme A1-I and A1-II
Hg2+
1 mM, 30% inhibition
Hg2+
1 mM, more than 95% inhibition
Hg2+
1 mM, 34% of initial activity
Mg2+
-
87% residual activity at 1 mM
Mg2+
1 mM, 65% of initial activity
Mn2+
28% inhibition at 1 mM
Mn2+
1 mM, 32% of initial activity
Mn2+
-
1 mM, 8% 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
-
-
N-bromosuccinimide
-
1 mM, no residual activity
Na+
-
at 1% w/v
Na+
-
59% residual activity at 900 mM
Ni2+
95% inhibition at 1 mM
Ni2+
-
2 mM, 65% residual activity; 35% inhibition at 2 mM
Ni2+
1 mM, 87% of initial activity
Ni2+
-
1 mM, 42% residual activity
Ni2+
-
67% residual activity at 1 mM
Ni2+
2 mM, 46% of initial activity
Ni2+
1 mM, 27% inhibition
Ni2+
-
1 mM, 20% residual activity
Ni2+
isoform A9mT is inhibited by 35% at 1 mM
Ni2+
1 mM, 32% of initial activity
SDS
-
-
SDS
-
35% residual activity at 1 mM
SDS
1 mM, complete inhibition
SDS
1mM, 88% of initial activity
SDS
1 mM, 94% loss of activity
SDS
strongly inhibits the enzyme activity by 90%
SDS
1 mM, 23% of initial activity
SDS
1 mM, 29% of initial activity
Sn2+
1 mM, 85% inhibition
Sn2+
-
slightly inhibiting
Sr2+
46% inhibition at 1 mM
Sr2+
-
2 mM, 70% residual activity; 30% inhibition at 2 mM
Sr2+
isoform A9mT is inhibited by 14% at 1 mM
Zn2+
-
1 mM, complete inhibition
Zn2+
1 mM ZnCl2 reduces the activity to 7.6% of the control level without Zn2+ added, 0.1 mM Zn2+ reduces the activity to 61%
Zn2+
1 mM, 91% of initial activity
Zn2+
-
1 mM, 32% residual activity
Zn2+
-
68% residual activity at 1 mM
Zn2+
-
50 mM, isoform A 10%, isoform B 14%, isoform C 12% of initial activity
Zn2+
1 mM, 21% inhibition
Zn2+
1 mM, more than 95% inhibition
Zn2+
isoform A9mT is inhibited by 19% at 1 mM
Zn2+
1 mM, 57% of initial activity
Zn2+
1 mM, 66% of initial activity
Zn2+
1 mM, 25% of initial activity
additional information
Ni2+, Co2+, and Mg2+ ions do not affect enzyme activity, dithiothreitol and 2-mercaptoethanol (5 mM each) do not affect the enzyme activity at all
-
additional information
not affected by EDTA
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additional information
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not affected by EDTA
-
additional information
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enzymatic activity is about two times higher in phosphate buffer than in Tris buffer
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additional information
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oligoalginate lyase is not affected by addition of 1 mM EDTA, GSH, 2-mercaptoethanol, iodoacetic acid, N-ethylmaleimide, and sugars at 5 mM, L-fucose, D-galactose, D-glucose, D-glucuronic acid, D-mannose, L-rhamnose, and D-xylose, no effect on oligoalginate lyase by Cu2+, Co2+, and Hg2+ at 1 mM
-
additional information
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isozymes A1-I and A1-II are not affected by addition of 1 mM EDTA, DTT, GSH, 2-mercaptoethanol, iodoacetic acid, and sugars, L-fucose, D-galactose, D-glucose, D-glucuronic acid, D-mannose, L-rhamnose, and D-xylose, no effect on isozymes A1-I and A1-II of Ca2+, Co2+, Mg2+, and Mn2+ at 1 mM
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4.2.2.3 mannuronate-specific alginate lyase
results (
results (
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